Anti-α-Glucosidase Activity by a Protease from <i>Bacillus licheniformis</i>

• Main Authors: Chien Thang Doan, Thi Ngoc Tran, Minh Trung Nguyen, Van Bon Nguyen, Anh Dzung Nguyen, San-Lang Wang
• Format: Article
• Language: English
• Published: MDPI AG 2019-02-01
• Series: Molecules
• Subjects: anti-α-glucosidase; protease; diabetes; microbial conversion; <i>Bacillus licheniformis</i>
• Online Access: https://www.mdpi.com/1420-3049/24/4/691

Anti-&#945;-glucosidase (AAG) compounds have received great attention due to their potential use in treating diabetes. In this study, <i>Bacillus licheniformis</i> TKU004, an isolated bacterial strain from Taiwanese soil, produced AAG activity in the culture supernatant when squid pens were used as the sole carbon/nitrogen (C/N) source. The protein TKU004P, which was isolated from <i>B. licheniformis</i> TKU004, showed stronger AAG activity than acarbose, a commercial anti-diabetic drug (IC₅₀ = 0.1 mg/mL and 2.02 mg/mL, respectively). The molecular weight of TKU004P, determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), was 29 kDa. High-performance liquid chromatography (HPLC) analysis showed that TKU004P may be a protease that demonstrates AAG activity by degrading yeast &#945;-glucosidase. Among the four chitinous sources of C/N, TKU004P produced the highest AAG activity in the culture supernatant when shrimp head powder was used as the sole source (470.66 U/mL). For comparison, 16 proteases, were investigated for AAG activity but TKU004P produced the highest levels. Overall, the findings suggest that TKU004P could have applications in the biochemical and medicinal fields thanks to its ability to control the activity of &#945;-glucosidase.