Abstract

 One of the main problems obstructed to the use of enzymes in industrial biotechnology is their improper stability under processing conditions. In the last decades, a lot of research has focused on the improvement of enzymes stability in the conditions in which they were to be used, and especially on thermal stability improvement. Long time ago different methods were suggested to enhance the enzyme stability. This review trying to explain the enzyme structure and the factors affecting its stability. also, tried to highlight and summarized most of these methods such as chemical modification, immobilization, and addition of various compounds. Also, give an overview of the recent progress in these methods.

Keywords: Enzyme; Chemicals; ^{Bacillus; Aspergillus}

References

1. de Bolster MWG. “Glossary of Terms Used in Bioinorganic Chemistry”. International Union of Pure and Applied Chemistry (1997).
2. Fisher Z., et al. “Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II”. Biochemistry 44 (2005): 1097-115.
3. Brenda et al. “The enzyme information system in 2007”. Barthelmes J., Ebeling C., Chang A., Schomburg I., Schomburg D., Nucleic Acids Research 35 (2007): D511-D514.
4. Mosbach K. (ed.). Methods in Enzymology. Academic Press, New York 44 (1976): 335- 353.
5. Mahajan RT and Badgujar SB. “Biological aspects of proteolytic enzymes: A Review Mahajan and Badgujar”. Journal of Pharmacy Research 3 (2010): 2048-2068.
6. Liu WQ., et al. “Alkaline unfolding and salt-induced folding of arginine kinase from shrimp Feneropenaeus chinensis under high pH conditions”. International Journal of Biological Macromolecule 38 (2006): 211-215.
7. Prakash K., et al. “Molecular and Structural Biology Division, Central Drug Research Institute, Lucknow 226 001”. India Protein Science 11 (2002): 46-57.
8. Fágáin CÓ. “Enzyme stabilization-recent experimental progress”. Enzyme and Microbial Technology 33 (2003): 137-149.
9. Cho YK and Bailey JE. “Immobilization of enzymes on activated carbon: Properties of immobilized glucoamylase, glucose oxidase, and gluconolactonase”. Biotechnology and Bioengineering 166 (2004): 1651-166.
10. Horowitz BM and Falksen K. “Oxidative Inactivation of the Enzyme Rhodanese by Reduced Nicotinamide Adenine Dinucleotide”. 261 (1986): 16953-16956.
11. Häring D and Schreier P. “Cross-linked enzyme crystals”. Current Opinion in Chemical Biology 3 (1999): 35-38.
12. Brugger R., et al. “Thermostability engineering of fungal phytases using low-Mr additives and chemical crosslinking”. Biocatalysis and Biotransformation 19 (2001): 339-516.
13. Govardhan CP., “Crosslinking of enzymes for improved stability and performance”. Current Opinion in Biotechnology 10 (1999): 331-335.
14. Visuri K., et al. “Stability of native and crosslinked crystalline glucose isomerase”. Biotechnology and Bioengineering 64 (1999): 377-380.
15. Bieniarz C., et al. “Alkaline phosphatase activatable polymeric cross-linkers and their use in the stabilization of proteins”. Bioconjugate Chemistry 9 (1998): 390-398.
16. Mostafa FA and Abd El Aty AA. “Thermodynamics enhancement of Alternaria tenuissima KM651985 laccase by covalent coupling to polysaccharides and its applications”. International Journal of Biological Macromolecule 120 (2018) 222-229.
17. Clark D.S. “A new phase for protein chemistry”. Nature Chemistry 2 (2010): 607-608.
18. Khajeh K., et al. “Chemical modification of lysine residues in Bacillus amylases: effect on activity and stability”. Enzyme and Microbial Technology 28 (2001): 543-549
19. Schiavon O., et al. “Surface modification of enzymes for therapeutic use: monomethoxypoly (ethylene glycol) derivatization of ribonuclease”. Farmacology 46 (1991): 967-78.
20. Anjum F., et al. “Compatibility of osmolytes with Gibbs energy of stabilization of proteins”. Biochimica et Biophysica Acta 1476 (2000): 75-84.
21. Singer MA and Lindquist S. “Multiple effects of trehalose on protein folding in vitro and in vivo”. Molecular Cell 1 (1998): 639-648.
22. Baptista RP., et al. “Trehalose delays the reversible but not the irreversible thermal denaturation of cutinase”. Biotechnology and Bioengineering 70 (2000): 699-703.
23. Kaushik JK and Bhat R. “Thermal stability of proteins in aqueous polyol solutions. The Journal of Physical Chemistry 102 (1998): 7058-7066.
24. Andersson MM and Hatti-Kaul R. “Protein stabilizing effect of polyethyleneimine”. Journal of Biotechnology 72 (1999): 21-31.
25. Marcozzi G., et al. “Effects of Surfactants on the Stabilization of the Bovine Lactoperoxidase Activity”. Biotechnology Progress 14 (1998): 653−656.
26. Shimizu T., et al. “Characteristics of proteinaceous additives in stabilizing enzymes during freeze-thawing and -drying”. Bioscience, Biotechnology, andBiochemistry 81 (2017): 687-697.
27. Illanes A., et al. “Immobilization of lactase and invertase on crosslinked chitin”. In: Bioreactor Immobilized Enzymes and Cells (Moo-Young, M. ed.) Elsevier Applied Science, London, (1988): 233-249.
28. Mostafa FA., et al. “Immobilization of xylanase on modified grafted alginate polyethyleneimine bead based on impact of sodium cation effect”. International Journal of Biological Macromolecules 140 (2019): 1284-1295.
29. Karam EA., et al. “Production, immobilization, and thermodynamic studies of free and immobilized Aspergillus awamori amylase”. International Journal of Biological Macromolecules 102 (2017): 694-703.
30. Abd El Aty AA., et al. “Covalent immobilization of Alternaria tenuissima KM651985 laccase and some applied aspects”. Biocatalysis and Agricultural Biotechnology 9 (2017): 74-81.
31. Bickerstaf GF. “Impact of genetic technology on enzyme technology”. Genetic Engineeringand Biotechnology 15 (1995): 13-30.
32. Abdel Naby AM., et al. “Immobilisation of Bacillus subtilis œ-amylase.and characterization of its enzyme properties”. Microbial Research 153 (1998): 319-325.
33. Asuri P., et al. “Enhanced stability of enzymes adsorbed onto nanoparticles”. Journal of Nanoscience and Nanotechnology 7 (2007): 1675-1678.
34. Esawy MA., et al. “Evaluation of free and immobilized Aspergillus niger NRC1ami pectinase applicable in industrial processes”. Carbohydrate Polymers (2013): 1463-1469.
35. Mohy Eldin M. S., et al. “β-Galactosidase covalent immobilization on the surface of alginate beads and its application in lactose hydrolysis. Deutsche Lebensmittel-Rundschau 101. Jahrgang, Heft; 6 (2005): 255-259.
36. Brodeliu P. In Enzymes and Immobilized Cells in Biotechnology. Benjamin Cummings, London; (1985): 109-148.
37. Wang Y and Frank C. “Enzyme encapsulation in nanoporous silicaspheres”.Chemical Communications (2004): 1528-1529.
38. Cabral JMS and Kennedy JF. Covalent and coordination immobilization of proteins, in Protein Immobilization—Fundamentals and Applications - (Taylor, R F, ed) Marcel Dekker, New York; (1991): 73-138.
39. Gemeiner P. “Materials for enzyme engineering”. In Gemeiner P (ed) enzyme engineering. Ellis Horwood, New York (1992): 13-119.
40. Hashem AM., et al. “Covalent immobilization of Enterococcus faecalis Esawy dextransucrase and dextran synthesis”. International Journal of Biological Macromolecules 82 (2016): 905-912.‏

41.                Elnashar MM., et al. “Optimal Immobilization of β-Galactosidase onto κ-Carrageenan Gel Beads Using Response Surface Methodology and Its Applications”. The Scientific World Journal (2014).

42. Aguiar‐Oliveira E., et al. “Effects of the Addition of Substrate and Salts in Both the Fructosyltransferase Immobilization and Its Catalytic Properties”. Journal of Food Biochemistry 37: (2013).
43. Klibanov AM. “Improving enzymes by using them in organic solvents”. Nature 409 (2001): 241-246.
44. Santucci R., et al. “ Effect of dimethyl sulfoxide on the structure and the functional properties of horseradish peroxidase as observed by spectroscopy and cyclic voltammetry’. Biochimica et Biophysica Acta 1596 (2002) :225-333.
45. Sears P., et al. “ The effect of counterion, water concentration and stirring on the stability of subtilisin BPN in organic solvents”. Journal of Molecular Catalysis B: Enzymatic 6 (1999): 297-304.
46. Lozano P and Combes D. “Effect of alkali halides on -chymotrypsin activity in the plastein reaction”. Journal of the Science of Food and Agriculture 62 (1993): 245-252.
47. Bryan PN. “Protein engineering of subtilisin”. Biochimica et Biophysica Acta 1543 (2000) :203-222.
48. Labrou NE. “Random mutagenesis methods for in vitro directed enzyme evolution”. Current Protein and Peptide Science 11 (2010): 91-100.
49. Cherry JR., et al. “Directed evolution of a fungal peroxidase”. Nature Biotechnology 17 (1999): 379-384.
50. Robertson AL and Bottomley S. “A Method for the Incremental Expansion of Polyglutamine Repeats in Recombinant Proteins”. Methods In Molecular Biology > Book: Tandem Repeats in Genes, Proteins, and Disease (2013).

Citation

Citation: Mona Abdeltawab Esawy and Bassem Mahmoud Salama. “Recent Approaches against SARS-COV-2: The Ongoing Outbreak of Coronavirus Disease 2019 (COVID-19)". Acta Scientific Microbiology 3.8 (2020): 98-111.

Copyright

Copyright: © 2020 Mona Abdeltawab Esawy and Bassem Mahmoud Salama. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.