Microbial proteases and their applications

Abstract

Proteases (proteinases or peptidases) are a class of hydrolases that cleave peptide chains in proteins. Endopeptidases are a type of protease that hydrolyze the internal peptide bonds of proteins, forming shorter peptides; exopeptidases hydrolyze the terminal peptide bonds from the C-terminal or N-terminal, forming free amino acids. Microbial proteases are a popular instrument in many industrial applications. In this review, the classification, detection, identification, and sources of microbial proteases are systematically introduced, as well as their applications in food, detergents, waste treatment, and biotechnology processes in the industry fields. In addition, recent studies on techniques used to express heterologous microbial proteases are summarized to describe the process of studying proteases. Finally, future developmental trends for microbial proteases are discussed.

Endophyte-mediated enhancement of salt resistance in Arachis hypogaea L. by regulation of osmotic stress and plant defense-related genes

“…Intriguingly, our results underscore that TSB plays a pivotal role in facilitating the growth advantage of salt-tolerant peanuts in salt-stressed environments. Furthermore, we observed that genes related to amino acid metabolic pathways were significantly upregulated in peanuts treated with TSB under salt stress ( Figure 8A ), potentially aiding in preserving protein reserves in peanuts ( Ahmed et al, 2022 ; Song et al, 2023 ). Similarly, pathways such as glutathione metabolism, ascorbate, and aldarate metabolism exhibited upregulation in response to TSB treatment ( Figures 8A , B ).…”

Solid-State Fermentation Using Bacillus licheniformis-Driven Changes in Composition, Viability and In Vitro Protein Digestibility of Oilseed Cakes

“…The evaluation of protein digestibility is crucial for nutritional assessment in terms of the quality and bioavailability of feed products. Therefore, fermentation enhances in vitro protein digestibility possibly by Bacillus licheniformis proteolytic activity that can target plant-based proteins, thereby promoting hydrolysis, protein modification [70][71][72], and remediation of anti-nutritional factors such as trypsin inhibitors [19]. Some studies using lactic bacteria achieved 65-79% IVPD in hemp [73].…”

Production Optimization, Partial Characterization, and Gluten-Digesting Ability of the Acidic Protease from Clavispora lusitaniae PC3

“…The inoculated plates were incubated at 30 • C for 4 to 5 days. Yeasts showing a clear zone around the colonies were selected and, considered protease-positive [7,25].…”

“…Protease enzymes degrade proteins at different sites [5]. Proteases within clans and families can be classified as asparagine proteases, aspartic proteases, cysteine proteases, glutamic proteases, mixed proteases, metalloproteases, threonine proteases, serine proteases, or unknown proteases based on these phylogenetic relationships and mechanisms of action [6,7].…”

“…A variety of enzymes are used in place of chemicals, with microbial enzymesparticularly proteases-being used most frequently within industrial sectors for the production of food (particularly in cheese making). They are also used in detergents; paper and waste management strategies [7][8][9]; the pharmaceutical, textile, feather bioconversion, and leather industries [10,11]; silver recovery and silver extraction from cast-off X-ray films [12,13]; and medical sectors [1,14].…”