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

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Abstract

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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Acknowledgements

Authors P. A. and R. V. kindly acknowledge the financial assistance and research grants under the “SHODH – Scheme of Developing High-Quality Research” fellowship by Department of Higher Education, Government of Gujarat Ref No: 201901380034 and UGC-BSR Start-Up Research Grant No.F.30-521/2020 by University Grants Commission, Government of India. The infrastructural support at the Department of Microbiology & Biotechnology, Gujarat University, Ahmedabad, is heartily acknowledged.

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    Prashant S. Arya, Shivani M. Yagnik, Kiransinh N. Rajput, Rakeshkumar R. Panchal & Vikram H. Raval

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Arya, P.S., Yagnik, S.M., Rajput, K.N. et al. Understanding the Basis of Occurrence, Biosynthesis, and Implications of Thermostable Alkaline Proteases. Appl Biochem Biotechnol 193, 4113–4150 (2021). https://doi.org/10.1007/s12010-021-03701-x

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