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 feature (40-80 degrees 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.

Automated summary

Proteases, known as hydrolytic enzymes, are favored for industrial use due to their thermostable nature and broad thermo-active features. Their key characteristics include ease of cultivation, maintenance, and bulk production, along with advancements in production technologies and purification strategies, making them dominant in various industries such as laundry, biomaterials, waste management, food and feed, tannery, and medical and pharmaceutical industries. Rigorous research in protein engineering and enzyme immobilization studies further enhance their catalytic capabilities, meeting the increasing demands of industrial applications.