Preprint10.21203/rs.3.rs-4089737/v1
Evaluation of extracellular alkaline proteases from Bacillus amyloliquefaciens, B. siamensis, B. subtilis, and B. velezensis
Kanoknart Prabmark,Kanphorn Saeng-kla,Katewadee Boonyapakron,Katesuda Aiewviriyasakul,Wipawee Sritus,Benjarat Bunterngsook,Wasin Poncheewin,Pattanop Kanokratana,Verawat Champreda,Thanaporn Laothanachareon +9 more
- 15 Mar 2024
TL;DR: Evaluation of extracellular alkaline proteases from Bacillus amyloliquefaciens, B. siamensis, B. subtilis, and B. velezensis reveals optimal production conditions and potential applications in detergents.
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Abstract: Abstract Alkaline proteases have several applications in various industries. In this study, alkaline proteases from Bacillus amyloliquefaciens TBRC 2902 , B. siamensis TBRC 1180 , B. subtilis TBRC 6663, and B. velezensis TBRC 7773 were characterized. The production of extracellular protease activity was optimal using tapioca starch as the carbon source for TBRC 2902 and TBRC 1180, and soluble starch for TBRC 7773, whereas both carbon sources were optimal for TBRC 6663. Yeast extract was the optimal organic nitrogen source for all the strains. Skim milk was an equally effective alternative organic nitrogen source for TBRC 2902, TBRC 1180, and TBRC 7773, whereas soytone was as effective as yeast extract for TBRC 6663. To enhance the alkaline protease activity by 10-20%, inorganic nitrogen sources are essential for certain strains including TBRC 2902 and TBRC 1180, which require diammonium hydrogen phosphate and potassium nitrate, respectively. The B. siamensis TBRC 1180 alkaline protease exhibited optimal pH and temperature values of 9.0 and 60°C, respectively, whereas the enzymes from the other strains showed lower optimal pH and temperature values of 8.0 and 50°C, respectively. All enzymes exhibited tolerance to non-ionic surfactants, with more than 40% relative activity remaining when exposed to Triton X-100, Tween-20, and Tween-80 for 24 hours, indicating the potential application of these enzymes as detergent additives.
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