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. 2019 Feb 15;24(4):691.
doi: 10.3390/molecules24040691.

Anti-α-Glucosidase Activity by a Protease from Bacillus licheniformis

Chien Thang Doan  1   2 , Thi Ngoc Tran  3   4 , Minh Trung Nguyen  5 , Van Bon Nguyen  6 , Anh Dzung Nguyen  7 , San-Lang Wang  8   9
Affiliations

Anti-α-Glucosidase Activity by a Protease from Bacillus licheniformis

Chien Thang Doan et al. Molecules. .

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.

Keywords: Bacillus licheniformis; anti-α-glucosidase; diabetes; microbial conversion; protease.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Elution profile of TKU004P on Macro-Prep High S chromatography.
Figure 2
Figure 2
Anti-α-glucosidase (AAG) activity of TKU004P and acarbose. (A) Concentration range of 0–20 mg/mL; (B) concentration range of 0–0.5 mg/mL.
Figure 3
Figure 3
SDS-PAGE analysis of the protease produced by B. licheniformis TKU004. M—molecular markers; 1—TKU004P.
Figure 4
Figure 4
Lineweaver–Burk plot analysis of AAG by TKU004P. p-nitrophenyl glucopyranoside (pNPG) was used as substrate. The concentration of TKU004P was 0 mg/mL (♦); 0.2 mg/mL (×); 0.4 mg/mL (▲); 0.8 mg/mL (■).
Figure 5
Figure 5
HPLC analysis of the time-course reaction of TKU004P and yeast α-glucosidase.
Figure 6
Figure 6
Effect of pH on the stability of TKU004P.
Figure 7
Figure 7
Effect of the C/N source on AAG (a), optical density (OD) (b) and protease activity production (c) of B. licheniformis TKU004.
Figure 8
Figure 8
Effect of TKU004P on different enzymes. 1—yeast α-glucosidase; 2—rat α-glucosidase; 3—porcine pancreatic α-amylase; 4—B. subtilis α-amylase; 5—lysozyme; 6—cellulose.
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