Extremozymes: unlocking potential of extreme environments for sustainable biotechnology

Abstract

Extremophiles pose challenges to microbiologists and researchers by inhabiting the environments with extreme conditions such as alkalinity, acidity, dryness, salinity, pressure and high temperature. The research on the extremophilic microbial communities such as the thermophiles, halophiles, psychrophiles and piezophiles has increased exponentially in past couple of decades as of their ability to produce an extensive range of enzymes with stability and catalytic activity under harsh conditions. These features of extremophilic enzymes make them an amazing alternative for applications in biotechnological, textile, detergent, pharmaceutical and food industries. Adding more, these enzymes serve as cornerstone for environmentally conscious and industrial sustainability. Further, advancements in omics approaches provide new insights into discovering the diversity of unculturable microbes. The multi-omics approaches provide a means to explore the extremophilic diversity, find out novel genes, enzymes and essential products with industrial relevance. Thus, the study of the extremophiles and their enzymes with potential applications is emerging in the recent years. The present review focuses on the biodiversity of extremozymes producing microbes, omics approaches for exploring these enzymes and major applications in diverse industries.

Keywords

Extremophiles / Extremozymes / Sustainability / Omics tools / Recombinant extremozymes / Biological Sciences / Microbiology

References

[1] KourD, RanaKL, KumarA, RastegariAA, YadavN, YadavANMolinaG, GuptaVK, SinghBN, GathergoodN. Gupta VK Extremophiles for hydrolytic enzymes productions: biodiversity and potential biotechnological applications. Bioprocessing for biomolecules production, 2019USAWiley321-372

[2] RampelottoPH. Extremophiles and Extreme Environments. Life, 2013, 33482-485

[3] MerinoN, AronsonHS, BojanovaDP, Feyhl-BuskaJ, WongML, ZhangS, et al. . Living at the extremes: extremophiles and the limits of life in a planetary context. Front Microbiol, 2019, 10: 780

[4] AroraNK, PanosyanH. Extremophiles: applications and roles in environmental sustainability. Environ Sustain, 2019, 23217-218

[5] ReedCJ, LewisH, TrejoE, WinstonV, EviliaC. Protein adaptations in archaeal extremophiles. Archaea, 2013, 20131373275

[6] RaddadiN, CherifA, DaffonchioD, NeifarM, FavaF. Biotechnological applications of extremophiles, extremozymes and extremolytes. Appl Microbiol Biotechnol, 2015, 99197907-7913

[7] Demirjian DC, Morı́s-Varas F, Cassidy CS. Enzymes from extremophiles. Curr Opin Chem Biol. 2001;5(2):144–51.

[8] LittlechildJA. Enzymes from extreme environments and their industrial applications. Front Bioeng Biotechnol, 2015, 3: 161

[9] Bhalla A, Bischoff KM, Uppugundla N, Balan V, Sani RK. Novel thermostable endo-xylanase cloned and expressed from bacterium Geobacillus sp. WSUCF1. Bioresour Technol. 2014;165:314–8.

[10] KumarS, NussinovR. How do thermophilic proteins deal with heat?. Cellular and Molecular Life Sciences CMLS, 2001, 5891216-1233

[11] GomesE, de SouzaAR, OrjuelaGL, Da SilvaR, de OliveiraTB, RodriguesASchmollM, DattenböckC. Applications and benefits of thermophilic microorganisms and their enzymes for industrial biotechnology. Gene expression systems in fungi: Advancements and applications, 2016ChamSpringer International Publishing459-492

[12] Kumari M, Padhi S, Sharma S, Phukon LC, Singh SP, Rai AK. Biotechnological potential of psychrophilic microorganisms as the source of cold-active enzymes in food processing applications. 3Biotech. 2021;11(11):479.

[13] Sarethy IP, Saxena Y, Kapoor A, Sharma M, Sharma SK, Gupta V, et al. Alkaliphilic bacteria: applications in industrial biotechnology. J Ind Microbiol Biotechnol. 2011;38(7):769-.

[14] KumarS, KaranR, KapoorS, SinghS, KhareS. Screening and isolation of halophilic bacteria producing industrially important enzymes. Brazilian J Microbiol, 2012, 43: 1595-1603

[15] SharmaA, ParasharD, SatyanarayanaTRampelottoPH. Acidophilic Microbes: Biology and applications. Biotechnology of extremophiles: Advances and challenges, 2016ChamSpringer International Publishing215-241

[16] Samanta D, Govil T, Saxena P, Thakur P, Narayanan A, Sani RK. Chapter 1 - Extremozymes and their applications. In: Arora NK, Agnihotri S, Mishra J, (eds). Extremozymes and Their Industrial Applications: Academic Press; 2022. p. 1–39.

[17] SysoevM, GrötzingerSW, RennD, EppingerJ, RuepingM, KaranR. Bioprospecting of novel extremozymes from prokaryotes—The advent of culture-independent methods. Front Microbiol, 2021, 12630013

[18] EspinaG, Muñoz-IbacacheSA, Cáceres-MorenoP, AmenabarMJ, BlameyJM. From the discovery of Extremozymes to an enzymatic product: roadmap based on their applications. Front Bioeng Biotechnol, 2022, 9752281

[19] ZhangY, AnJ, YangG, ZhangX, XieY, ChenL, et al. . Structure features of GH10 xylanase from Caldicellulosiruptor bescii: implication for its thermophilic adaption and substrate binding preference. Acta Biochim et Biophysica Sinica, 2016, 4810948-957

[20] GhumroPB, ShafiqueM, AliMI, JavedI, AhmadB, JamalA, et al. . Isolation and screening of protease producing thermophilic Bacillus strains from different soil types of Pakistan. African J Microbiol Res, 2011, 5315534-5539

[21] Das A, Bhattacharya S, Murali L. Production of cellulase from a thermophilic Bacillus sp. isolated from cow dung. AM Eurasian J Agric Environ Sci. 2010;8:685–91.

[22] OmidiniaE. Isolation, purification and characterization of a thermophilic alkaline protease from Bacillus subtilis BP-36. J Sci Islamic Republic Iran, 2012, 2317-13

[23] KhalilA. Isolation and characterization of three thermophilic bacterial strains (lipase, cellulose and amylase producers) from hot springs in Saudi Arabia. African J Biotechnol, 2011, 10448834-8839

[24] MehtaA, KumarR, GuptaR. Isolation of lipase producing thermophilic bacteria: Optimization of production and reaction conditions for lipase from Geobacillus sp. Acta Microbiol et Immunol Hungarica, 2012, 594435-450

[25] Panda MK, Sahu MK, Tayung K. Isolation and characterization of a thermophilic Bacillus sp. with protease activity isolated from hot spring of Tarabalo, Odisha, India. Iran J Microbiol. 2013;5(2):159–65.

[26] PandeyS, SinghS, YadavAN, NainL, SaxenaAK. Phylogenetic diversity and characterization of novel and efficient cellulase producing bacterial isolates from various extreme environments. Biosci Biotechnol Biochem, 2013, 7771474-1480

[27] HusseinAA, KhudhairSH, MohammedMK. Isolation and screening of thermophilic bacteria for producing cellulase enzyme using agricultural waste. Al-Nahrain J Sci, 2017, 202103-107

[28] AlrummanS, MostafaYSM, Al-QahtaniS, TahaTHT. Hydrolytic enzyme production by thermophilic bacteria isolated from Saudi hot springs. Open Life Sci, 2018, 131470-480

[29] YasarG, GulhanUG, GudukE, AktasF. Screening, partial purification and characterization of the hyper-thermophilic lipase produced by a new isolate of Bacillus subtilis LP2. Biocatal Biotransform, 2020, 385367-375

[30] SarangthemI, RajkumariL, NgashangvaN, NandeibamJ, YendrembamRBS, MukherjeePK. Isolation and characterization of Bacteria from Natural Hot Spring and Insights into the Thermophilic Cellulase Production. Curr Microbiol, 2023, 80264

[31] ValenzuelaB, Solís-CornejoF, ArayaR, ZamoranoP. Isolation of Thermophilic Bacteria from Extreme Environments in Northern Chile. Microorganisms, 2024, 123473

[32] GutaM, AbebeG, BachaK, CoolsP. Screening and characterization of thermostable enzyme-producing bacteria from selected hot springs of Ethiopia. Microbiol Spectr, 2024, 123e03710-e3723

[33] FellerG, GerdayC. Psychrophilic enzymes: hot topics in cold adaptation. Nat RevMicrobiol, 2003, 13200-208

[34] SiddiquiKS, WilliamsTJ, WilkinsD, YauS, AllenMA, BrownMV, et al. Psychrophiles Ann Rev Earth Planetary Sci, 2013, 41: 87-115

[35] JeonJH, KimJ-T, KangSG, LeeJ-H, KimS-J. Characterization and its potential application of two esterases derived from the arctic sediment metagenome. Marine Biotechnol, 2009, 11: 307-316

[36] NakagawaT, NagaokaT, TaniguchiS, MiyajiT, TomizukaN. Isolation and characterization of psychrophilic yeasts producing cold-adapted pectinolytic enzymes. Lett Appl Microbiol, 2004, 385383-387

[37] LoperenaL, SoriaV, VarelaH, LupoS, BergalliA, GuigouM, et al. . Extracellular enzymes produced by microorganisms isolated from maritime Antarctica. World J Microbiol Biotechnol, 2012, 2852249-2256

[38] GuptaG, PrakashV. Isolation and identification of a novel, cold active lipase producing psychrophilic bacterium Pseudomonas vancouverensis. Trends Biosci, 2014, 7223708-3711

[39] DivyaK, PadmaPN. Psychrophilic yeast isolates for cold-active lipase production. Int J Sci Prog Res, 2015, 10: 93-97

[40] YadavAN, SachanSG, VermaP, KaushikR, SaxenaAK. Cold active hydrolytic enzymes production by psychrotrophic Bacilli isolated from three sub-glacial lakes of NW Indian Himalayas. J Basic Microbiol, 2016, 563294-307

[41] Salwoom L, Raja Abd Rahman RNZ, Salleh AB, Mohd. Shariff F, Convey P, Pearce D, et al. Isolation, characterisation, and lipase production of a cold-adapted bacterial strain Pseudomonas sp. LSK25 isolated from Signy Island, Antarctica. Molecules. 2019;24(4):715.

[42] Sun S, Zhang Y, Liu K, Chen X, Jiang C, Huang M, et al. Insight into biodegradation of cellulose by psychrotrophic bacterium Pseudomonas sp. LKR-1 from the cold region of China: optimization of cold-active cellulase production and the associated degradation pathways. Cellulose. 2020;27(1):315–33.

[43] Li D, Feng L, Liu K, Cheng Y, Hou N, Li C. Optimization of cold-active CMCase production by psychrotrophic Sphingomonas sp. FLX-7 from the cold region of China. Cellulose.2016; 23(2):1335–47.

[44] Sivasankar P, Poongodi S, Sivakumar K., Al-Qahtani WH, Arokiyaraj S, Jothiramalingam R. Exogenous production of cold-active cellulase from polar Nocardiopsis sp. with increased cellulose hydrolysis efficiency. Arch Microbiol. 2022; 204–218. https://doi.org/10.1007/s00203-022-02830-z

[45] Abdella B, Youssif AM, Sabry SA, Ghozlan HA. Production, purification, and characterization of cold-active lipase from the psychrotroph Pseudomonas sp. A6. Brazilian J Microbiol. 2023;54(3):1623–33. https://link.springer.com/article/https://doi.org/10.1007/s42770-023-01079-y

[46] DasSarma S, Arora P. Halophiles. e LS. 2001.

[47] Wang C-Y, Hsieh Y-R, Ng C-C, Chan H, Lin H-T, Tzeng W-S, et al. Purification and characterization of a novel halostable cellulase from Salinivibrio sp. strain NTU-05. Enzyme Microbial Technol. 2009;44(6):373–9.

[48] de Lourdes Moreno M, García MT, Ventosa A, Mellado E. Characterization of Salicola sp. IC10, a lipase- and protease-producing extreme halophile. FEMS Microbiol Ecol. 2009;68(1):59–71. https://doi.org/10.1111/j.1574-6941.2009.00651.x

[49] Karbalaei-HeidariHR, AmoozegarMA, HajighasemiM, ZiaeeA-A, VentosaA. Production, optimization and purification of a novel extracellular protease from the moderately halophilic bacterium Halobacillus karajensis. J Indust Microbiol Biotechnol, 2009, 36121-27.

[50] GhasemiY, Rasoul-AminiS, KazemiA, ZarriniG, MorowvatMH, KargarM. Isolation and characterization of some moderately halophilic bacteria with lipase activity. Microbiology, 2011, 804483-487

[51] Li X, Wang H-L, Li T, Yu H-Y. Purification and characterization of an organic solvent-tolerant alkaline cellulase from a halophilic isolate of Thalassobacillus. Biotechnol Lett. 2012;34(8):1531–6. https://link.springer.com/article/https://doi.org/10.1007/s10529-012-0938-z

[52] Yu H-Y, Li X. Alkali-stable cellulase from a halophilic isolate, Gracilibacillus sp. SK1 and its application in lignocellulosic saccharification for ethanol production. Biomass Bioenergy. 2015;81:19–25.

[53] Gutiérrez-ArnillasE, RodríguezA, SanrománMA, DeiveFJ. New sources of halophilic lipases: Isolation of bacteria from Spanish and Turkish saltworks. Biochem Engineer J, 2016, 109: 170-177

[54] Korany AH, Ali AE, Essam TM, Megahed SA. Optimization of cellulase production by Halobacillus sp. QLS 31 isolated from Lake Qarun, Egypt. Appl Biochem Biotechnol. 2017;183(1):189–99. https://link.springer.com/article/https://doi.org/10.1007/s12010-017-2438-z

[55] Ai L, Huang Y, Wang C. Purification and characterization of halophilic lipase of Chromohalobacter sp. from ancient salt well. J Basic Microbiol. 2018;58(8):647–57. https://doi.org/10.1002/jobm.201800116

[56] BanoA, ChenX, PrasongsukS, AkbarA, LotrakulP, PunnapayakH, et al. . Purification and Characterization of Cellulase from Obligate Halophilic Aspergillus flavus (TISTR 3637) and Its Prospects for Bioethanol Production. Appl Biochem Biotechnol, 2019, 18941327-1337

[57] YousefNMH, MawadAMM. Characterization of thermo/halo stable cellulase produced from halophilic Virgibacillus salarius BM-02 using non-pretreated biomass. World J Microbiol Biotechnol, 2022, 39122

[58] HorikoshiK. Alkaliphiles. Proceedings of the Japan Academy, Series B, 2004, 804166-178

[59] Kulkarni S, Dhakar K, Joshi A. Alkaliphiles: Diversity and Bioprospection. In: Das S and Dash HR (eds). Microbial Diversity in the Genomic Era: Academic Press; 2019. p. 239–63.

[60] FujinamiS, FujisawaM. Industrial applications of alkaliphiles and their enzymes – past, present and future. Environ Technol, 2010, 318–9845-856

[61] Vasundhara M, Singh K, Suryanarayanan TS, Reddy MS. Alkaliphilic and thermostable lipase production by leaf litter fungus Leptosphaerulina trifolii A SMR-2011. Arch Microbiol. 2024;206(6):264. https://link.springer.com/article/https://doi.org/10.1007/s00203-024-03997-3

[62] Oluoch KR. Characterization of an alkaline amylase and a pectinase from alkaliphilic Bacillus halodurans Lbw 5117 Isolated from Lake Bogoria in Kenya and demonstration of their applications in bio-processing woven cotton: University of Nairobi; 2023.

[63] Ibrahim ASS, Elbadawi YB, El-Tayeb MA, Al-maary KS, Maany DAF, Ibrahim SSS, et al. Alkaline serine protease from the new halotolerant alkaliphilic Salipaludibacillus agaradhaerens strain AK-R: purification and properties. 3 Biotech. 2019;9(11):391. https://link.springer.com/article/https://doi.org/10.1007/s13205-019-1928-9

[64] Zhou C, Qin H, Chen X, Zhang Y, Xue Y, Ma Y. A novel alkaline protease from alkaliphilic Idiomarina sp. C9–1 with potential application for eco-friendly enzymatic dehairing in the leather industry. Sci Rep. 2018;8(1):16467.

[65] Ibrahim ASS, Al-Salamah AA, El-Badawi YB, El-Tayeb MA, Antranikian G. Detergent-, solvent- and salt-compatible thermoactive alkaline serine protease from halotolerant alkaliphilic Bacillus sp. NPST-AK15: purification and characterization. Extremophiles. 2015;19(5):961–71. https://link.springer.com/article/https://doi.org/10.1007/s00792-015-0771-0

[66] Aygan A, Arikan B, Korkmaz H, Dinçer S, Çolak Ö. Highly thermostable and alkaline α-amylase from a halotolerant-alkaliphilic Bacillus sp. AB68. Brazilian J Microbiol. 2008;39:547–53.

[67] Ma Y, Xue Y, Dou Y, Xu Z, Tao W, Zhou P. Characterization and gene cloning of a novel β-mannanase from alkaliphilic Bacillus sp. N16–5. Extremophiles. 2004;8(6):447–54.

[68] Burhan A, Nisa U, Gökhan C, Ömer C, Ashabil A, Osman G. Enzymatic properties of a novel thermostable, thermophilic, alkaline and chelator resistant amylase from an alkaliphilic Bacillus sp. isolate ANT-6. Process Biochem. 2003;38(10):1397–403. https://doi.org/10.1016/S0032-9592(03)00037-2

[69] Endo K, Hakamada Y, Takizawa S, Kubota H, Sumitomo N, Kobayashi T, et al. A novel alkaline endoglucanase from an alkaliphilic Bacillus isolate: enzymatic properties, and nucleotide and deduced amino acid sequences. Appl Microbiol Biotechnol. 2001;57(1):109–16. https://link.springer.com/article/https://doi.org/10.1007/s002530100744

[70] KobayashiT, HatadaY, HigakiN, LusterioDD, OzawaT, KoikeK, et al. . Enzymatic properties and deduced amino acid sequence of a high-alkaline pectate lyase from an alkaliphilic Bacillus isolate. Biochimica et Biophysica Acta (BBA), 1999, 14272145-154

[71] VivekK, SandhiaGS, SubramaniyanS. Extremophilic lipases for industrial applications: A general review. Biotechnol Adv, 2022, 60108002

[72] Sharma A, Kawarabayasi Y, Satyanarayana T. Acidophilic bacteria and archaea: acid stable biocatalysts and their potential applications. Extremophiles. 2012;16(1):1–19. https://link.springer.com/article/https://doi.org/10.1007/s00792-011-0402-3

[73] MatzkeJ, SchwermannB, BakkerEP. Acidostable and acidophilic proteins: The example of the α-amylase from Alicyclobacillus acidocaldarius. Comparative Biochem Physiol Part A: Physiol, 1997, 1183475-479

[74] BeenaP, SoorejM, ElyasK, SaritaGB, ChandrasekaranM. Acidophilic tannase from marine Aspergillus awamori BTMFW032. J Microbiol Biotechnol, 2010, 20101403-1414

[75] Asoodeh A, Chamani J, Lagzian M. A novel thermostable, acidophilic α-amylase from a new thermophilic “Bacillus sp. Ferdowsicous” isolated from Ferdows hot mineral spring in Iran: Purification and biochemical characterization. Int J Biol Macromol. 2010;46(3):289–97. https://doi.org/10.1016/j.ijbiomac.2010.01.013

[76] LiaoH, XuC, TanS, WeiZ, LingN, YuG, et al. . Production and characterization of acidophilic xylanolytic enzymes from Penicillium oxalicum GZ-2. Bioresour Technol, 2012, 123: 117-124

[77] Asoodeh A, Alemi A, Heydari A, Akbari J. Purification and biochemical characterization of an acidophilic amylase from a newly isolated Bacillus sp. DR90. Extremophiles. 2013;17(2):339–48. https://link.springer.com/article/https://doi.org/10.1007/s00792-013-0520-1

[78] OkerekeOE, AkanyaHO, EgwimEC. Purification and characterization of an acidophilic cellulase from Pleurotus ostreatus and its potential for agrowastes valorization. Biocatal Agric Biotechnol, 2017, 12: 253-259.

[79] Somayaji A, Dhanjal CR, Lingamsetty R, Vinayagam R, Selvaraj R, Varadavenkatesan T, et al. An insight into the mechanisms of homeostasis in extremophiles. Microbiol Res. 2022:127115. https://doi.org/10.1016/j.micres.2022.127115

[80] Aatif M, Rahman S, Bano B. Protein unfolding studies of thiol-proteinase inhibitor from goat (Capra hircus) muscle in the presence of urea and GdnHCl as denaturants. European Biophys J. 2011;40:611–7. https://link.springer.com/article/https://doi.org/10.1007/s00249-010-0658-z

[81] AngelinJ, KavithaMMolecular mechanisms behind the cold and hot adaptation in extremozymes, 2022Extremozymes and their industrial applicationsElsevier141-176

[82] WangQ, CenZ, ZhaoJ. The survival mechanisms of thermophiles at high temperatures: An angle of omics. Physiology, 2015, 30297-106

[83] Collins T, Margesin R. Psychrophilic lifestyles: mechanisms of adaptation and biotechnological tools. Appl Microbiol Biotechnol. 2019;103:2857–71. https://link.springer.com/article/https://doi.org/10.1007/s00253-019-09659-5

[84] CavicchioliR, CharltonT, ErtanH, OmarSM, SiddiquiK, WilliamsT. Biotechnological uses of enzymes from psychrophiles. Microbial Biotechnol, 2011, 44449-460

[85] FellerG. Protein stability and enzyme activity at extreme biological temperatures. J Phys: Condens Matter, 2010, 2232323101

[86] MarasB, ValianteS, ChiaraluceR, ConsalviV, PolitiL, De RosaM, et al. . The amino acid sequence of glutamate dehydrogenase from Pyrococcus furiosus, a hyperthermophilic archaebacterium. J Protein Chem, 1994, 132253-259

[87] SarmientoF, PeraltaR, BlameyJM. Cold and hot extremozymes: Industrial relevance and current trends. Front Bioeng Biotechnol, 2015, 3: 148

[88] Kulkarni S, Dhakar K, Joshi A. Alkaliphiles: diversity and bioprospection. Microbial diversity in the genomic era: Elsevier; 2019. p. 239–63.

[89] XiY, YeL, YuH. Enhanced thermal and alkaline stability of L-lysine decarboxylase CadA by combining directed evolution and computation-guided virtual screening. Bioresour Bioprocess, 2022, 911-15

[90] ShiraiT, SuzukiA, YamaneT, AshidaT, KobayashiT, HitomiJ, et al. . High-resolution crystal structure of M-protease: phylogeny aided analysis of the high-alkaline adaptation mechanism. Protein Eng, 1997, 106627-634

[91] FujinamiS, FujisawaM. Industrial applications of alkaliphiles and their enzymes–past, present and future. Environ Technol, 2010, 318–9845-856

[92] Coker JA. Extremophiles and biotechnology: current uses and prospects. F1000Research. 2016;5.

[93] Delgado-GarcíaM, Valdivia-UrdialesB, Aguilar-GonzálezCN, Contreras-EsquivelJC, Rodríguez-HerreraR. Halophilic hydrolases as a new tool for the biotechnological industries. J Sci Food Agri, 2012, 92132575-2580

[94] Dumorné K, Córdova DC, Astorga-Eló M, Renganathan P. Extremozymes: a potential source for industrial applications. 2017.

[95] KaranR, CapesMD, DasSarmaS. Function and biotechnology of extremophilic enzymes in low water activity. Aquatic Biosyst, 2012, 814

[96] GrötzingerSW, KaranR, StrillingerE, BaderS, FrankA, Al RowaihiIS, et al. . Identification and experimental characterization of an extremophilic brine pool alcohol dehydrogenase from single amplified genomes. ACS Chem Biol, 2018, 131161-170

[97] KaranR, MathewS, MuhammadR, BautistaDB, VoglerM, EppingerJ, et al. . Understanding high-salt and cold adaptation of a polyextremophilic enzyme. Microorganisms, 2020, 8101594

[98] MaY, GalinskiEA, GrantWD, OrenA, VentosaA. Halophiles 2010: life in saline environments. Appl Environ Microbiol, 2010, 76216971-6981

[99] JinM, GaiY, GuoX, HouY, ZengR. Properties and Applications of Extremozymes from Deep-Sea Extremophilic Microorganisms: A Mini Review. Mar Drugs, 2019, 1712656

[100] Kikani B, Patel R, Thumar J, Bhatt H, Rathore DS, Koladiya GA, et al. Solvent tolerant enzymes in extremophiles: Adaptations and applications. Int J Biol Macromolecules. 2023:124051.

[101] Kumar A, Mukhia S, Kumar R. Industrial applications of cold-adapted enzymes: Challenges, innovations and future perspective. 3 Biotech. 2021;11:1–18.

[102] TangY, WuP, JiangS, SelvarajJN, YangS, ZhangG. A new cold-active and alkaline pectate lyase from Antarctic bacterium with high catalytic efficiency. Appl Microbiol Biotechnol, 2019, 103: 5231-5241

[103] Salwan R, Sharma V. Physiological and biotechnological aspects of extremophiles: Academic Press; 2020.

[104] Cira-Chávez LA, Guevara-Luna J, Soto-Padilla MY, Román-Ponce B, Vásquez-Murrieta MS, Estrada-Alvarado MI. Kinetics of halophilic enzymes. Kinetics Enzymatic Synthesis. 2018:3–26.

[105] AbeF. Exploration of the effects of high hydrostatic pressure on microbial growth, physiology and survival: perspectives from piezophysiology. Biosci Biotechnol Biochem, 2007, 71102347-2357

[106] RaoAS, NairA, NivethaK, MoreVS, AnantharajuK, MoreSSMolecular adaptations in proteins and enzymes produced by extremophilic microorganisms, 2022Extremozymes and Their Industrial ApplicationsElsevier205-230

[107] Sarma J, Sengupta A, Laskar MK, Sengupta S, Tenguria S, Kumar A. Microbial adaptations in extreme environmental conditions. Bacterial Survival in the Hostile Environment: Elsevier; 2023. pp 193–206.

[108] ValentineRC, ValentineDL. Omega-3 fatty acids in cellular membranes: a unified concept. Progress Lipid Res, 2004, 435383-402

[109] KohliI, JoshiNC, MohapatraS, VarmaA. Extremophile–an adaptive strategy for extreme conditions and applications. Curr Genom, 2020, 21296-110

[110] ChatterjeeA, PuriS, SharmaPK, DeepaP, ChowdhuryS. Nature-inspired Enzyme engineering and sustainable catalysis: biochemical clues from the world of plants and extremophiles. Front Bioengin Biotechnol, 2023, 11: 1229300

[111] JacobsenEN, FinneyNS. Synthetic and biological catalysts in chemical synthesis: how to assess practical utility. Chem Biol, 1994, 1285-90

[112] BashkinJK. Hydrolysis of phosphates, esters and related substrates by models of biological catalysts. Curr Opin Cheml Biol, 1999, 36752-758

[113] Vasudevan N, Jayshree A. Extremozymes and extremoproteins in biosensor applications. In: Kim S-K, editor. Encyclopedia of Marine Biotechnology. 3. Hoboken, NJ, USA,: John Wiley & Sons Ltd.; 2020. pp 1711–36.

[114] HussainI, AletiG, NaiduR, PuschenreiterM, MahmoodQ, RahmanMM, et al. . Microbe and plant assisted-remediation of organic xenobiotics and its enhancement by genetically modified organisms and recombinant technology: a review. Sci Total Environ, 2018, 628: 1582-1599

[115] SamantaD, GovilT, SaxenaP, ThakurP, NarayananA, SaniRKAroraNK, AgnihotriS, MishraJ. Extremozymes and their applications. Extremozymes and their industrial applications, 2022Cambridge, MA, USAElsevier1-39

[116] BukhariDA, BibiZ, UllahA, RehmanA. Isolation, characterization, and cloning of thermostable pullulanase from Geobacillus stearothermophilus ADM-11. Saudi J Biol Sci, 2024, 312103901

[117] Zhao Y, Liu Y, Fu Q, Zhou Y, Qin R, Xiong H, et al. Domain analysis and site-directed mutagenesis of a thermophilic pullulanase from Thermotoga maritima MSB8. 2023.

[118] WuH, YuX, ChenL, WuG. Cloning, overexpression and characterization of a thermostable pullulanase from Thermus thermophilus HB27. Protein Expr Purif, 2014, 95: 22-27

[119] GomesI, GomesJ, SteinerW. Highly thermostable amylase and pullulanase of the extreme thermophilic eubacterium Rhodothermus marinus: production and partial characterization. Bioresour Technol, 2003, 902207-214

[120] Kashiwabara S-i, Ogawa S, Miyoshi N, Oda M, Suzuki Y. Three domains comprised in thermostable molecular weight 54,000 pullulanase of type I from Bacillus flavocaldarius KP1228. Biosci Biotechnol Biochem. 1999;63(10):1736–48. https://doi.org/10.1271/bbb.63.1736

[121] SahaB, MathupalaS, ZeikusJ. Purification and characterization of a highly thermostable novel pullulanase from Clostridium thermohydrosulfuricum. Biochemic J, 1988, 2522343-348

[122] FangY, LiuF, ShiY, YangT, XinY, GuZ, et al. . N-terminal lid swapping contributes to the substrate specificity and activity of thermophilic lipase TrLipE. Front Microbiol, 2023, 14: 1193955

[123] SürmeliY, TekedarHC, Şanlı-MohamedG. Sequence identification and in silico characterization of novel thermophilic lipases from Geobacillus species. Biotechnol Appl Biochem, 2024, 711162-175.

[124] AtanasovaN, Paunova-KrastevaT, KambourovaM, BoyadzhievaI. A thermostable lipase isolated from Brevibacillus thermoruber strain 7 degrades Ɛ-Polycaprolactone. Biotech, 2023, 12123

[125] NajmTA, WalshMK, ParkN. Different substrate selectivity and product patterns of immobilized thermophilic lipases from Geobacillus stearothermophilus, Anoxybacillus flavithermus, and Thermomyces lanuginosus for Glyceryl Decanoate Synthesis. Chem Engineer, 2024, 8112.

[126] HuG, LuoJ, BaoT, HuX, YangJ, ZhangH. Rational design of disulfide bonds to improve the thermostability and γ-cyclodextrin production capacity of γ-cyclodextrin glycosyltransferase. Process Biochem, 2024.

[127] ChungH-J, YoonS-H, LeeM-J, KimM-J, KweonK-S, LeeI-W, et al. . Characterization of a Thermostable Cyclodextrin Glucanotransferase Isolated from Bacillus s tearothermophilus ET1. J Agric Food Chem, 1998, 463952-959

[128] Lee M-H, Yang S-J, Kim J-W, Lee H-S, Kim J-W, Park K-H. Characterization of a thermostable cyclodextrin glucanotransferase from Pyrococcus furiosus DSM3638. Extremophiles. 2007;11:537–41. https://link.springer.com/article/https://doi.org/10.1007/s00792-007-0061-6

[129] Theriot CM, Tove SR, Grunden AM. Characterization of two proline dipeptidases (prolidases) from the hyperthermophilic archaeon Pyrococcus horikoshii. Appl Microbiol Biotechnol. 2010;86:177–88. https://link.springer.com/article/https://doi.org/10.1007/s00253-009-2235-x

[130] GhoshM, GrundenAM, DunnDM, WeissR, AdamsMW. Characterization of native and recombinant forms of an unusual cobalt-dependent proline dipeptidase (prolidase) from the hyperthermophilic archaeon Pyrococcus furiosus. J Bacteriol, 1998, 180184781-4789

[131] ZhuY, LiJ, CaiH, NiH, XiaoA, HouL. Characterization of a new and thermostable esterase from a metagenomic library. Microbiol Res, 2013, 1689589-597.

[132] Kim S-B, Lee W, Ryu Y-W. Cloning and characterization of thermostable esterase from Archaeoglobus fulgidus. J Microbiol. 2008;46:100–7. https://link.springer.com/article/https://doi.org/10.1007/s12275-007-0185-5

[133] ParryN, BeeverD, OwenE, NerinckxW, ClaeyssensM, Van BeeumenJ, et al. . Biochemical characterization and mode of action of a thermostable endoglucanase purified from Thermoascus aurantiacus. Arch Biochem Biophys, 2002, 4042243-253

[134] Gomes I, Gomes J, Gomes D, Steiner W. Simultaneous production of high activities of thermostable endoglucanase and β-glucosidase by the wild thermophilic fungus Thermoascus aurantiacus. Appl Microbiol Biotechnol. 2000;53:461–8. https://link.springer.com/article/https://doi.org/10.1007/s002530051642

[135] NarangS, SatyanarayanaT. Thermostable α-amylase production by an extreme thermophile Bacillus thermooleovorans. Lett Appl Microbiol, 2001, 32131-35

[136] Dheeran P, Kumar S. Extremophiles: General and Plant Biomass Based Biorefinery: CRC Press; 2022.

[137] Mutlu-Ingok A, Kahveci D, Karbancioglu-Guler F, Ozcelik B. Applications of extremozymes in the food industry. Microbial Extremozymes. 2022:197–206. https://doi.org/10.1016/B978-0-12-822945-3.00012-9

[138] AdapaV, RamyaL, PulicherlaKCold-active enzymes: Enabling nonthermal processing in food industry, 2022Microbial ExtremozymesElsevier39-53

[139] KhanM, SathyaT. Extremozymes from metagenome: Potential applications in food processing. Crit Rev Food Sci Nutr, 2018, 58122017-2025.

[140] Cáceres-MorenoP, Muñoz-IbacacheSA, MonsalvesMT, AmenabarMJ, BlameyJMFunctional approach for the development and production of novel extreme biocatalysts, 2019Next Generation Biomanufacturing TechnologiesACS Publications1-22

[141] Bhatt BM, Trivedi UB, Patel KC. Extremophilic amylases: Microbial production and applications. In: Arora N, Mishra J, Mishra V (eds) Microbial enzymes: Roles and applications in industries. Springer, Singapore 2020; pp 185–205. https://doi.org/10.1007/978-981-15-1710-5_7

[142] Al-MaqtariQA, WaleedA, MahdiAA. Cold-active enzymes and their applications in industrial fields-A review. Int J Res Agric Sci, 2019, 642348-3997

[143] Hamid B, Mohiddin FA. Cold-active enzymes in food processing. In: Kuddus M (eds)Enzymes in Food Technology: Improvements and Innovations. Springer, Singapore 2018:383–400. . https://doi.org/10.1007/978-981-13-1933-4_19

[144] SanchezAC, RavanalMC, AndrewsBA, AsenjoJA. Heterologous expression and biochemical characterization of a novel cold-active α-amylase from the Antarctic bacteria Pseudoalteromonas sp. Protein Expr Purif, 2019, 155: 78-85.

[145] López-GutiérrezI, Razo-FloresE, Mendez-AcostaHO, Amaya-DelgadoL, Alatriste-MondragónF. Optimization by response surface methodology of the enzymatic hydrolysis of non-pretreated agave bagasse with binary mixtures of commercial enzymatic preparations. Biomass Convers Biorefin, 2021, 11: 2923-2935

[146] YeginS, AltinelB, TulukK. A novel extremophilic xylanase produced on wheat bran from Aureobasidium pullulans NRRL Y-2311-1: Effects on dough rheology and bread quality. Food Hydrocoll, 2018, 81: 389-397

[147] NieterA, KelleS, LinkeD, BergerRG. A p-coumaroyl esterase from Rhizoctonia solani with a pronounced chlorogenic acid esterase activity. New Biotechnol, 2017, 37: 153-161

[148] SunQ, ChenF, GengF, LuoY, GongS, JiangZ. A novel aspartic protease from Rhizomucor miehei expressed in Pichia pastoris and its application on meat tenderization and preparation of turtle peptides. Food Chem, 2018, 245: 570-577

[149] Kaur H, Gill PK. Microbial enzymes in food and beverages processing. In Grumezescu AM and Holban AM (eds) Engineering tools in the beverage industry: Elsevier; 2019. pp 255–82. https://doi.org/10.1016/B978-0-12-815258-4.00009-3

[150] Fernández-Sanromán Á, Sanromán M. Value-Addition in food products and processing through enzyme Technology. Elsevier Amsterdam, The Netherlands:; 2022.

[151] EspinaG, AtalahJ, BlameyJM. Extremophilic oxidoreductases for the industry: five successful examples with promising projections. Front Bioeng Biotechnol, 2021, 9710035

[152] MesbahNM. Industrial biotechnology based on enzymes from extreme environments. Front Bioeng Biotechnol, 2022, 10870083

[153] FurhanJ, AwasthiP, SharmaS. Biochemical characterization and homology modelling of cold-active alkophilic protease from Northwestern Himalayas and its application in detergent industry. Biocatal Agri Biotechnol, 2019, 17: 726-735

[154] KakkarP, WadhwaN. Extremozymes used in textile industry. J Textile Inst, 2022, 11392007-2015

[155] ArabacıN, ArıkanB. Isolation and characterization of a cold-active, alkaline, detergent stable α-amylase from a novel bacterium Bacillus subtilis N8. Prep Biochem Biotechnol, 2018, 485419-426

[156] LuZ, HuX, ShenP, WangQ, ZhouY, ZhangG, et al. . A pH-stable, detergent and chelator resistant type I pullulanase from Bacillus pseudofirmus 703 with high catalytic efficiency. Int J Biol Macromol, 2018, 109: 1302-1310

[157] SchultzJ, RosadoAS. Extreme environments: a source of biosurfactants for biotechnological applications. Extremophiles, 2020, 24: 189-206

[158] Mokashe N, Chaudhari B, Patil U. Detergent-compatible robust alkaline protease from newly isolated halotolerant Salinicoccus sp. UN-12. J Surfactants Deterg. 2017;20:1377–93.

[159] Chen K, Mo Q, Liu H, Yuan F, Chai H, Lu F, et al. Identification and characterization of a novel cold-tolerant extracellular protease from Planococcus sp. CGMCC 8088. Extremophiles. 2018;22:473–84.

[160] IbrahimM, AdamsC, El-ZaartA. Paving the way to smart sustainable cities: Transformation models and challenges. J Inform Syst Technol Manag, 2015, 12: 559-576

[161] TrudgeonB, DieserM, BalasubramanianN, MessmerM, ForemanCMLow-temperature biosurfactants from polar microbes Microorganisms, 2020, 881183

[162] Arora NK, Agnihotri S, Mishra J. Extremozymes and their industrial applications: Academic Press; 2022.

[163] NiyonzimaFN. Detergent-compatible bacterial cellulases. J Basic Microbiol, 2019, 592134-147.

[164] Kuddus M. Microbial extremozymes: novel sources and industrial applications: Academic Press; 2021.

[165] MonsalvesMT, Ollivet-BessonGP, AmenabarMJ, BlameyJM. Isolation of a psychrotolerant and UV-C-resistant bacterium from elephant island, antarctica with a highly thermoactive and thermostable catalase. Microorganisms, 2020, 8195.

[166] OzturkE, KoseogluH, KaraboyaciM, YigitNO, YetisU, KitisM. Sustainable textile production: cleaner production assessment/eco-efficiency analysis study in a textile mill. J Clean Prod, 2016, 138: 248-263

[167] MadhuA, ChakrabortyJN. Developments in application of enzymes for textile processing. J Clean Prod, 2017, 145: 114-133

[168] Nadaroglu H, Polat MS. Microbial extremozymes: Novel sources and industrial applications. In Kuddus M (ed) Microbial Extremozymes: Elsevier; 2022. pp 67–88. https://doi.org/10.1016/B978-0-12-822945-3.00019-1

[169] MeghwanshiGK, KaurN, VermaS, DabiNK, VashishthaA, CharanP, et al. . Enzymes for pharmaceutical and therapeutic applications. Biotechnol Appl Biochem, 2020, 674586-601.

[170] BeheraHT, MojumdarA, DasSR, JemaS, RayL. Production of N-acetyl chitooligosaccharide by novel Streptomyces chilikensis strain RC1830 and its evaluation for anti-radical, anti-inflammatory, anti-proliferative and cell migration potential. Bioresour Technol Rep, 2020, 11. 100428

[171] Sarjadi MS, Zin SM, Awalludin A, Wid N, Kadir KA. The composition of chitin, chitosan and its derivatives in the context of preparation and usability-a review. borneo science| J Sci Technol. 2020;41(2).

[172] KumarD, NarulaA, DeswalD. Role of fungal enzymes in the synthesis of pharmaceutically important scaffolds: a green approach. Green Chem, 2023, 25239463-9500

[173] LiuZ-Q, LuM-M, ZhangX-H, ChengF, XuJ-M, XueY-P, et al. . Significant improvement of the nitrilase activity by semi-rational protein engineering and its application in the production of iminodiacetic acid. Int J Biol Macromol, 2018, 116: 563-571

[174] FuL, LiX, XiaoX, XuJ. Purification and characterization of a thermostable aliphatic amidase from the hyperthermophilic archaeon Pyrococcus yayanosii CH1. Extremophiles, 2014, 182429-440

[175] SuzukiY, OhtaH. Identification of a thermostable and enantioselective amidase from the thermoacidophilic archaeon Sulfolobus tokodaii strain 7. Protein Expr Purif, 2006, 452368-373

[176] d' Abusco A, Ammendola S, Scandurra R, Politi L. Molecular and biochemical characterization of the recombinant amidase from hyperthermophilic archaeon Sulfolobus solfataricus. Extremophiles. 2001;5(3):183–92. https://link.springer.com/article/https://doi.org/10.1007/s007920100190#citeas

[177] MuellerP, EgorovaK, VorgiasCE, BoutouE, TrauthweinH, VerseckS, et al. . Cloning, overexpression, and characterization of a thermoactive nitrilase from the hyperthermophilic archaeon Pyrococcus abyssi. Protein Expr Purif, 2006, 472672-681

[178] ZahraniNAA, El-ShishtawyRM, AsiriAM. Recent developments of gallic acid derivatives and their hybrids in medicinal chemistry: A review. European J Medicinal Chem, 2020, 204112609

[179] Kotb E, Alabdalall AH, Alsayed MA, Alghamdi AI, Alkhaldi E, AbdulAzeez S, et al. Isolation, Screening, and Identification of Alkaline Protease-Producing Bacteria and Application of the Most Potent Enzyme from Bacillus sp. Mar64. Fermentation. 2023;9(7):637.

[180] Al-GhanayemAA, JosephB. Current prospective in using cold-active enzymes as eco-friendly detergent additive. Applied Microbiol Biotechnol, 2020, 10472871-2882

[181] KanekarPP, KanekarSPAlkaliphilic, alkalitolerant microorganisms, 2022Diversity and biotechnology of extremophilic microorganisms from IndiaSpringer71-116

[182] HamidB, BashirZ, YatooAM, MohiddinF, MajeedN, BansalM, et al. . Cold-active enzymes and their potential industrial applications—a review. Molecules, 2022, 27185885

[183] Azevedo MA, do Nascimento LP, dos Remédios Vieira-Neta M, Duarte ICS. Production of biosurfactant by bacteria from extreme environments: biotechnological potential and applications. In: Kumar P and Dubey RC (eds) Multifunctional Microbial Biosurfactants: Springer Cham; 2023. pp 129–56. https://doi.org/10.1007/978-3-031-31230-4_6

[184] Saha I, Datta S, Biswas D, Sengupta D. A comparative study on chemical characterization and properties of surface active compounds from Gram-positive Bacillus and Gram-negative Ochrobactrum strains utilizing pure hydrocarbons and waste mineral lubricating oils. World J Microbiol Biotechnol. 2022;38(8):141. https://link.springer.com/article/https://doi.org/10.1007/s11274-022-03321-5

[185] Gaonkar SK, Furtado IJ. Simultaneous purification and characterization of detergent-stable, solvent-tolerant haloextremozymes protease and lipase from Haloferax sp. strain GUBF 2. Arch Microbiol. 2022;204(12):705. https://link.springer.com/article/https://doi.org/10.1007/s00203-022-03286-x

[186] JoshiS, SatyanarayanaT. Biotechnology of cold-active proteases. Biology, 2013, 22755-783

[187] Lee MS, Kim GA, Seo MS, Lee JH, Kwon ST. Characterization of heat‐labile uracil‐DNA glycosylase from Psychrobacter sp. HJ147 and its application to the polymerase chain reaction. Biotechnol Appl Biochem. 2009;52(2):167–75. https://doi.org/10.1042/BA20080013

[188] GeorletteD, JonssonZ, Van PetegemF, ChessaJP, Van BeeumenJ, HübscherU, et al. . A DNA ligase from the psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures. Eur J Biochem, 2000, 267123502-3512.

[189] RothschildLJ, MancinelliRL. Life in extreme environments. Nature, 2001, 40968231092-1101

[190] FujiwaraS. Extremophiles: Developments of their special functions and potential resources. J Biosci Bioeng, 2002, 946518-525

[191] GomesJ, SteinerW. The biocatalytic potential of extremophiles and extremozymes. Food Technol Biotechnol, 2004, 424223-225

[192] Souii A, Ghorrab A, Hammami K, Masmoudi AS, Cherif A, Neifar M. Extremozyme‐Based Technology for Biofuel Generation: Bioactivity and Stability Performances. In Gupta VK, Sarkar SD, Sharma M, Pirovani ME, Usmani Z, Chelliah (eds) Biomolecules from Natural Sources: Advances and Applications. 2022:214–51. https://doi.org/10.1002/9781119769620.ch

[193] ElleucheS, SchröderC, SahmK, AntranikianG. Extremozymes—biocatalysts with unique properties from extremophilic microorganisms. Curr Opin Biotechnol, 2014, 29: 116-123.

[194] KochR, ZablowskiP, SpreinatA, AntranikianG. Extremely thermostable amylolytic enzyme from the archaebacterium Pyrococcus furiosus. FEMS Microbiol Lett, 1990, 711–221-26

[195] Kim JW, Flowers LO, Whiteley M, Peeples TL. Biochemical confirmation and characterization of the family-57-like α-amylase of Methanococcus jannaschii. Folia Microbiol. 2001;46(6):467–73. https://link.springer.com/article/https://doi.org/10.1007/BF02817988

[196] Capolupo L, Faraco V. Green methods of lignocellulose pretreatment for biorefinery development. Appl Microbiol Biotechnol. 2016;100(22):9451–67. https://link.springer.com/article/https://doi.org/10.1007/s00253-016-7884-y

[197] AtalahJ, Cáceres-MorenoP, EspinaG, BlameyJM. Thermophiles and the applications of their enzymes as new biocatalysts. Bioresour Technol, 2019, 280: 478-488.

[198] BaezaM, AlcaínoJ, CifuentesV, TurchettiB, BuzziniPSibirnyAA. Cold-Active Enzymes from Cold-Adapted Yeasts. Biotechnology of Yeasts and Filamentous Fungi, 2017ChamSpringer International Publishing297-324

[199] Yao Q, Huang M, Bu Z, Zeng J, Wang X, Liu Z, et al. Identification and characterization of a novel bacterial carbohydrate esterase from the bacterium Pantoea ananatis Sd-1 with potential for degradation of lignocellulose and pesticides. Biotechnol Lett. 2020;42(8):1479–88. https://link.springer.com/article/https://doi.org/10.1007/s10529-020-02855-8

[200] Kim H, Park AK, Lee JH, Shin SC, Park H, Kim H-W. PsEst3, a new psychrophilic esterase from the Arctic bacterium Paenibacillus sp. R4: crystallization and X-ray crystallographic analysis. Acta Crystallogr Sect F Struct Biol Commun. 2018;74(6):367–72.

[201] XieY, HuQ, FengG, JiangX, HuJ, HeM, et al. . Biodetoxification of phenolic inhibitors from lignocellulose pretreatment using Kurthia huakuii LAM0618T and subsequent lactic acid fermentation. Molecules, 2018, 23102626.

[202] Cubas-CanoE, VenusJ, González-FernándezC, Tomás-PejóE. Assessment of different Bacillus coagulans strains for l-lactic acid production from defined media and gardening hydrolysates: Effect of lignocellulosic inhibitors. J Biotechnol, 2020, 323: 9-16

[203] Sharma A, Shadiya, Sharma T, Kumar R, Meena K, Kanwar SS. Biodiesel and the Potential Role of Microbial Lipases in Its Production. In: Arora PK, (ed). Microbial Technology for the Welfare of Society. Singapore: Springer Singapore; 2019. Pp 83–99.

[204] UgurA, SaracN, BoranR, AyazB, CeylanO, OkmenG. New lipase for biodiesel production: Partial purification and characterization of LipSB 25–4. Int Sch Res Notices, 2014, 20141289749

[205] LeeD-W, KohY-S, KimK-J, KimB-C, ChoiH-J, KimD-S, et al. . Isolation and characterization of a thermophilic lipase from Bacillus thermoleovorans ID-1. FEMS Microbiol Lett, 1999, 1792393-400

[206] Dharmsthiti S, Luchai S. Production, purification and characterization of thermophilic lipase from Bacillus sp. THL027. FEMS microbiology letters. 1999;179(2):241–6.

[207] Tripathi R, Singh J, Bharti Rk, Thakur IS. Isolation, purification and characterization of lipase from Microbacterium sp. and its application in biodiesel production. Energy Procedia. 2014;54:518–29.

[208] ChristopherLP, ZambareVP, ZambareA, KumarH, MalekL. A thermo-alkaline lipase from a new thermophile Geobacillus thermodenitrificans AV-5 with potential application in biodiesel production. J ChemTechnol Biotechnol, 2015, 90112007-2016.

[209] KrügerA, SchäfersC, SchröderC, AntranikianG. Towards a sustainable biobased industry – Highlighting the impact of extremophiles. New Biotechnol, 2018, 40: 144-153

[210] Dyrda G, Boniewska-Bernacka E, Man D, Barchiewicz K, Słota R. The effect of organic solvents on selected microorganisms and model liposome membrane. Mol Biol Rep. 2019;46:3225–32. https://link.springer.com/article/https://doi.org/10.1007/s11033-019-04782-y

[211] UsamiR, FukushimaT, MizukiT, InoueA, YoshidaY, HorikoshiK. Organic solvent tolerance of halophilic archaea. Biosci Biotechnol Biochem, 2003, 6781809-1812

[212] UsamiR, FukushimaT, MizukiT, YoshidaY, InoueA, HorikoshiK. Organic solvent tolerance of halophilic archaea, Haloarcula strains: Effects of NaCl concentration on the tolerance and polar lipid composition. J Biosci Bioeng, 2005, 992169-174

[213] KobayashiH, TakamiH, HirayamaH, KobataK, UsamiR, HorikoshiK. Outer membrane changes in a toluene-sensitive mutant of toluene-tolerant Pseudomonas putida IH-2000. J Bacterio, 1999, 181154493-4498

[214] PátekM, GrulichM, NešveraJ. Stress response in Rhodococcus strains. Biotechnol Adv, 2021, 53. 107698

[215] KikaniB, PatelR, ThumarJ, BhattH, RathoreDS, KoladiyaGA, et al. . Solvent tolerant enzymes in extremophiles: Adaptations and applications. Int J BiolMacromo, 2023, 238. 124051

[216] GuptaA, KhareS. Enzymes from solvent-tolerant microbes: useful biocatalysts for non-aqueous enzymology. Crit Rev Biotechnol, 2009, 29144-54.

[217] WangS, LeiH, JiZ. Exploring oxidoreductases from extremophiles for biosynthesis in a non-aqueous system. Int J Mol Sci, 2023, 2476396

[218] CassidyJ, ParadisiF. Haloquadratum walsbyi Yields a Versatile, NAD⁺/NADP⁺ Dual Affinity, Thermostable, Alcohol Dehydrogenase (HwADH). Mol Biotechnol, 2018, 606420-426

[219] Alsafadi D, Paradisi F. Effect of organic solvents on the activity and stability of halophilic alcohol dehydrogenase (ADH2) from Haloferax volcanii. Extremophiles. 2013;17(1):115–22. https://link.springer.com/article/https://doi.org/10.1007/s00792-012-0498-0

[220] Ding H-T, Du Y-Q, Liu D-F, Li Z-L, Chen X-J, Zhao Y-H. Cloning and expression in E. coli of an organic solvent-tolerant and alkali-resistant glucose 1-dehydrogenase from Lysinibacillus sphaericus G10. Bioresour Techno. 2011;102(2):1528–36. https://doi.org/10.1016/j.biortech.2010.08.018

[221] FongaroG, MaiaGA, RogovskiP, CadamuroRD, LopesJC, MoreiraRS, et al. . Extremophile microbial communities and enzymes for bioenergetic application based on multi-omics tools. Curr Genom, 2020, 214240-252

[222] Madhavan A, Sindhu R, Parameswaran B, Sukumaran RK, Pandey A. Metagenome Analysis: A powerful tool for enzyme bioprospecting. Appl Biochem Biotechnol. 2017;183(2):636–51. https://link.springer.com/article/https://doi.org/10.1007/s12010-017-2568-3

[223] DanielR. The metagenomics of soil. Nat Rev Microbiol, 2005, 36470-478

[224] Simon C, Daniel R. Achievements and new knowledge unraveled by metagenomic approaches. Appl Microbiol Biotechnol. 2009;85(2):265–76. https://link.springer.com/article/https://doi.org/10.1007/s00253-009-2233-z

[225] Wang H, Gong Y, Xie W, Xiao W, Wang J, Zheng Y, et al. Identification and characterization of a novel thermostable gh-57 gene from metagenomic fosmid library of the Juan de Fuca ridge hydrothemal vent. Appl Biochem Biotechnol. 2011;164(8):1323–38. https://link.springer.com/article/https://doi.org/10.1007/s12010-011-9215-1

[226] Gupta R, Govil T, Capalash N, Sharma P. Characterization of a Glycoside Hydrolase Family 1 β-galactosidase from hot spring metagenome with transglycosylation activity. Appl Biochem Biotechnol. 2012;168(6):1681–93. https://link.springer.com/article/https://doi.org/10.1007/s12010-012-9889-z

[227] LeisB, AngelovA, MientusM, LiH, PhamVT, LauingerB, et al. . Identification of novel esterase-active enzymes from hot environments by use of the host bacterium Thermus thermophilus. Front Microbiol, 2015, 6: 275.

[228] López-PérezM, MireteS. Discovery of novel antibiotic resistance genes through metagenomics. Recent Adv DNA Gene Sequences, 2014, 8115-19.

[229] BohmannK, EvansA, GilbertMTP, CarvalhoGR, CreerS, KnappM, et al. . Environmental DNA for wildlife biology and biodiversity monitoring. Trends Ecol Evol, 2014, 296358-367

[230] Chi KR. Singled out for sequencing. Nature Publishing Group; 2013.

[231] BlaineyPC. The future is now: single-cell genomics of bacteria and archaea. FEMS Microbiol Rev, 2013, 373407-427

[232] WoykeT, TigheD, MavromatisK, ClumA, CopelandA, SchackwitzW, et al. . One bacterial cell, one complete genome. PLoS ONE, 2010, 54. e10314

[233] WilsonMC, MoriT, RückertC, UriaAR, HelfMJ, TakadaK, et al. . An environmental bacterial taxon with a large and distinct metabolic repertoire. Nature, 2014, 506748658-62

[234] Landry ZC, Giovanonni SJ, Quake SR, Blainey PC. Chapter Four - Optofluidic Cell Selection from Complex Microbial Communities for Single-Genome Analysis. In: DeLong EF, editor. Methods in Enzymology. 531: Academic Press; 2013. pp 61–90.

[235] Frumkin D, Wasserstrom A, Itzkovitz S, Harmelin A, Rechavi G, Shapiro E. Amplification of multiple genomic loci from single cells isolated by laser micro-dissection of tissues. BMC Biotechnol. 2008;8(1):17. https://link.springer.com/article/https://doi.org/10.1186/1472-6750-8-17

[236] LearyDH, HerveyWJ, DeschampsJR, KusterbeckAW, VoraGJ. Which metaproteome? The impact of protein extraction bias on metaproteomic analyses. Mol Cell Probes, 2013, 275193-199.

[237] Hassa J, Maus I, Off S, Pühler A, Scherer P, Klocke M, et al. Metagenome, metatranscriptome, and metaproteome approaches unraveled compositions and functional relationships of microbial communities residing in biogas plants. Appl Microbiol Biotechnol. 2018;102(12):5045–63. https://link.springer.com/article/https://doi.org/10.1007/s00253-018-8976-7

[238] Maseh K, Ehsan N, Mukhtar S, Mehnaz S, Malik KA. Metaproteomics: an emerging tool for the identification of proteins from extreme environments. Environ Sustain. 2021;4(1):39–50. https://link.springer.com/article/https://doi.org/10.1007/s42398-020-00158-2

[239] Babu P, Chandel AK, Singh OV. Challenges in Advancing Extremophiles for Therapeutic Applications. Extremophiles and Their Applications in Medical Processes. Cham: Springer International Publishing; 2015. p. 37–41.

[240] Mandelli F, Couger MB, Paixão DAA, Machado CB, Carnielli CM, Aricetti JA, et al. Thermal adaptation strategies of the extremophile bacterium Thermus filiformis based on multi-omics analysis. Extremophiles. 2017;21(4):775–88. https://link.springer.com/article/https://doi.org/10.1007/s00792-017-0942-2

[241] Busch P, Suleiman M, Schäfers C, Antranikian G. A multi-omic screening approach for the discovery of thermoactive glycoside hydrolases. Extremophiles. 2021;25(2):101–14. https://link.springer.com/article/https://doi.org/10.1007/s00792-020-01214-9

[242] IaconoR, StrazzulliA, GiglioR, BitettiF, Cobucci-PonzanoB, MoracciM. Valorization of biomasses from energy crops for the discovery of novel thermophilic glycoside hydrolases through metagenomic analysis. Int J Mol Sci, 2022, 231810505.

[243] Cario A, Oliver GC, Rogers KL. Exploring the Deep Marine Biosphere: Challenges, innovations, and opportunities. Front Earth Sci. 2019;7. https://doi.org/10.3389/feart.2019.00225

[244] UsmaniZ, SharmaM, AwasthiAK, SivakumarN, LukkT, PecoraroL, et al. . Bioprocessing of waste biomass for sustainable product development and minimizing environmental impact. Bioresour Technol, 2021, 322. 124548

[245] Kumar A, Mukhia S, Kumar R. Industrial applications of cold-adapted enzymes: challenges, innovations and future perspective. 3 Biotech. 2021;11(10):426. https://link.springer.com/article/https://doi.org/10.1007/s13205-021-02929-y

[246] Al-GhanayemAA. Recent developments and future prospects of extremozymes in detergent applications. Afr J Microbiol Res, 2024, 187137-146.

[247] Pinzón-MartínezD, Rodríguez-GómezC, Miñana-GalbisD, Carrillo-ChávezJ, Valerio-AlfaroG, Oliart-RosR. Thermophilic bacteria from Mexican thermal environments: isolation and potential applications. Environ Technol, 2010, 318–9957-966.

[248] Samaei-Nouroozi A, Rezaei S, Khoshnevis N, Doosti M, Hajihoseini R, Khoshayand MR, et al. Medium-based optimization of an organic solvent-tolerant extracellular lipase from the isolated halophilic Alkalibacillus salilacus. Extremophiles. 2015;19:933–47. https://link.springer.com/article/https://doi.org/10.1007/s00792-015-0769-7

[249] Abdel-Hamed AR, Abo-Elmatty DM, Wiegel J, Mesbah NM. Biochemical characterization of a halophilic, alkalithermophilic protease from Alkalibacillus sp. NM-Da2. Extremophiles. 2016;20:885–94. https://link.springer.com/article/https://doi.org/10.1007/s00792-016-0879-x

[250] KikaniB, SinghS. The stability and thermodynamic parameters of a very thermostable and calcium-independent α-amylase from a newly isolated bacterium, Anoxybacillus beppuensis TSSC-1. Process Biochem, 2012, 47121791-1798.

[251] Bano A, Chen X, Prasongsuk S, Akbar A, Lotrakul P, Punnapayak H, et al. Purification and characterization of cellulase from obligate halophilic Aspergillus flavus (TISTR 3637) and its prospects for bioethanol production. Appl Biochem Biotechnol. 2019;189:1327–37. https://link.springer.com/article/https://doi.org/10.1007/s12010-019-03086-y

[252] SalihiA, AsoodehA, AliabadianM. Production and biochemical characterization of an alkaline protease from Aspergillus oryzae CH93. Int J Biol Macromol, 2017, 94: 827-835.

[253] Awasti P, Shrivastava S. Screening and identification of thermophilic glycosyl hydrolases producing microorganisms. J Biotechnol Biores. 2018;1–5

[254] MohammadBT, Al DaghistaniHI, JaouaniA, Abdel-LatifS, KennesC. Isolation and characterization of thermophilic bacteria from Jordanian hot springs: Bacillus licheniformis and Thermomonas hydrothermalis isolates as potential producers of thermostable enzymes. Int J Microbiol, 2017, 201716943952.

[255] DhundaleVR, MoreVR, NagarkarandRD, HemkeVM, TambekarDH. Isolation and characterization of a novel amylase from Bacillus pseudofirmus DW4 (1). Indian J Life Sci, 2014, 4169

[256] BawejaM, TiwariR, SinghPK, NainL, ShuklaP. An alkaline protease from Bacillus pumilus MP 27: functional analysis of its binding model toward its applications as detergent additive. Front Microbiol, 2016, 7: 1195.

[257] BawejaM, SinghPK, SadafA, TiwariR, NainL, KhareSK, et al. . Cost effective characterization process and molecular dynamic simulation of detergent compatible alkaline protease from Bacillus pumilus strain MP27. Process Biochemi, 2017, 58: 199-203

[258] HemkeVM, DhundaleVR. Characterization and stability of extracellular alkaline proteases from halophilic and alkaliphilic bacteria isolated from saline habitat of lonar soda lake. India Int J Pharm Sci Res, 2018, 951974-1979

[259] Nomwesigwa C, Noby N, Hammad S, Abdel-Mawgood A. Screening for extremophilic lipase producing bacteria: Partial purification and characterization of thermo-halophilic, solvent tolerant lipase from Bacillus sp. Int J Eng Technol. 2023;15(1).

[260] HomaeiA, IzadpanahQF. Purification and characterization of a robust thermostable protease isolated from Bacillus subtilis strain HR02 as an extremozyme. J Appl Microbiol, 2022, 13352779-2789.

[261] Ali N, Ullah N, Qasim M, Rahman H, Khan SN, Sadiq A, et al. Molecular characterization and growth optimization of halo-tolerant protease producing Bacillus Subtilis Strain BLK-1.5 isolated from salt mines of Karak, Pakistan. Extremophiles. 2016;20:395–402.

[262] SuganthiC, MageswariA, KarthikeyanS, GothandamKM. Insight on biochemical characteristics of thermotolerant amylase isolated from extremophile bacteria Bacillus vallismortis TD6 (HQ992818). Microbiology, 2015, 84: 210-218

[263] Necula-Petrareanu G, Lavin P, Paun VI, Gheorghita GR, Vasilescu A, Purcarea C. Highly stable, cold-active aldehyde dehydrogenase from the Marine Antarctic Flavobacterium sp. PL002. Fermentation. 2021;8(1):7. https://doi.org/10.3390/fermentation8010007

[264] Elbanna K, Ibrahim IM, Revol-Junelles A-M. Purification and characterization of halo-alkali-thermophilic protease from Halobacterium sp. strain HP25 isolated from raw salt, Lake Qarun, Fayoum, Egypt. Extremophiles. 2015;19:763–74. https://link.springer.com/article/https://doi.org/10.1007/s00792-015-0752-3

[265] Moshfegh M, Shahverdi AR, Zarrini G, Faramarzi MA. Biochemical characterization of an extracellular polyextremophilic α-amylase from the halophilic archaeon Halorubrum xinjiangense. Extremophiles. 2013;17:677–87. https://link.springer.com/article/https://doi.org/10.1007/s00792-013-0551-7

[266] PerezD, MartínS, Fernandez-LorenteG, FiliceM, GuisánJM, VentosaA, et al. . A novel halophilic lipase, LipBL, showing high efficiency in the production of eicosapentaenoic acid (EPA). PLoS ONE, 2011, 68. e23325

[267] Martínez-Pérez RB, Rodríguez JA, Cira-Chávez LA, Dendooven L, Viniegra-González G, Estrada-Alvarado I. Exoenzyme-producing halophilic bacteria from the former Lake Texcoco: Identification and production of n-butyl oleate and bioactive peptides. Folia Microbiol. 2020;65:835–47. https://link.springer.com/article/https://doi.org/10.1007/s12223-020-00794-5

[268] AroraA, KrishnaP, MalikV, ReddyMS. Alkalistable xylanase production by alkalitolerant Paenibacillus montaniterrae RMV 1 isolated from red mud. J Basic Microbiol, 2014, 54101023-1029

[269] Omrane Benmrad M, Mechri S, Zaraî Jaouadi N, Ben Elhoul M, Rekik H, Sayadi S, et al. Purification and biochemical characterization of a novel thermostable protease from the oyster mushroom Pleurotus sajor-caju strain CTM10057 with industrial interest. BMC Biotechnol. 2019;19:1–18. https://link.springer.com/article/https://doi.org/10.1186/s12896-019-0536-4

[270] Darnal S, Patial V, Kumar V, Kumar S, Kumar V, Padwad YS, et al. Biochemical characterization of extremozyme L-asparaginase from Pseudomonas sp. PCH199 for therapeutics. AMB Express. 2023;13(1):22.

[271] Zheng X, Chu X, Zhang W, Wu N, Fan Y. A novel cold-adapted lipase from Acinetobacter sp. XMZ-26: gene cloning and characterisation. Appl Microbiol Biotechnol. 2011;90(3):971–80. https://link.springer.com/article/https://doi.org/10.1007/s00253-011-3154-1

[272] NakagawaT, FujimotoY, UchinoM, MiyajiT, TakanoK, TomizukaN. Isolation and characterization of psychrophiles producing cold-active -galactosidase. Lett Appl Microbiol, 2003, 372154-157.

[273] Farooq S, Nazir R, Ganai SA, Ganai BA. Isolation and characterization of a new cold-active protease from psychrotrophic bacteria of Western Himalayan glacial soil. Sci Rep. 2021;11(1):12768. https://www.nature.com/articles/s41598-021-92197-w

[274] Joseph B, Ramteke PW. Extracellular solvent stable cold-active lipase from psychrotrophic Bacillus sphaericus MTCC 7526: partial purification and characterization. Ann Microbiol. 2013;63(1):363–70. https://link.springer.com/article/https://doi.org/10.1007/s13213-012-0483-y

[275] HamidB, SinghP, MohiddinFA, SahayS. Partial characterization of cold-active β-galactosidase activity produced by Cystophallobaidium capatitum SPY11 and Rhodotorella musloganosa PT1. J Endocytobiosis Cell Res, 2013, 23: 26

[276] JosephB, ShrivastavaN, RamtekePW. Extracellular cold-active lipase of Microbacterium luteolum isolated from Gangotri glacier, western Himalaya: Isolation, partial purification and characterization. J Genetic Eng Biotechnol, 2012, 101137-144.

[277] SahayS, ChouhanD. Study on the potential of cold-active lipases from psychrotrophic fungi for detergent formulation. J Genetic Eng Biotechnol, 2018, 162319-325.

[278] Van de VoordeI, GoirisK, SyrynE, Van den BusscheC, AertsG. Evaluation of the cold-active Pseudoalteromonas haloplanktis β-galactosidase enzyme for lactose hydrolysis in whey permeate as primary step of d-tagatose production. Process Biochem, 2014, 49122134-2140.

[279] Ramya LN, Pulicherla KK. Molecular insights into cold active polygalacturonase enzyme for its potential application in food processing. J Food Sci Technol. 2015;52(9):5484–96. https://link.springer.com/article/https://doi.org/10.1007/s13197-014-1654-6

[280] Qin Y, Huang Z, Liu Z. A novel cold-active and salt-tolerant α-amylase from marine bacterium Zunongwangia profunda: molecular cloning, heterologous expression and biochemical characterization. Extremophiles. 2014;18(2):271–81. https://link.springer.com/article/https://doi.org/10.1007/s00792-013-0614-9

[281] WeiH, TuckerMP, BakerJO, HarrisM, LuoY, XuQ, et al. . Tracking dynamics of plant biomass composting by changes in substrate structure, microbial community, and enzyme activity. Biotechnol Biofuels, 2012, 5120

[282] SharmaM, ChadhaBS, SainiHS. Purification and characterization of two thermostable xylanases from Malbranchea flava active under alkaline conditions. Bioresour Technol, 2010, 101228834-8842.

[283] Sharma M, Mahajan C, Bhatti MS, Chadha BS. Profiling and production of hemicellulases by thermophilic fungus Malbranchea flava and the role of xylanases in improved bioconversion of pretreated lignocellulosics to ethanol. 3 Biotech. 2016;6(1):30. https://link.springer.com/article/https://doi.org/10.1007/s13205-015-0325-2

[284] Apostolidi ME, Kalantzi S, Hatzinikolaou DG, Kekos D, Mamma D. Catalytic and thermodynamic properties of an acidic α-amylase produced by the fungus Paecilomyces variotii ATHUM 8891. 3 Biotech. 2020;10(7):311. https://link.springer.com/article/https://doi.org/10.1007/s13205-020-02305-2

[285] McPhillips K, Waters DM, Parlet C, Walsh DJ, Arendt EK, Murray PG. Purification and characterisation of a β-1,4-xylanase from Remersonia thermophila CBS 540.69 and its application in bread making. Appl Biochem Biotechnol. 2014;172(4):1747–62. https://link.springer.com/article/https://doi.org/10.1007/s12010-013-0640-1

[286] FawziE. Highly thermostable xylanase purified from Rhizomucor miehei NRL 3169. Acta Biol Hung, 2011, 62185-94

[287] Romdhane IB-B, Romdhane ZB, Gargouri A, Belghith H. Esterification activity and stability of Talaromyces thermophilus lipase immobilized onto chitosan. J Mol Catal B: Enzym. 2011;68(3):230–9. https://doi.org/10.1016/j.molcatb.2010.11.010

[288] ZhangM, PuriAK, GovenderA, WangZ, SinghS, PermaulK. The multi-chitinolytic enzyme system of the compost-dwelling thermophilic fungus Thermomyces lanuginosus. Process Biochem, 2015, 502237-244.

[289] KuhadRC, GuptaR, SinghA. Microbial cellulases and their industrial applications. Enzyme Res, 2011, 20111. 280696

[290] Vreeland RH, Piselli Jr AF, McDonnough S, Meyers SS. Distribution and diversity of halophilic bacteria in a subsurface salt formation. Extremophiles. 1998;2(3):321–31. https://link.springer.com/article/https://doi.org/10.1007/s007920050075

[291] Pérez-Pomares F, Bautista V, Ferrer J, Pire C, Marhuenda-Egea FC, Bonete MJ. α-Amylase activity from the halophilic archaeon Haloferax mediterranei. Extremophiles. 2003;7(4):299–306. https://link.springer.com/article/https://doi.org/10.1007/s00792-003-0327-6

[292] CoronadoM-J, VargasC, HofemeisterJ, VentosaA, NietoJJ. Production and biochemical characterization of an α-amylase from the moderate halophile Halomonas meridiana. FEMS Microbiol Lett, 2000, 183167-71

[293] TianF, GuoG, ZhangC, YangF, HuZ, LiuC, et al. . Isolation, cloning and characterization of an azoreductase and the effect of salinity on its expression in a halophilic bacterium. Int J Biol Macromol, 2019, 123: 1062-1069.

[294] GulatiR, SaxenaR, GuptaR. A rapid plate assay for screening L-asparaginase producing micro-organisms. Lett Appl Microbiol, 1997, 24123-26

[295] Kobayashi T, Kanai H, Hayashi T, Akiba T, Akaboshi R, Horikoshi K. Haloalkaliphilic maltotriose-forming alpha-amylase from the archaebacterium Natronococcus sp. strain Ah-36. J Bacteriol. 1992;174(11):3439–44.

[296] BoutaibaS, BhatnagarT, HaceneH, MitchellDA, BarattiJC. Preliminary characterisation of a lipolytic activity from an extremely halophilic archaeon, Natronococcus sp. J Mol Catal B: Enzym, 2006, 41121-26.

[297] Amoozegar MA, Salehghamari E, Khajeh K, Kabiri M, Naddaf S. Production of an extracellular thermohalophilic lipase from a moderately halophilic bacterium, Salinivibrio sp. strain SA‐2. J Basic Microbiol. 2008;48(3):160–7. https://doi.org/10.1002/jobm.200700361

[298] Bose A, Chawdhary V, Keharia H, Subramanian RB. Production and characterization of a solvent-tolerant protease from a novel marine isolate Bacillus tequilensis P15. Ann Microbiol. 2014;64(1):343–54. https://link.springer.com/article/https://doi.org/10.1007/s13213-013-0669-y

[299] Fukushima T, Mizuki T, Echigo A, Inoue A, Usami R. Organic solvent tolerance of halophilic α-amylase from a Haloarchaeon, Haloarcula sp. strain S-1. Extremophiles. 2005;9(1):85–9. https://link.springer.com/article/https://doi.org/10.1007/s00792-004-0423-2

[300] Uttatree S, Winayanuwattikun P, Charoenpanich J. Isolation and characterization of a novel thermophilic-organic solvent stable lipase from Acinetobacter baylyi. Appl Biochem Biotechnol. 2010;162(5):1362–76. https://link.springer.com/article/https://doi.org/10.1007/s12010-010-8928-x

[301] Zhang S, Wu G, Liu Z, Shao Z, Liu Z. Characterization of EstB, a novel cold-active and organic solvent-tolerant esterase from marine microorganism Alcanivorax dieselolei B-5(T). Extremophiles. 2014;18(2):251–9. https://link.springer.com/article/https://doi.org/10.1007/s00792-013-0612-y

[302] Samaei-Nouroozi A, Rezaei S, Khoshnevis N, Doosti M, Hajihoseini R, Khoshayand MR, et al. Medium-based optimization of an organic solvent-tolerant extracellular lipase from the isolated halophilic Alkalibacillus salilacus. Extremophiles. 2015;19(5):933–47. https://link.springer.com/article/https://doi.org/10.1007/s00792-015-0769-7

[303] XuJ, JiangM, SunH, HeB. An organic solvent-stable protease from organic solvent-tolerant Bacillus cereus WQ9-2: Purification, biochemical properties, and potential application in peptide synthesis. Bioresour Technol, 2010, 101207991-7994.

[304] Malekabadi S, Badoei-dalfard A, Karami Z. Biochemical characterization of a novel cold-active, halophilic and organic solvent-tolerant lipase from B. licheniformis KM12 with potential application for biodiesel production. Int J Biol Macromol. 2018;109:389–98. https://doi.org/10.1016/j.ijbiomac.2017.11.173

[305] ZhangW, XuH, WuY, ZengJ, GuoZ, WangL, et al. . A new cold-adapted, alkali-stable and highly salt-tolerant esterase from Bacillus licheniformis. Int J Biol Macromol, 2018, 111: 1183-1193.

[306] Singh P, Patel V, Shah V, Madamwar D. A solvent-tolerant alkaline lipase from Bacillus sp. DM9K3 and its potential applications in esterification and polymer degradation. Appl Biochem Microbiol. 2019;55(6):603–14. https://doi.org/10.1134/S0003683819060139

[307] RuizDM, De CastroRE. Effect of organic solvents on the activity and stability of an extracellular protease secreted by the haloalkaliphilic archaeon Natrialba magadii. J Ind Microbiol Biotechnol, 2007, 342111-115.

[308] Shafiei M, Ziaee A-A, Amoozegar MA. Purification and characterization of an organic-solvent-tolerant halophilic α-amylase from the moderately halophilic Nesterenkonia sp. strain F. J Ind Microbiol Biotechnol. 2011;38(2):275–81. https://doi.org/10.1007/s10295-010-0770-1

[309] OginoH, GembaY, YutoriY, DoukyuN, IshimiK, IshikawaH. Stabilities and conformational transitions of various proteases in the presence of an organic solvent. Biotechnol Prog, 2007, 231155-161.

[310] Xin L, Hui-Ying Y. Purification and characterization of an extracellular esterase with organic solvent tolerance from a halotolerant isolate, Salimicrobium sp. LY19. BMC Biotechnol. 2013;13(1):108. https://doi.org/10.1186/1472-6750-13-108

[311] ThumarJT, SinghSP. Organic solvent tolerance of an alkaline protease from salt-tolerant alkaliphilic Streptomyces clavuligerus strain Mit-1. J Ind Microbiol Biotechnol, 2009, 362211-218.

[312] RampelottoPH. Extremophiles and extreme environments: A decade of progress and challenges. Life, 2024, 143482-485.

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