淡江大學機構典藏:Item 987654321/115777
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    Please use this identifier to cite or link to this item: https://tkuir.lib.tku.edu.tw/dspace/handle/987654321/115777


    Title: Anti-α-glucosidase activity by a protease from Bacillus licheniformis
    Authors: Chien Thang Doan;Thi Ngoc Tran;Minh Trung Nguyen;Van Bon Nguyen;Anh Dzung Nguyen;San-Lang Wang
    Keywords: anti-α-glucosidase;protease;diabetes;microbial conversion;Bacillus licheniformis
    Date: 2019-02-15
    Issue Date: 2019-02-18 12:10:14 (UTC+8)
    Publisher: MDPI
    Abstract: Anti-α-glucosidase (AAG) compounds have received great attention due to their potential
    use in treating diabetes. In this study, Bacillus licheniformis 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
    B. licheniformis 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 α-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 α-glucosidase.
    Relation: Molecules 24(4), 691
    DOI: 10.3390/molecules24040691
    Appears in Collections:[Graduate Institute & Department of Chemistry] Journal Article

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