Abstract
The NaCl-activated and detergent-stable proteinases from Virgibacillus halodenitrificans SK1-3-7 isolated from fish sauce fermentation were purified and characterized. The enzymes with molecular masses of 20 and 36 kDa showed caseinolytic activity on a zymogram. Optimum azocaseinolytic activity was at 60 °C and pH 9. The proteolytic activity increased in the presence of 10 mM CaCl2 and 0.5 M NaCl and showed high stability at 0–2 M NaCl. The enzymes were stable at pH 4–10 and 10–50 °C. The enzymes preferably hydrolyzed Suc-Ala-Ala-Pro-Phe-pNA and were completely inhibited by phenylmethanesulfonyl fluoride (PMSF), showing subtilisin-like characteristics. Activity and stability remained high in the presence of H2O2 and various surfactants. The enzymes exhibited high stability (>95 %) in various organic solvents (DMSO, butanol, ethanol, 2-propanol, and acetonitrile) at concentration of 50 %. The V. halodenitrificans SK1-3–7 proteinases showed potential as a biocatalyst in aqueous-organic solvent systems and as an additive in laundry detergent.
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This work was financially supported by the Suranaree University of Technology Research and Development Fund.
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Montriwong, A., Rodtong, S. & Yongsawatdigul, J. Detergent-Stable Salt-Activated Proteinases from Virgibacillus halodenitrificans SK1-3-7 Isolated from Fish Sauce Fermentation. Appl Biochem Biotechnol 176, 505–517 (2015). https://doi.org/10.1007/s12010-015-1591-5
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DOI: https://doi.org/10.1007/s12010-015-1591-5