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Biomolecules 2013, 3(3), 597-611; doi:10.3390/biom3030597

Microbial Enzymes with Special Characteristics for Biotechnological Applications

Biomedical Science Research Institute, University of Ulster, Coleraine BT52 1SA, UK
Received: 28 June 2013 / Revised: 6 August 2013 / Accepted: 15 August 2013 / Published: 23 August 2013
(This article belongs to the Special Issue Enzymes and Their Biotechnological Applications)
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This article overviews the enzymes produced by microorganisms, which have been extensively studied worldwide for their isolation, purification and characterization of their specific properties. Researchers have isolated specific microorganisms from extreme sources under extreme culture conditions, with the objective that such isolated microbes would possess the capability to bio-synthesize special enzymes. Various Bio-industries require enzymes possessing special characteristics for their applications in processing of substrates and raw materials. The microbial enzymes act as bio-catalysts to perform reactions in bio-processes in an economical and environmentally-friendly way as opposed to the use of chemical catalysts. The special characteristics of enzymes are exploited for their commercial interest and industrial applications, which include: thermotolerance, thermophilic nature, tolerance to a varied range of pH, stability of enzyme activity over a range of temperature and pH, and other harsh reaction conditions. Such enzymes have proven their utility in bio-industries such as food, leather, textiles, animal feed, and in bio-conversions and bio-remediations. View Full-Text
Keywords: microbial-enzymes; thermophilic; alkalophilic; thermostable; protease; keratinase; amylase; xylanase; laccase microbial-enzymes; thermophilic; alkalophilic; thermostable; protease; keratinase; amylase; xylanase; laccase
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Nigam, P.S. Microbial Enzymes with Special Characteristics for Biotechnological Applications. Biomolecules 2013, 3, 597-611.

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