Abstract
A newly isolated alkaline protease-producing myxobacterium was isolated from soil. The strain was identified as Pyxidicoccus sp. S252 on the basis of 16S rRNA sequence analysis. The extracellular alkaline proteases produced by isolate S252 (PyCP) was optimally active in the pH range of 11.0–12.0 and temperature range of 40–50°C The zymogram of PyCP showed six caseinolytic protease bands. The proteases were stable in the pH range of 8.0–10.0 and temperature range of 40–50°C. The activity of PyCP was enhanced in the presence of Na+, Mg2+, Cu2+, Tween-20, and hydrogen peroxide (H2O2) (hydrogen peroxide), whereas in Triton X-100, glycerol, ethylenediaminetetraacetic acid (EDTA), and Co2+, it was stable. PyCP showed a potential in various applications. The addition of PyCP in the commercial detergent enhanced the wash performance of the detergent by efficiently removing the stains of tomato ketchup and coffee. PyCP efficiently hydrolyzed the gelatin layer on X-ray film to release the embedded silver. PyCP also showed potent dehairing of goat skin and also efficiently deproteinized sea shell waste indicating its application in chitin extraction. Thus, the results of the present study indicate that Pyxidicoccus sp. S252 proteases have the potential to be used as an ecofriendly replacement of chemicals in several industrial processes.
Highlights
Proteases are hydrolytic enzymes that are capable of catalyzing the hydrolysis of peptide bonds and degrade proteins into simpler peptides
S252, secreted extracellular proteases which were active over a wide range of pH and temperature
The alkaline PyCP were stable in several detergent components and showed a remarkable washing performance when added to the commercial laundry detergent
Summary
Proteases are hydrolytic enzymes that are capable of catalyzing the hydrolysis of peptide bonds and degrade proteins into simpler peptides. Proteases can be classified based on the site of action, substrate specificity, similarity to studied enzymes, amino acids at the active site, and pH optima (Banerjee and Ray, 2017). On the basis of the site of action, they are categorized into endo- or exo-enzymes, and based on the amino acids at the active site, they are classified as serine, cysteine, aspartic, and metallo proteases. Based on the pH optima, they are classified as acidic, neutral, and alkaline proteases (Rao et al, 1998). Proteases are ubiquitous in prokaryotes and eukaryotes, where they play important roles in physiology of the host organisms.
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