A new microtiter plate-based screening method for microorganisms producing Alpha-amylase inhibitors
Tóm tắt
Alpha-amylase inhibitors are widely used by the pharmaceutical and agricultural industries, such as the treatment of diabetes and obesity and insect controller. Here, we developed a colorimetric method to screen for α-amylase inhibitor producing strains or mutants with higher α-amylase inhibitor productivity. This method relies on absorbance changes at 402 nm that are due to the inhibition of α-amylase catalyzed hydrolysis of 2-Chloro-4-nitrophenyl-4-O-β-D-galactopyranosyl-maltoside by α-amylase inhibitors. The assay can be performed on a microtiter plate, making it simple and convenient. Using this method, α-amylase inhibitor producing strains and mutants with higher α-amylase inhibitor productivity can be rapidly screened. One strain, ZJB-08196, with the highest α-amylase inhibition was isolated and identified as Actinoplanes utahensis, and one mutant with higher acarbose production was obtained by screening 3,000 variants using this method.
Tài liệu tham khảo
Rossetti, L., A. Giaccari, and R. A. DeFronzo (1990) Glucose toxicity. Diabetes Care 13: 610–630.
Yang, W., J. Lu, J. Weng, W. Jia, L. Ji, J. Xiao, Z. Shan, J. Liu, H. Tian, and Q. Ji (2010) Prevalence of diabetes among men and women in China. New Engl. J. Med. 362: 1090–1101.
Apostolidis, E. and C. M. Lee (2010) In vitro potential of Ascophyllum nodosum phenolic antioxidant-mediated alpha-glucosidase and alpha-amylase inhibition. J. Food Sci. 75: 97–102.
Krentz, A. J. and C. J. Bailey (2005) Oral antidiabetic agents: Current role in type 2 diabetes mellitus. Drugs 65: 385–411.
Jung, B., M. Matzke, and J. Stoltefus (1996) Chemistry and structure activity relationship of glucosidase inhibitors. pp. 411–467. In: J. Kuhlman and W. Puls (eds.). Handbook of Experimental Pharmacology. Springer, Berlin, Germany.
Wehmeier, U. F. and W. Piepersberg (2004) Biotechnology and molecular biology of the alpha-glucosidase inhibitor acarbose. Appl. Microbiol. Biotechnol. 63: 613–625.
Prashanth, D., R. Padmaja, and D. S. Samiulla (2001) Effect of certain plant extracts on alpha-amylase activity. Fitoterapia. 72: 179–181.
Martins, J. C., M. Enassar, R. Willem, J. M. Wieruzeski, G. Lippens, and S. J. Wodak (2001) Solution structure of the main alpha-amylase inhibitor from amaranth seeds. Eur. J. Biochem. 268: 2379–2389.
Kotowaroo, M. I., M. F. Mahomoodally, A. Gurib-Fakim, and A. H. Subratty (2006) Screening of traditional antidiabetic medicinal plants of Mauritius for possible alpha-amylase inhibitory effects in vitro. Phytother Res. 20: 228–231.
Wang, Y. F., Z. W. Yang, and X. L. Wei (2010) Sugar compositions, α-glucosidase inhibitory and amylase inhibitory activities of polysaccharides from leaves and owers of Camellia sinensis obtained by different extraction methods. Int. J. Biol. Macromol. 47: 534–539.
Hansawasdi, C., J. Kawabata, and T. Kasai (2000) Alpha-amylase inhibitors from roselle (Hibiscus sabdariffa Linn.) tea. Biosci. Biotechnol. Biochem. 64: 1041–1043.
Choi, H. J., N. J. Kim, and D. H. Kim (2000) Inhibitory effects of crude drugs on alpha-glucosidase. Arch. Pharm.Res. 23: 261–266.
Mueller, L. (1989) Chemistry, biochemistry and therapeutic potential of microbial α-glucosidase inhibitors. pp. 109–113. In: A. L. Demain, G. A. Somkuti, J. C. Hunter-Cevera, and H. W. Rossmoore (eds.). Novel Microbial Products for Medicine and Agriculture. Elsevier Science Ltd., New York, US.
Frommer, W., W. Puls, and D. Schaefer (1975) Glycoside-hydrolase enzyme inhibitors. US Patent 3,876,766.
Imada, C. (2005) Enzyme inhibitors and other bioactive compounds from marine actinomycetes. Antonie. Van. Leeuwenhoek. 87: 59–63.
Miller, G. (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 31: 426–428.
Hamdan, I. and F. Afifi (2010) Capillary electrophoresis as a screening tool for alpha amylase inhibitors in plant extracts. Saudi. Pharm. J. 18: 91–95.
Bates, F., D. French, and R. Rundle (1943) Amylose and amylopectin content of starches determined by their iodine complex formation. J. Am. Chem.Soc. 65: 142–148.
Kandra, L. and G. Gyemant (2000) Examination of the active sites of human salivary alpha-amylase (HSA). Carbohyd. Res. 329: 579–585.
Liu, Z. Q., J. F. Zhang, Y. G. Zheng, and Y. C. Shen (2008) Improvement of astaxanthin production by a newly isolated Phaffia rhodozyma mutant with low energy ion beam implantation. J. Appl. Microbiol. 104: 861–872.
Williams, S. T., M. E. Sharpe, and J. G. Holt (1989) Bergey’s manual of systematic bacteriology. pp. 2299–2302. In: S. T. Williams, M. E. Sharpe, and J. G. Holt (eds.). Actinomycetes. Williams and Wilkins, Baltimore, US.
Long, P. (1994) Identification of some industrially important Actinoplanes species. J. Ind. Microbiol. Biotechnol. 13: 300–310.
Frommer, W., B. J., U. Keup, L. Mller, W. Puls, and D. Schmidt (1977) Amino sugar derivatives. US Patent 4,062,950.
Walker, J., J. Winder, and S. Kellam (1993) High-throughput microtiter plate-based chromogenic assays for glycosidase inhibitors. Appl. Biochem. Biotechnol. 38: 141–146.
Truscheit, E., W. Frommer, B. Junge, L. Mueller, D. Schmidt, and W. Wingender (1981) Chemistry and biochemistry of microbial α-Glucosidase inhibitors. Angew. Chem. Int. Ed. 20: 744–761.
Choi, B. and C. Shin (2003) Reduced formation of byproduct component C in acarbose fermentation by Actinoplanes sp. CKD485-16. Biotechnol. Prog. 19: 1677–1682.
Wang, Y. J., Y. G. Zheng, Y. P. Xue, Y. S. Wang, and Y. C. Shen (2011) Analysis and determination of anti-diabetes drug acarbose and its structural analogs. Curr. Pharm. Anal. 7: 12–20.
Chen, X. L., Y. G. Zheng, and Y. C. Shen (2005) A new method for production of valienamine with microbial degradation of acarbose. Biotechnol. Prog. 21: 1002–1003.
Zheng, Y. G., Y. P. Xue, and Y. C. Shen (2006) Production of valienamine by a newly isolated strain: Stenotrophomonas maltrophilia. Enz. Microb. Technol. 39: 1060–1065.
Li, W., H. Zheng, J. Bukuru, and N. De Kimpe (2004) Natural medicines used in the traditional Chinese medical system for therapy of diabetes mellitus. J. Ethnopharmacol. 92: 1–21.
Bhandari, M., N. Jong-Anurakkun, G. Hong, and J. Kawabata (2008) α-Glucosidase and α-amylase inhibitory activities of Nepalese medicinal herb Pakhanbhed (Bergenia ciliata, Haw.). Food Chem. 106: 247–252.