An Extensive Review: Industrially Important Enzymes, their Classification and Depicting the Consortium of Industrial Applications
Asian Journal of Biotechnology and Genetic Engineering,
Microorganism has been used since the start of human society. Enzyme processing processes are quickly gaining the attention because of their short time of processing, cost effective, non-toxic, low energy input and environment friendly characters as well. Moreover, through protein engineering and recombinant DNA technology, a microorganism can be easily manipulated and cultured in large scale to meet increased demand in different sectors. Therapeutic enzymes have a huge variety of selective uses such as anticoagulants or thrombolytics, oncolytics and also as replacement for various metabolic deficiencies. Proteolytic enzymes are excellent anti-inflammatory agents. There are various factors that decrease the potential of microbial source enzymes, once we enter to medical sciences due to high molecular size of catalyst which stop their distribution within somatic cells. In industrial processes the quantity of enzymes should be high, while in therapeutic case the purity and specificity should be excellent, if the quantity level is less no matter. The kinetics of such enzymes is high and low so that it is maximally efficient even at low concentration of substrate and enzymes. The source of such enzymes should be designated with high care to minimize or prevent the chances of undesirable growth by mismatched material and also to enable ready purification.
- Industrial enzymes
How to Cite
Gurung N, Ray S, Bose S, Rai V. A broader view: microbial enzymes and their relevance in industries, medicine, and beyond. BioMed Research International; 2013.
Anastas PT, Bartlett LB, Kirchhoff MM, Williamson TC. The role of catalysis in the design, development, and implementation of green chemistry. Catalysis Today. 2000;55(1-2):11-22.
Singh R, Kumar M, Mittal A, Mehta PK. Microbial enzymes: industrial progress in 21st century. 3 Biotech. 2016;6(2): 1-15.
Almeida MG, Serra A, Silveira CM, Moura JJ. Nitrite biosensing via selective enzymes—a long but promising route. Sensors. 2010;10(12):11530- 11555.
Liu. Mass spectrometry-based strategies in protein higher order structure analysis: fast photochemical oxidation of proteins and hydrogen deuterium exchange. St. Louis, Missouri. 2015;1001:1.
Anbu P, Gopinath SC, Chaulagain BP, Tang TH, Citartan M. Microbial enzymes and their applications in industries and medicine 2014. In: Hindawi; 2015.
Bartlett GJ, Porter CT, Borkakoti N, Thornton JM. Analysis of catalytic residues in enzyme active sites. Journal of Molecular Biology. 2002;324(1): 105-121.
Kotera M, Okuno Y, Hattori M, Goto S, Kanehisa M. Computational assignment of the EC numbers for genomic-scale analysis of enzymatic reactions. Journal of the American Chemical Society. 2004;126(50):16487-16498.
Edner C, Li J, Albrecht T, Mahlow S, Hejazi M, Hussain H, Steup M. Glucan, water dikinase activity stimulates breakdown of starch granules by plastidial β-amylases. Plant Physiology. 2007;145(1):17-28.
Souza PMD. Application of microbial α-amylase in industry-A review. Brazilian Journal of Microbiology. 2010;41(4):850-861.
Sundarram A, Murthy TPK. α-amylase production and applications: a review. Journal of Applied & Environmental Microbiology. 2014;2(4):166-175.
Butterworth PJ, Warren FJ, Ellis PR. Human α‐amylase and starch digestion: An interesting marriage. Starch‐Stärke. 2011;63(7):395-405.
Guzmán‐Maldonado H, Paredes‐López O, Biliaderis CG. Amylolytic enzymes and products derived from starch: a review. Critical Reviews in Food Science & Nutrition. 1995;35(5):373-403.
Prakash O, Jaiswal N. α-Amylase: an ideal representative of thermostable enzymes. Applied Biochemistry and Biotechnology. 2010;160(8):2401-2414.
Ventosa A, Nieto J. Biotechnological applications and potentialities of halophilic microorganisms. World Journal of Microbiology and Biotechnology. 1995; 11(1):85-94.
Caton TM, Witte LR, Ngyuen H, Buchheim JA, Buchheim MA, Schneegurt MA. Halotolerant aerobic heterotrophic bacteria from the Great Salt Plains of Oklahoma. Microbial Ecology. 2004; 48(4):449-462.
Edbeib MF, Wahab RA, Huyop F. Halophiles: biology, adaptation, and their role in decontamination of hypersaline environments. World Journal of Microbiology and Biotechnology. 2016;32(8):1-23.
Kango N, Jana UK, Choukade R. Fungal enzymes: Sources and Biotechnological Applications. In Advancing Frontiers in Mycology & Mycotechnology. Springer. 2019;515-538.
Machida M, Asai K, Sano M, Tanaka T, Kumagai T, Terai G, Kashiwagi Y. Genome sequencing and analysis of Aspergillus oryzae. Nature. 2005;438(7071):1157-1161.
Hajar-Azhari S, Wan WAAQI, Ab Kadir S, Abd Rahim MH, Saari, N. Evaluation of a Malaysian soy sauce koji strain Aspergillus oryzae NSK for γ-aminobutyric acid (GABA) production using different native sugars. Food Science and Biotechnology. 2018; 27(2):479-488.
Djekrif-Dakhmouche S, Gheribi-Aoulmi Z, Meraihi Z, Bennamoun L. Application of a statistical design to the optimization of culture medium for α-amylase production by Aspergillus niger ATCC 16404 grown on orange waste powder. Journal of Food Engineering. 2006; 73(2):190-197.
Tiwari S, Srivastava R, Singh C, Shukla K, Singh R, Singh P, Sharma R. Amylases: an overview with special reference to alpha amylase. J Global Biosci. 2015;4:1886-1901.
Arreaza G, Devane WA, Omeir RL, Sajnani G, Kunz J, Cravatt BF, Deutsch DG. The cloned rat hydrolytic enzyme responsible for the breakdown of anandamide also catalyzes its formation via the condensation of arachidonic acid and ethanolamine. Neuroscience Letters. 1997;234(1):59-62.
Rahman NZRA, Basri M. New lipases and proteases: Nova Publishers; 2006.
Saini R, Saini HS, Dahiya A. Amylases: Characteristics and industrial applications. Journal of Pharmacognosy and Phytochemistry. 2017;6(4):1865- 1871.
Goodman BE. Insights into digestion and absorption of major nutrients in humans. Advances in Physiology Education. 2010;34(2):44-53.
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 Biochemistry. 2003; 38(10):1397-1403.
Pascoal A, Estevinho LM, Martins IM, Choupina AB. Novel sources and functions of microbial lipases and their role in the infection mechanisms. Physiological and Molecular Plant Pathology. 2018;104:119-126.
Gupta R, Gupta N, Rathi P. Bacterial lipases: an overview of production, purification and biochemical properties. Applied Microbiology and Biotechnology. 2004;64(6): 763-781.
Verma ML. Biotechnological applications of lipases in flavour and fragrance ester production. In Microbial Technology for the Welfare of Society. Springer. 2019; 1-24.
Mehta A, Bodh U, Gupta R. Fungal lipases: a review. Journal of Biotech Research. 2017;8.
Akoh CC, Lee GC, Shaw JF. Protein engineering and applications of Candida rugosa lipase isoforms. Lipids. 2004;39(6):513-526.
Vellard M. The enzyme as drug: application of enzymes as pharmaceuticals. Current Opinion in Biotechnology. 2003;14(4):444-450.
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