Research Progress Based on SpyTag/SpyCatcher Self-Assembling Peptides and Their Applications in the Food Field

Meng-meng Cai , Zi-fu Ni , Zhong-ke Sun , Xiao-long Li , Zi-hao Wang , Min Zhang , Cheng-wei Li

Food Bioengineering ›› 2025, Vol. 4 ›› Issue (3) : 279 -291.

PDF
Food Bioengineering ›› 2025, Vol. 4 ›› Issue (3) :279 -291. DOI: 10.1002/fbe2.70023
REVIEW ARTICLE
Research Progress Based on SpyTag/SpyCatcher Self-Assembling Peptides and Their Applications in the Food Field
Author information +
History +
PDF

Abstract

The SpyTag/SpyCatcher system is a modular protein assembly tool based on isopeptide bond-mediated covalent conjugation, distinguished by mild reaction conditions, rapid ligation rate, and independence from exogenous enzymes or chemical reagents. Owing to its high efficiency, orthogonality, and stability, it has exhibited multi-dimensional application value in the food sector, enabling the enhancement of enzyme stability and reusability in food enzyme engineering, efficient product synthesis and metabolic optimization in microbial fermentation, high-sensitivity recognition of mycotoxins in detection, as well as toxin degradation and antimicrobial film construction in preservation packaging. Despite challenges such as large-scale production and safety evaluation, future advancements through molecular design optimization and interdisciplinary technology integration are expected to accelerate the development of the food industry, providing revolutionary solutions for green processing and food safety.

Keywords

covalent coupling / enzyme engineering / food processing / self-assembly / SpyTag/SpyCatcher

Cite this article

Download citation ▾
Meng-meng Cai, Zi-fu Ni, Zhong-ke Sun, Xiao-long Li, Zi-hao Wang, Min Zhang, Cheng-wei Li. Research Progress Based on SpyTag/SpyCatcher Self-Assembling Peptides and Their Applications in the Food Field. Food Bioengineering, 2025, 4(3): 279-291 DOI:10.1002/fbe2.70023

登录浏览全文

4963

注册一个新账户 忘记密码

References

[1]

Anderson, G. P., J. L. Liu, L. C. Shriver-Lake, et al. 2019. “Oriented Immobilization of Single-Domain Antibodies Using SpyTag/SpyCatcher Yields Improved Limits of Detection.” Analytical Chemistry 91, no. 15: 9424–9429. https://doi.org/10.1021/acs.analchem.9b02096.

[2]

Bai, J., Y. Wang, W. Li, et al. 2025. “Development of a Self-Assembled Dual-Enzyme Co-Display Platform on the Surface of the Natural “Chitosan Beads” of Yeast Spores.” International Journal of Biological Macromolecules 286: 138308. https://doi.org/10.1016/j.ijbiomac.2024.138308.

[3]

Bhatwa, A., W. Wang, Y. I. Hassan, N. Abraham, X. Z. Li, and T. Zhou. 2021. “Challenges Associated With the Formation of Recombinant Protein Inclusion Bodies in Escherichia coli and Strategies to Address Them for Industrial Applications.” Frontiers in Bioengineering and Biotechnology 9: 630551. https://doi.org/10.3389/fbioe.2021.630551.

[4]

Bintsis, T. 2018. “Microbial Pollution and Food Safety.” AIMS Microbiology 4, no. 3: 377–396. https://doi.org/10.3934/microbiol.2018.3.377.

[5]

Cai, C., Y. Xia, Y. Guo, et al. 2025. “Biosynthetic Small Molecule Antigens Mimics Medicated Lateral Flow Immunoassay for Mycotoxin Fumonisin B(1) Using Nanobody Fusion Proteins.” Journal of Hazardous Materials 487: 137194. https://doi.org/10.1016/j.jhazmat.2025.137194.

[6]

Caparco, A. A., D. R. Dautel, and J. A. Champion. 2022. “Protein Mediated Enzyme Immobilization.” Small 18, no. 19: e2106425. https://doi.org/10.1002/smll.202106425.

[7]

Chen, H., X. Wang, H. Ge, et al. 2025. “RmZHD Surface-Displayed Escherichia coli for High Efficiency and Low-Cost Degradation of Zearalenone.” ACS Applied Bio Materials 8, no. 4: 3127–3134. https://doi.org/10.1021/acsabm.4c01994.

[8]

Chen, H., T. Zhou, S. Li, et al. 2023. “Living Magnetotactic Microrobots Based on Bacteria With a Surface-Displayed CRISPR/Cas12a System for Penaeus Viruses Detection.” ACS Applied Materials & Interfaces 15, no. 41: 47930–47938. https://doi.org/10.1021/acsami.3c09690.

[9]

Conte, M. P., K. H. A. Lau, and R. V. Ulijn. 2017. “Biocatalytic Self-Assembly Using Reversible and Irreversible Enzyme Immobilization.” ACS Applied Materials & Interfaces 9, no. 4: 3266–3271. https://doi.org/10.1021/acsami.6b13162.

[10]

C.t, M. K., S. S., S. K. M.h., L. N. N., and J. R. K. 2024. “Preparation of Nano-Immobilised β-galactosidase Using Mesoporous Silicon Dioxide Nanoparticles and Its Efficiency in Production of Galactooligosaccharides.” International Dairy Journal 150: 105847. https://doi.org/10.1016/j.idairyj.2023.105847.

[11]

Du, C., S. Tan, L. Liu, Y. Zhou, P. Wu, and G. Zhang. 2023. “Correction to: Improving the Specific Activity and Stability of Alkaline Pectinase PEL3 Through Spytag/Spycatcher Cyclization.” Biotechnology Letters 45, no. 9: 1245–1247. https://doi.org/10.1007/s10529-023-03409-4.

[12]

Fierer, J. O., O. E. Tovar-Herrera, J. Y. Weinstein, et al. 2023. “Affinity-Induced Covalent Protein-Protein Ligation via the SpyCatcher-SpyTag Interaction.” Green Carbon 1, no. 1: 33–42. https://doi.org/10.1016/j.greenca.2023.07.001.

[13]

Gao, S., W. Yang, X. Zheng, et al. 2025. “Advances of Nanobody-Based Immunosensors for Detecting Food Contaminants.” Trends in Food Science & Technology 156: 104871. https://doi.org/10.1016/j.tifs.2025.104871.

[14]

Gao, X., C. Wei, H. Qi, C. Li, F. Lu, and H. M. Qin. 2023. “Directional Immobilization of D-Allulose 3-epimerase Using SpyTag/SpyCatcher Strategy as a Robust Biocatalyst for Synthesizing D-Allulose.” Food Chemistry 401: 134199. https://doi.org/10.1016/j.foodchem.2022.134199.

[15]

Guicherd, M., M. Ben Khaled, M. Guéroult, et al. 2024. “An Engineered Enzyme Embedded Into PLA to Make Self-Biodegradable Plastic.” Nature 631, no. 8022: 884–890. https://doi.org/10.1038/s41586-024-07709-1.

[16]

Guo, C., X. Guo, X. Li, et al. 2024. “The Spycatcher-Spytag Interaction Mediates Tunable Anti-Tumor Cytotoxicity of NK Cells.” Molecular Immunology 165: 11–18. https://doi.org/10.1016/j.molimm.2023.12.001.

[17]

Han, M., C. Xu, B. Guan, et al. 2022. “Enhanced Thermal Stability of the β-galactosidase BgaB From Bacillus Circulans by Cyclization Mediated via Spytag/Spycatcher Interaction and Its Use in Galacto-Oligosaccharides Synthesis.” International Journal of Biological Macromolecules 222, no. Pt B: 2341–2352. https://doi.org/10.1016/j.ijbiomac.2022.10.021.

[18]

Hatlem, D., T. Trunk, D. Linke, and J. C. Leo. 2019. “Catching a SPY: Using the SpyCatcher-SpyTag and Related Systems for Labeling and Localizing Bacterial Proteins.” International Journal of Molecular Sciences 20, no. 9: 2129. https://doi.org/10.3390/ijms20092129.

[19]

Hu, M., T. Bao, Z. Qin, et al. 2025. “Programmable Scaffold-Mediated Assembly Regulation Tool for Dynamic Control of a Multienzyme Biocatalyst.” ACS Catalysis 15, no. 3: 2236–2249. https://doi.org/10.1021/acscatal.4c05420.

[20]

Jia, M., Z. Luo, H. Chen, et al. 2022. “Programmable Polyproteams of Tyrosine Ammonia Lyases as Cross-Linked Enzymes for Synthesizing p-Coumaric Acid.” Biomolecules 12, no. 7: 997. https://doi.org/10.3390/biom12070997.

[21]

Kamboj, S., N. Gupta, J. D. Bandral, G. Gandotra, and N. Anjum. 2020. “Food Safety and Hygiene: A Review.” International Journal of Chemical Studies 8, no. 2: 358–368. https://doi.org/10.22271/chemi.2020.v8.i2f.8794.

[22]

Kang, H. J., and E. N. Baker. 2011. “Intramolecular Isopeptide Bonds: Protein Crosslinks Built for Stress?” Trends in Biochemical Sciences 36, no. 4: 229–237. https://doi.org/10.1016/j.tibs.2010.09.007.

[23]

Kang, W., T. Ma, M. Liu, et al. 2019. “Modular Enzyme Assembly for Enhanced Cascade Biocatalysis and Metabolic Flux.” Nature Communications 10, no. 1: 4248. https://doi.org/10.1038/s41467-019-12247-w.

[24]

Katsura, M., M. Fukushima, K. Kameyama, T. Kokuho, Y. Nakahira, and K. Takeuchi. 2023. “Novel Bovine Viral Diarrhea Virus (BVDV) Virus-Like Particle Vaccine Candidates Presenting the E2 Protein Using the SpyTag/SpyCatcher System Induce a Robust Neutralizing Antibody Response in Mice.” Archives of Virology 168, no. 2: 49. https://doi.org/10.1007/s00705-022-05653-x.

[25]

Keeble, A. H., A. Banerjee, M. P. Ferla, S. C. Reddington, I. N. A. K. Anuar, and M. Howarth. 2017. “Evolving Accelerated Amidation by SpyTag/SpyCatcher to Analyze Membrane Dynamics.” Angewandte Chemie International Edition 56, no. 52: 16521–16525. https://doi.org/10.1002/anie.201707623.

[26]

Keeble, A. H., and M. Howarth. 2020. “Power to the Protein: Enhancing and Combining Activities Using the Spy Toolbox.” Chemical Science 11, no. 28: 7281–7291. https://doi.org/10.1039/d0sc01878c.

[27]

Keeble, A. H., P. Turkki, S. Stokes, et al. 2019. “Approaching Infinite Affinity Through Engineering of Peptide–Protein Interaction.” Proceedings of the National Academy of Sciences of the United States of America 116, no. 52: 26523–26533. https://doi.org/10.1073/pnas.1909653116.

[28]

Koklu, A., S. Wustoni, K. Guo, et al. 2022. “Convection Driven Ultrarapid Protein Detection via Nanobody-Functionalized Organic Electrochemical Transistors.” Advanced Materials 34, no. 35: e2202972. https://doi.org/10.1002/adma.202202972.

[29]

Krishnan, N., Y. Jiang, J. Zhou, et al. 2024. “A Modular Approach to Enhancing Cell Membrane-Coated Nanoparticle Functionality Using Genetic Engineering.” Nature Nanotechnology 19, no. 3: 345–353. https://doi.org/10.1038/s41565-023-01533-w.

[30]

Li, D., H. Zhang, L. Yang, et al. 2020. “Surface Display of Classical Swine Fever Virus E2 Glycoprotein on Gram-Positive Enhancer Matrix (GEM) Particles Via the SpyTag/SpyCatcher System.” Protein Expression and Purification 167: 105526. https://doi.org/10.1016/j.pep.2019.105526.

[31]

Li, L., J. O. Fierer, T. A. Rapoport, and M. Howarth. 2014. “Structural Analysis and Optimization of the Covalent Association Between SpyCatcher and a Peptide Tag.” Journal of Molecular Biology 426, no. 2: 309–317. https://doi.org/10.1016/j.jmb.2013.10.021.

[32]

Lisboa, H. M., M. B. Pasquali, A. I. dos Anjos, et al. 2024. “Innovative and Sustainable Food Preservation Techniques: Enhancing Food Quality, Safety, and Environmental Sustainability.” 16(18): 8223. https://doi.org/10.3390/su16188223.

[33]

Liyanagedera, S. B. W., J. Williams, J. P. Wheatley, et al. 2024. “Directional Immobilisation of SpyTag Bacteriophage on PDMS Surfaces for Phage Based Microfluidics.” bioRxiv : 2024-10. https://doi.org/10.1101/2024.10.11.617866.

[34]

Ma, X., S. Xing, X. Liu, et al. 2025. “A Customized Multienzyme Cascade Immobilization System for Efficiently Biosynthesizing Allitol.” Food Bioscience 68: 106578. https://doi.org/10.1016/j.fbio.2025.106578.

[35]

Ma, Y., J. Miao, Q. Chen, H. Sun, Y. Chang, and H. Luo. 2025. “SpyTag/SpyCatcher-Mediated Spyring Cyclization Improves the Operational Stability and Renaturation Efficiency of Immobilized Enzymes After Catalytic Inactivation.” Process Biochemistry 156: 93–103. https://doi.org/10.1016/j.procbio.2025.05.017.

[36]

Mazzitelli, C., T. Maravic, E. Mancuso, et al. 2022. “Influence of the Activation Mode on Long-Term Bond Strength and Endogenous Enzymatic Activity of Dual-Cure Resin Cements.” Clinical Oral Investigations 26, no. 2: 1683–1694. https://doi.org/10.1007/s00784-021-04141-x.

[37]

Motta, J. F. G., B. C. B. d Freitas, A. F. d Almeida, G. A. S. Martins, and S. V. Borges. 2023. “Use of Enzymes in the Food Industry: A Review.” Food Science and Technology 43: e106222. https://doi.org/10.1590/fst.106222.

[38]

Ni, Z. F., N. Li, P. Xu, Z. W. Guo, M. H. Zong, and W. Y. Lou. 2022. “Enhancement of Thermostability and Catalytic Properties of Ammonia Lyase Through Disulfide Bond Construction and Backbone Cyclization.” International Journal of Biological Macromolecules 219: 804–811. https://doi.org/10.1016/j.ijbiomac.2022.07.213.

[39]

Ölçücü, G., O. Klaus, K.-E. Jaeger, et al. 2021. “Emerging Solutions for In Vivo Biocatalyst Immobilization: Tailor-Made Catalysts for Industrial Biocatalysis.” ACS Sustainable Chemistry & Engineering 9, no. 27: 8919–8945. https://doi.org/10.1021/acssuschemeng.1c02045.

[40]

Oloketuyi, S., R. Bernedo, A. Christmann, et al. 2021. “Native Llama Nanobody Library Panning Performed by Phage and Yeast Display Provides Binders Suitable for C-Reactive Protein Detection.” Biosensors 11, no. 12: 496. https://doi.org/10.3390/bios11120496.

[41]

Pinheiro, B., A. C. Moura, P. Oliveira, J. E. Azevedo, A. do Vale, and N. M. S. dos Santos. 2025. “Exploring Protein-Protein Ligation Approaches for the Cytosolic Delivery of Antigens Using AIP56.” Frontiers in Cellular and Infection Microbiology 15: 1596550. https://doi.org/10.3389/fcimb.2025.1596550.

[42]

Plavec, T. V., and A. Berlec. 2019. “Surface Anchoring on Lactococcus Lactis by Covalent Isopeptide Bond.” Acta Chimica Slovenica 66, no. 1: 18–27. https://doi.org/10.17344/acsi.2018.4422.

[43]

Pradanas-González, F., B. Glahn-Martínez, E. Benito-Peña, H. O. Arola, T. K. Nevanen, and M. C. Moreno-Bondi. 2022. “Molecular Super-Gluing: A Straightforward Tool for Antibody Labelling and Its Application to Mycotoxin Biosensing.” Analytical and Bioanalytical Chemistry 414, no. 18: 5373–5384. https://doi.org/10.1007/s00216-021-03841-3.

[44]

Qu, Z., L. Xu, F. Jiang, Y. Liu, and W. B. Zhang. 2024. “Folds From Fold: Exploring Topological Isoforms of a Single-Domain Protein.” Proceedings of the National Academy of Sciences 121, no. 43: e2407355121. https://doi.org/10.1073/pnas.2407355121.

[45]

Reddington, S. C., and M. Howarth. 2015. “Secrets of a Covalent Interaction for Biomaterials and Biotechnology: SpyTag and SpyCatcher.” Current Opinion in Chemical Biology 29: 94–99. https://doi.org/10.1016/j.cbpa.2015.10.002.

[46]

Robescu, M. S., and T. Bavaro. 2025. “A Comprehensive Guide to Enzyme Immobilization: All You Need to Know.” Molecules 30, no. 4: 939. https://doi.org/10.3390/molecules30040939.

[47]

Schoene, C., S. P. Bennett, and M. Howarth. 2016. “SpyRings Declassified: A Blueprint for Using Isopeptide-Mediated Cyclization to Enhance Enzyme Thermal Resilience.” Methods in Enzymology 580: 149–167. https://doi.org/10.1016/bs.mie.2016.05.004.

[48]

Shah, Y. A., S. Bhatia, A. Al-Harrasi, et al. 2023. “Mechanical Properties of Protein-Based Food Packaging Materials.” Polymers 15, no. 7: 1724. https://doi.org/10.3390/polym15071724.

[49]

Shen, X., S. Tang, Q. Xu, H. Huang, and L. Jiang. 2019. “SpyCatcher/SpyTag-Mediated Self-Assembly of a Supramolecular Complex for Improved Biocatalytic Production of Trehalose.” Applied Biochemistry and Microbiology 55, no. 6: 596–602. https://doi.org/10.1134/S0003683819060115.

[50]

Shen, Z., Y. Pan, Y. Liu, H. Song, and C. Xu. 2024. “Construction of Chitinase Complexes Using Self-Assembly Systems for Efficient Hydrolysis of Chitin.” ACS Synthetic Biology 13, no. 12: 4143–4153. https://doi.org/10.1021/acssynbio.4c00613.

[51]

Song, J. E., W. S. Song, S. Y. Yeo, H. R. Kim, and S. H. Lee. 2017. “Covalent Immobilization of Enzyme on Aminated Woven Poly (Lactic Acid) Via Ammonia Plasma: Evaluation of the Optimum Immobilization Conditions.” Textile Research Journal 87, no. 10: 1177–1191. https://doi.org/10.1177/0040517516648514.

[52]

Steinmann, B., A. Christmann, T. Heiseler, J. Fritz, and H. Kolmar. 2010. “In Vivo Enzyme Immobilization by Inclusion Body Display.” Applied and Environmental Microbiology 76, no. 16: 5563–5569. https://doi.org/10.1128/aem.00612-10.

[53]

Sun, X., T. Zhang, Y. Liu, et al. 2024. “Self-Assembled Multienzyme Complex Facilitates Synthesis of Glucosylglycerol From Maltodextrin and Glycerol.” Journal of the Science of Food and Agriculture 104, no. 1: 266–272. https://doi.org/10.1002/jsfa.12907.

[54]

Veggiani, G., T. Nakamura, M. D. Brenner, et al. 2016. “Programmable Polyproteams Built Using Twin Peptide Superglues.” Proceedings of the National Academy of Sciences 113, no. 5: 1202–1207. https://doi.org/10.1073/pnas.1519214113.

[55]

Venning-Slater, M., D. O. Hooks, and B. H. A. Rehm. 2014. “In Vivo Self-Assembly of Stable Green Fluorescent Protein Fusion Particles and Their Uses in Enzyme Immobilization.” Applied and Environmental Microbiology 80, no. 10: 3062–3071. https://doi.org/10.1128/aem.00323-14.

[56]

Wang, B. P., X. Yin, M. Y. Huang, et al. 2024. “A Self-Assembling γPFD-SpyCatcher Hydrogel Scaffold for the Coimmobilization of SpyTag-Enzymes to Facilitate the Catalysis of Regulated Enzymes.” Journal of Agricultural and Food Chemistry 72, no. 36: 19940–19947. https://doi.org/10.1021/acs.jafc.4c03403.

[57]

Wang, D., X. Fu, J. Gao, X. Zhao, and W. Bai. 2024. “Enhancing Poly-γ-glutamic Acid Production in Bacillus Tequilensis BL01 Through a Multienzyme Assembly Strategy and Expression Features of Glutamate Synthesis From Corynebacterium Glutamicum.” Journal of Agricultural and Food Chemistry 72, no. 15: 8674–8683. https://doi.org/10.1021/acs.jafc.4c00685.

[58]

Wang, H., H. Chen, Q. Li, et al. 2022. “Enhancing the Thermostability of Transglutaminase From Streptomyces Mobaraensis Based on the Rational Design of a Disulfide Bond.” Protein Expression and Purification 195–196: 106079. https://doi.org/10.1016/j.pep.2022.106079.

[59]

Wang, Q., J. Yang, W. Cao, H. Liu, and C. Li. 2025. “Engineering Robust β-Glucuronidase Via Protein Assembly and Immobilization for Enhanced Glycyrrhizin Hydrolysis.” Biochemical Engineering Journal 221: 109772. https://doi.org/10.1016/j.bej.2025.109772.

[60]

Wang, Z., M. Hu, M. Fang, et al. 2022. “Heterologous Expression of Thermotolerant α-Glucosidase in Bacillus subtilis 168 and Improving Its Thermal Stability by Constructing Cyclized Proteins.” 8(10): 498. https://doi.org/10.3390/fermentation8100498.

[61]

Wei, B., Y. Kang, Y. Zhao, H. Xu, and H. Liang. 2024. “Rational Design of Spontaneous Self-Cyclization Enzymes In Vivo and In Vitro With Improved Thermal Tolerance and Activity.” ACS Catalysis 14, no. 7: 5469–5480. https://doi.org/10.1021/acscatal.4c00056.

[62]

Wolf, S., J. Becker, Y. Tsuge, et al. 2021. “Advances in Metabolic Engineering of Corynebacterium Glutamicum to Produce High-Value Active Ingredients for Food, Feed, Human Health, and Well-Being.” Essays in Biochemistry 65, no. 2: 197–212. https://doi.org/10.1042/ebc20200134.

[63]

Wu, S., J. Xu, W. Chen, et al. 2024. “Protein Nanoscaffold Enables Programmable Nanobody-Luciferase Immunoassembly for Sensitive and Simultaneous Detection of Aflatoxin B1 and Ochratoxin A.” Journal of Hazardous Materials 462: 132701. https://doi.org/10.1016/j.jhazmat.2023.132701.

[64]

Xu, C., Q. Xu, H. Huang, and L. Jiang. 2018. “Enhancing the Stability of Trehalose Synthase Via SpyTag/SpyCatcher Cyclization to Improve Its Performance in Industrial Biocatalysts.” Bioscience, Biotechnology, and Biochemistry 82, no. 9: 1473–1479. https://doi.org/10.1080/09168451.2018.1475212.

[65]

Yang, W., H. Sun, Z. Cui, et al. 2024. “Spatially Sequential Co-Immobilization of Phosphorylases in Tiny Environments and Its Application in the Synthesis of Glucosyl Glycerol.” International Journal of Biological Macromolecules 279: 135139. https://doi.org/10.1016/j.ijbiomac.2024.135139.

[66]

Zakeri, B., J. O. Fierer, E. Celik, et al. 2012. “Peptide Tag Forming a Rapid Covalent Bond to a Protein, Through Engineering a Bacterial Adhesin.” Proceedings of the National Academy of Sciences 109, no. 12: E690–E697. https://doi.org/10.1073/pnas.1115485109.

[67]

Zhai, H., L. Cui, Z. Xiong, Q. Qi, and J. Hou. 2022. “Crispr-Mediated Protein-Tagging Signal Amplification Systems for Efficient Transcriptional Activation and Repression in Saccharomyces cerevisiae.” Nucleic Acids Research 50, no. 10: 5988–6000. https://doi.org/10.1093/nar/gkac463.

[68]

Zhang, G., M. B. Quin, and C. Schmidt-Dannert. 2018. “Self-Assembling Protein Scaffold System for Easy In Vitro Coimmobilization of Biocatalytic Cascade Enzymes.” ACS Catalysis 8, no. 6: 5611–5620. https://doi.org/10.1021/acscatal.8b00986.

[69]

Zhang, S. 2017. “Discovery and Design of Self-Assembling Peptides.” Interface Focus 7, no. 6: 20170028. https://doi.org/10.1098/rsfs.2017.0028.

[70]

Zhang, S. 2020. “Self-Assembling Peptides: From a Discovery in a Yeast Protein to Diverse Uses and Beyond.” Protein Science 29, no. 11: 2281–2303. https://doi.org/10.1002/pro.3951.

[71]

Zhou, Y. B., J. W. Cao, X. B. Sun, et al. 2020. “Enhanced Stability of a Rumen-Derived Xylanase Using Spytag/Spycatcher Cyclization.” World Journal of Microbiology and Biotechnology 36, no. 2: 33. https://doi.org/10.1007/s11274-020-2809-4.

RIGHTS & PERMISSIONS

2025 The Author(s). Food Bioengineering published by John Wiley & Sons Australia, Ltd. on behalf of State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology.

PDF

4

Accesses

0

Citation

Detail

Sections
Recommended

/