Optimization of production of an oxidant and detergent-stable alkaline β-keratinase from Brevibacillus sp. strain AS-S10-II: Application of enzyme in laundry detergent formulations and in leather industry

Enzymatic activity of circular sortase A under denaturing conditions: An advanced tool for protein ligation

“…These techniques facilitate the NMR analyses of large proteins because the partial labeling of the molecule prevents signal overlap on the obtained spectra while still enabling the study of the structure of the domains in their natural surroundings within a multi-subunit molecule [3,4]. Various large multi-domain enzymes, e.g., ␣-amylases, ␤-keratinases, or cellulases, are of a great interest because they can be efficiently used in industry [5][6][7]. Thus, structural studies of such enzymes in solution, e.g., via NMR, are crucial for a better understanding of the key mechanisms and processes of substrate recognition.…”

Understanding the Regioselective Hydrolysis of Human Serum Albumin by Zr(IV)-Substituted Polyoxotungstates Using Tryptophan Fluorescence Spectroscopy

“…For instance, protein hydrolysis is of prime importance for a broad range of proteomics techniques ranging from protein sequencing to protein identification [3][4][5]. Moreover, efficient and selective protein hydrolysis is also highly used in the food industry [6], leather processing [7], the cleaning industry [8] and medicine [9]. These applications demand the use of reagents that are on the one hand capable of hydrolyzing the extremely inert peptide bond, and achieving this reactivity in a highly selective manner on the other hand.…”

Keratin Degrading Microbial Keratinase as a Tool for Bioremediation

“…Literature survey shows that alkaline proteases, in general keratinase known as "green chemicals" have made their way as key-ingredient in detergent formulations as well [13]. They are used as additives for cleaning up of drains clogged with keratinase wastes and also to improve the wash performance of enzymebased laundry detergents [14].…”