Understanding the Basis of Occurrence, Biosynthesis, and Implications of Thermostable Alkaline Proteases

The group of hydrolytic enzymes synonymously known as proteases is predominantly most favored for the class of industrial enzymes. The present work focuses on the thermostable nature of these proteolytic enzymes that occur naturally among mesophilic and thermophilic microbes. The broad thermo-active...

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Published inApplied biochemistry and biotechnology Vol. 193; no. 12; pp. 4113 - 4150
Main Authors Arya, Prashant S., Yagnik, Shivani M., Rajput, Kiransinh N., Panchal, Rakeshkumar R., Raval, Vikram H.
Format Journal Article
LanguageEnglish
Published New York Springer US 01.12.2021
Springer Nature B.V
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Summary:The group of hydrolytic enzymes synonymously known as proteases is predominantly most favored for the class of industrial enzymes. The present work focuses on the thermostable nature of these proteolytic enzymes that occur naturally among mesophilic and thermophilic microbes. The broad thermo-active feature (40–80 °C), ease of cultivation, maintenance, and bulk production are the key features associated with these enzymes. Detailing of contemporary production technologies, and controllable operational parameters including the purification strategies, are the key features that justify their industrial dominance as biocatalysts. In addition, the rigorous research inputs by protein engineering and enzyme immobilization studies add up to the thermo-catalytic features and application capabilities of these enzymes. The work summarizes key features of microbial proteases that make them numero-uno for laundry, biomaterials, waste management, food and feed, tannery, and medical as well as pharmaceutical industries. The quest for novel and/or designed and engineered thermostable protease from unexplored sources is highly stimulating and will address the ever-increasing industrial demands.
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ISSN:0273-2289
1559-0291
DOI:10.1007/s12010-021-03701-x