Abstract
Simple SummaryIn the current investigation, we describe the characteristic features of a novel Bacillus megaterium bacterium-derived protease with excellent thermostable enzyme activity under stringent alkaline conditions. The protease is highly compatible with various detergents and thus appears to be an eco-friendly additive for a variety of industrial applications.An increased need by the green industry for enzymes that can be exploited for eco-friendly industrial applications led us to isolate and identify a unique protease obtained from a proteolytic Bacillus megaterium-TK1 strain from a seawater source. The extracellular thermostable serine protease was processed by multiple chromatography steps. The isolated protease displayed a relative molecular weight (MW) of 33 kDa (confirmed by zymography), optimal enzyme performance at pH 8.0, and maximum enzyme performance at 70 °C with 100% substrate specificity towards casein. The proteolytic action was blocked by phenylmethylsulfonyl fluoride (PMSF), a serine hydrolase inactivator. Protease performance was augmented by several bivalent metal cations. The protease tolerance was studied under stringent conditions with different industrial dispersants and found to be stable with Surf Excel, Tide, or Rin detergents. Moreover, this protease could clean blood-stained fabrics and showed dehairing activity for cow skin with significantly reduced pollution loads. Our results suggest that this serine protease is a promising additive for various eco-friendly usages in both the detergent and leather industries.
Highlights
Proteases, known as peptidases, degrade proteins and peptides by hydrolyzing their peptide bonds, thereby producing shorter byproducts
We screened prawn- and artemia-rich marine water locations to isolate protease producing microbes that were stable at alkaline pH and high temperature
The proteolytic activity of various candidates was screened on skim milk agar medium, and B. megaterium-TK1 was selected as the most promising candidate
Summary
Known as peptidases, degrade proteins and peptides by hydrolyzing their peptide bonds, thereby producing shorter byproducts They belong to a group of industrial proteins that account for ~60% of the total global market [1,2]. Biology 2020, 9, 472 alkaline proteolytic proteins are deemed to be a key group of proteins because of their wide use in different industries, including those for agriculture, detergents, textiles, and leather [1,3,4,5]. Thermostable alkaline proteases do not tolerate a variety of solvents, metal ions, or surfactants, significantly compromising their potential applications in the wider detergent industry [12,13]. It is of utmost interest to find an alternative protease that shows excellent performance towards pH values, temperatures, surfactant types, metal ions, and solvents for effective commercial applications
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