Research Progress on Improving the Performance of Natural Enzymes with Catalytic Activity

DOI: https://doi.org/10.62517/jnse.202417214

Author(s)

Renjie Li1, Linyu Qu2, Yuqi Feng1, Jinchao Hu1, Yufei Mao2, Qixuan Liu2, Qijia Jiang2, Jie Huang1,*

Affiliation(s)

1College of Packaging and Material Engineering, Hunan University of Technology, Zhuzhou, Hunan, China 2Technical College, Hunan University of Technology, Zhuzhou, Hunan, China *Corresponding Author.

Abstract

Enzyme modification technology can improve the catalytic activity and stability of enzymes, making them more suitable for use in the medical testing industry. This article focuses on seven molecular chemical modification methods, including small molecule chemical modification, polymer modification, enzyme cross-linking modification, and cofactor modification, as well as three genetic engineering modification methods, including directed evolution and site-specific mutation modification. The development prospects of enzyme modification technology are also discussed.

Keywords

Enzyme; Chemical Modification; Genetic Engineering; Cofactor

References

[1] Karaki, N.; Aljawish, A.; Humeau, C.; Muniglia, L.; Jasniewski, J., Enzymatic modification of polysaccharides: Mechanisms, properties, and potential applications: A review. Enzyme and Microbial Technology 2016, 90, 1-18. [2] Punia Bangar, S.; Ashogbon, A. O.; Singh, A.; Chaudhary, V.; Whiteside, W. S., Enzymatic modification of starch: A green approach for starch applications. Carbohydrate Polymers 2022, 287, 119265. [3] Schmelter, T.; Wientjes, R.; Vreeker, R.; Klaffke, W., Enzymatic modifications of pectins and the impact on their rheological properties. Carbohydrate Polymers 2002, 47 (2), 99-108. [4] Herr, N.; Ratzka, J.; Lauterbach, L.; Lenz, O.; Ansorge-Schumacher, M. B., Stability enhancement of an O2-tolerant NAD+-reducing [NiFe]-hydrogenase by a combination of immobilisation and chemical modification. Journal of Molecular Catalysis B: Enzymatic 2013, 97, 169-174. [5] Gübitz, G. M.; Paulo, A. C., New substrates for reliable enzymes: enzymatic modification of polymers. Current Opinion in Biotechnology 2003, 14 (6), 577-582. [6] Liu, W.; Wang, P., Cofactor regeneration for sustainable enzymatic biosynthesis. Biotechnology Advances 2007, 25 (4), 369-384. [7] Zhang Yongshuai; Li Yuanzhao; Sun Junliang, research progress in enzyme modification. Food Industry Technology, 2014,35 (2), 4-7. [8] Habibi, Y., Key advances in the chemical modification of nanocelluloses. Chemical Society Reviews 2014, 43 (5), 1519-1542. [9] Xiong Yahong; Gao Jingzhong; Zheng Jianpeng, a study on the chemical modification method to improve laccase stability. Chemical Research and Applications 2011,23 (08), 985-990. [10] Distel, K. A.; Zhu, G.; Wang, P., Biocatalysis using an organic-soluble enzyme for the preparation of poly(lactic acid) in organic solvents. Bioresource Technology 2005, 96 (5), 617-623. [11] Ma Jianbiao, polymeric to enzyme, modification of antibody DNA, immobilization and its biomedical applications. Journal of Chemistry of Higher Education 1997,18 (7), 9-14. [12] Longo, M. A.; Combes, D., Thermostability of modified enzymes: a detailed study. Journal of Chemical Technology & Biotechnology 1999, 74 (1), 25-32. [13] Barbosa, O.; Torres, R.; Ortiz, C.; Fernandez-Lafuente, R., The slow-down of the CALB immobilization rate permits to control the inter and intra molecular modification produced by glutaraldehyde. Process Biochemistry 2012, 47 (5), 766-774. [14] Mogi, K.-i.; Nakajima, M., Selection of surfactant-modified lipases for interesterification of triglyceride and fatty acid. Journal of the American Oil Chemists’ Society 1996, 73 (11), 1505-1512. [15] Zeng Jun; Yang Guolong; Bi Yanlan; Sun Shangde; Zhang Jie, Span modified pig pancreatic lipase catalyzes camellia oil and linoleic acid in solvent-free system. Journal of Henan University of Technology: Natural Science Edition 2011,32 (1), 4-8. [16] Li Chunyi; Huang Zhulie, application of chemical modification in enzyme molecular modification. Biotechnology Bulletin 2011, (9), 5-8. [17] Aharoni, A.; Thieme, K.; Chiu, C. P. C.; Buchini, S.; Lairson, L. L.; Chen, H.; Strynadka, N. C. J.; Wakarchuk, W. W.; Withers, S. G., High-throughput screening methodology for the directed evolution of glycosyltransferases. Nature Methods 2006, 3 (8), 609-614. [18] Khumtaveeporn, K.; Ullmann, A.; Matsumoto, K.; Davis, B. G.; Jones, J. B., Expanding the utility of proteases in synthesis: broadening the substrate acceptance in non-coded amide bond formation using chemically modified mutants of subtilisin. Tetrahedron: Asymmetry 2001, 12 (2), 249-261.