Agroresidues enhanced peroxidase activity expression by Bacillus sp. MABINYA-1 under submerged fermentation

Ayodeji O. Falade , Leonard V. Mabinya , Anthony I. Okoh , Uchechukwu U. Nwodo

Bioresources and Bioprocessing ›› 2020, Vol. 7 ›› Issue (1) : 55

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Bioresources and Bioprocessing ›› 2020, Vol. 7 ›› Issue (1) : 55 DOI: 10.1186/s40643-020-00345-3
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Agroresidues enhanced peroxidase activity expression by Bacillus sp. MABINYA-1 under submerged fermentation

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Abstract

Agroresidues have continued to gain preference over conventional carbon sources for microbial enzyme production due to the low price and abundance in the environment. Therefore, this study aimed at improving peroxidase yield by Bacillus sp. MABINYA-1 (BMAB-1) using agroresidues under submerged fermentation. The culture parameters that support maximum peroxidase yield by BMAB-1 was initially determined and the results showed that peroxidase activity expression was optimum at pH 5, 30 °C and 150 rpm while veratryl alcohol and ammonium sulphate served as the best peroxidase-inducer and inorganic nitrogen source, respectively. BMAB-1 exhibited maximum peroxidase expression (17.50 ± 0.10 U/mg) at 72 h using kraft lignin liquid medium (KLLM) under the optimized culture conditions. Upon utilization of selected agroresidues (sawdust, wheat straw and maize stover) as sole carbon sources by BMAB-1 in the fermentation process, peroxidase activity was significantly enhanced when compared with glucose (14.91 ± 0.31 U/mg) and kraft lignin (17.50 ± 0.10 U/mg). Sawdust produced the highest peroxidase yield (47.14 ± 0.41 U/mg), followed by maize stover (37.09 ± 0.00 U/mg) while wheat straw yielded the lowest peroxidase specific activity (21.65 ± 0.35 U/mg). This indicates that utilization of sawdust by BMAB-1 resulted in 3.2- and 2.7-fold increase in peroxidase activity expression as compared to glucose and kraft lignin, respectively. The aptitude of BMAB-1 to utilize agroresidues would reduce the cost of peroxidase production by the bacteria since the substrates are cheaper than the conventional carbon sources and are, as well, more readily available.

Keywords

Culture conditions / Maize stover / Peroxidase / Sawdust / Submerged fermentation / Wheat straw

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Ayodeji O. Falade, Leonard V. Mabinya, Anthony I. Okoh, Uchechukwu U. Nwodo. Agroresidues enhanced peroxidase activity expression by Bacillus sp. MABINYA-1 under submerged fermentation. Bioresources and Bioprocessing, 2020, 7(1): 55 DOI:10.1186/s40643-020-00345-3

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References

[1]

Arnau J, Yaver D, Hjort CM. Nevalainen H. Strategies and challenges for the development of industrial enzymes using fungal cell factories. Grand Challenges in Fungal Biotechnology, Grand Challenges in Biology and Biotechnology, 2020, Switzerland: Springer Nature, 179-210.

[2]

Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem, 1976, 72: 248-254.

[3]

Chance B, Maehly AC. Assay of catalases and peroxidases. Methods Enzymol, 1955, 2: 773-775.

[4]

Dumorne K. Biotechnological and industrial applications of enzymes produced by extremophilic bacteria. A mini review. Preprints, 2018

[5]

Ehiosun KI, Usman M. Evaluation of crude oil biodegradation efficiency and peroxidase production by Streptomyces albus. J Appl Sci Environ Manage, 2018, 22(2): 213-217.

[6]

Falade A, Mabinya L, Okoh A, Nwodo U. Peroxidases produced by new ligninolytic Bacillus strains isolated from marsh and grassland decolourized anthraquinone and azo dyes. Pol J Environ Stud, 2019, 28(5): 3163-3172.

[7]

Falade AO, Jaouani A, Mabinya LV, Okoh AI, Nwodo UU. Exoproduction and molecular characterization of peroxidase from Ensifer adhaerens. Appl Sci, 2019, 9: 3121.

[8]

Falade AO, Eyisi OAL, Mabinya LV, Nwodo UU, Okoh AI. Peroxidase production and ligninolytic potentials of freshwater bacteria Raoultella ornithinolytica and Ensifer adhaerens. Biotechnol Rep, 2017, 16: 12-17.

[9]

Falade AO, Mabinya LV, Okoh AI, Nwodo UU. Ligninolytic enzymes: versatile biocatalysts for the elimination of endocrine-disrupting chemicals in wastewater. MicrobiologyOpen, 2018, 7: e722.

[10]

Falade AO, Mabinya LV, Okoh AI, Nwodo UU. Agrowastes utilization by Raoultella ornithinolytica for optimal extracellular peroxidase activity. Biotechnol Appl Biochem, 2019, 66: 60-67.

[11]

Falade AO, Mabinya LV, Okoh AI, Nwodo UU. Studies on peroxidase production and detection of Sporotrichum thermophile-like catalase-peroxidase gene in a Bacillus species isolated from Hogsback forest reserve. South Africa Heliyon, 2019, 5: e03012.

[12]

Falade AO, Nwodo UU, Iweriebor BC, Green E, Mabinya LV, Okoh AI. Lignin peroxidase functionalities and prospective applications. MicrobiologyOpen, 2017, 6: e00394.

[13]

Galhaup C, Wagner H, Hinterstoisser B, Haltrich D. Increased production of laccase by the wood-degrading basidiomycete Trametes pubescens. Enzyme Microb Technol, 2002, 30: 529-536.

[14]

Gao D, Wen X, Qian Y. Effect of nitrogen concentration in culture medium on growth and enzyme production of Phanerochaete chrysosporum. J Environ Sci, 2005, 17(2): 190-193.

[15]

Ijoma GN, Selvarajan R, Tekere M. The potential of fungal co-cultures as biological inducers for increased ligninolytic enzymes on agricultural residues. Int J Environ Sci Technol, 2018

[16]

Jackson BR, Noble C, Lavesa-Curto M, Bond PL, Bowater RP. Characterization of an ATP-dependent DNA ligase from the acidophilic archaeon “Ferroplasma acidarmanus” Fer1. Extremophiles, 2007, 11: 315-327.

[17]

Kaal EEJ, Field JA, Joyce TW. Increasing ligninolytic enzyme activities in several white-rot basidiomycetes by nitrogen sufficient media. Bioresour Technol, 1995, 53: 133-139.

[18]

Kamsani N, Salleh MM, Yahya A, Chong CS. Production of lignocellulolytic enzymes by microorganisms isolated from Bulbitermes sp. termite gut in solid-state fermentation. Waste Biomass Valor, 2016, 7: 357.

[19]

Kumar A, Singh AK, Ahmad S, Chandra R. Optimization of laccase production by Bacillus sp strain AKRC01 in presence of agro-waste as effective substrate using response surface methodology. J Pure Appl Microbiol, 2020, 14(1): 1-12.

[20]

McNeil B, Harvey LM, Giavasis I. The effect of agitation and aeration on the synthesis and molecular weight of gellan in batch cultures of Sphingomonas paucimobilis. Enzyme Microb Technol, 2006, 38: 101-108.

[21]

Min K, Gong G, Woo HM, Kim Y, Um Y. A dye-decolorizing peroxidase from Bacillus subtilis exhibiting substrate-dependent optimum temperature for dyes and -ether lignin dimer. Sci Rep, 2015, 5: 8245.

[22]

Musengi A, Khan N, Le Roes-Hill M, Pletschke BI. Increasing the scale of peroxidase production by Streptomyces sp. strain BSII#1. J Appl Microbiol, 2014, 116: 554-562.

[23]

Niladevi KN, Prema P. Effect of inducers and process parameters on laccase production by Streptomyces psammoticus and its application in dye decolourization. Bioresour Technol, 2008, 99: 4583-4589.

[24]

Nour El-Dein MM, Shereif AEA, Mansour FA, Abou-Dobara MI, Ball AS. Optimization of xylanase and peroxidase production from Streptomyces sp. K37. J BioSci Biotech, 2014, 3: 29-42.

[25]

Papagianni M, Moo-Young M. Protease secretion in glucoamylase producer Aspergillus niger cultures: Fungal morphology and inoculum effects. Process Biochem, 2002, 37: 1271-1278.

[26]

Patil SR. Production and purification of lignin peroxidase from Bacillus megaterium and its application in bioremediation. CIBTech J Microbiol, 2014, 3: 22-28.

[27]

Pedri ZC, Lozano LMS, Hermann KL, Helm CV, Peralta RM, Tavares LBB. Influence of nitrogen sources on the enzymatic activity and grown by Lentinula edodes in biomass Eucalyptus benthamii. Braz J Biol, 2015

[28]

Rajkumar R, Yaakob Z, Takriff MS, Kamarudin KF. Optimization of medium composition for production of peroxidase by Bacillus sp. Der Pharma Chemica, 2013, 5: 167-174.

[29]

Rao PR, Kavya P. Production, isolation and purification of peroxidase using Bacillus subtilis. 2014 1st International Congress on Environmental, Biotechnology, and Chemistry Engineering. IPCBEE, 2014, 64: 21-27.

[30]

Ray AK, Bairagi A, Ghosh KS, Sen SK. Optimization of fermentation conditions for cellulase production by Bacillus subtilis CY5 and Bacillus circulans TP3 isolated from fish gut Acta Ichthyol. Piscat, 2007, 3: 47-53.

[31]

Regalado C, Garcia-Almendarez BE, Duarte-Vazquez MA. Biotechnological applications of peroxidases. Phytochem Rev, 2004, 3: 243-256.

[32]

Saleem R, Khurshid M, Ahmed S. Laccases, manganese peroxidases and xylanases used for the bio-bleaching of paper pulp: an environmental friendly approach. Protein peptide lett, 2018, 25: 180-186.

[33]

Sharma A, Parashar D, Satyanarayana T. Rampelotto PH. Acidophilic microbes: biology and applications. Biotechnology of extremophiles, grand challenges in biology and biotechnology, 2016, Switzerland: Springer International Publishing, 215-241.

[34]

Taboada-Puig R, Lu-Chau TA, Eibes G, Feijoo G, Moreira MT, Lema JM. Continuous removal of endocrine disruptors by versatile peroxidase using a two-stage system. Biotechnol Proc, 2015, 31: 908-916.

[35]

Tandon D, Sharma N. Isolation of potential novel cellulolytic and xylanolytic bacteria and optimization of their cultural conditions for enhanced production of cellulase and xylanase. J Agroaliment Proc Technol, 2014, 20: 231-240.

[36]

Taylor CR, Hardiman EM, Ahmad M, Sainsbury PD, Norris PR, Bugg TDH. Isolation of bacterial strains able to metabolize lignin from screening of environmental samples. J Appl Microbiol, 2012, 113(3): 521-530.

[37]

Tuncer M, Rob A, Ball AS, Wilson MT. Optimisation of extracellular lignocellulolytic enzyme production by a thermophilic actinomycete Thermomonospora fusca BD25. Enzym Microb Technol, 1999, 25: 38-47.

[38]

Unuofin JO, Okoh AI, Nwodo UU. Maize stover as a feedstock for enhanced laccase production by two gamma proteobacteria: a solution to agroindustrial waste stockpiling. Ind Crop Prod, 2019, 129: 611-623.

[39]

Wang FQ, Xie H, Chen W, Wang ET, Du FG, Song AD. Biological pretreatment of corn stover with ligninolytic enzyme for high efficient enzymatic hydrolysis. Bioresour Technol, 2013, 144: 572-578.

Funding

National Research Foundation, South Africa(95364)

South African Medical Research Council(UFH/P790)

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