Purification and Characterization of C. maculatus α-amylase

Authors

  • Anussorn Wisessing Department of Biochemistry, Faculty of Science, Kasetsart University, Bangkok 10900, Thailand.
  • Arunee Engkagul Department of Biochemistry, Faculty of Science, Kasetsart University, Bangkok 10900, Thailand.
  • Arunee Wongpiyasatid Department of Applied Radiation and Isotopes, Faculty of Science, Kasetsart University, Bangkok 10900, Thailand.
  • Kiattawee Chuwongkomon Department of Biochemistry, Faculty of Science, Kasetsart University, Bangkok 10900, Thailand.

Keywords:

mungbean seeds, α-amylase, characterization, C. maculates, purification

Abstract

Callosobruchus maculatus causes damaging of storage mungbean seeds. Understanding control mechanism of a-amylase activity is essential for developing method for the insect control. In this study, C. maculatus a-amylase was purified and characterized. Purification was carried out using self-coupled β-cyclodextrin sepharose 6B affinity column. It was found that C. maculatus α-amylase had one isoform with a molecular weight of 50 kDa. The purified enzyme with specific activity of 182.78 U mg protein-1, showing optimum pH at around 5-6 and optimum temperature at 50-60 °C.

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Published

2008-12-31

How to Cite

Anussorn Wisessing, Arunee Engkagul, Arunee Wongpiyasatid, and Kiattawee Chuwongkomon. 2008. “Purification and Characterization of C. Maculatus α-Amylase”. Agriculture and Natural Resources 42 (5). Bangkok, Thailand:240-44. https://li01.tci-thaijo.org/index.php/anres/article/view/244601.

Issue

Vol. 42 No. 5 (2008): January-December

Section

Research Article

License

online 2452-316X print 2468-1458/Copyright © 2022. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/),
production and hosting by Kasetsart University of Research and Development Institute on behalf of Kasetsart University.