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.
Highlights
Alpha-glucosidase (EC 3.2.1.20) is a hydrolytic enzyme that acts mainly on α-1→4 glycosidic linkages of complex carbohydrates to release a single α-glucose [1]
The release of glucose from complex carbohydrates is the main reason for postprandial hyperglycemia, an important factor in developing type II diabetes [7]
By using a modified protein as the substrate, TKU004P showed the most activity on azocasein, followed by azoalbumin. These results indicate that TKU004P is a caseinolytic protease
Summary
Alpha-glucosidase (EC 3.2.1.20) is a hydrolytic enzyme that acts mainly on α-1→4 glycosidic linkages of complex carbohydrates to release a single α-glucose [1]. Many living creatures can produce α-glucosidase, including bacteria, yeast, plants and animals [2,3,4,5,6]. Based on the specific substrate, α-glucosidases are separated into three types: types I, II and III. Α-glucosidase is secreted by the epithelial cells of the small intestine and cleaves dietary carbohydrates into glucose. The release of glucose from complex carbohydrates is the main reason for postprandial hyperglycemia, an important factor in developing type II diabetes [7]. As such, counteracting the activity of α-glucosidase may decrease postprandial hyperglycemia and, as a result, prevent the onset of diabetes [8,9,10]
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