Characterization of two coleopteran a-amylases and molecular insights into their differential inhibition by synthetic a-amylase inhibitor, acarbose

Article


Channale, Sonal M., Bhide, Amey J., Yadav, Yashpal, Kashyap, Garima, Pawar, Pankaj K., Maheshwari, V. L., Ramasamy, Sureshkumar and Giri, Ashok P.. 2016. "Characterization of two coleopteran a-amylases and molecular insights into their differential inhibition by synthetic a-amylase inhibitor, acarbose." Insect Biochemistry and Molecular Biology. 74, pp. 1-11. https://doi.org/10.1016/j.ibmb.2016.04.009
Article Title

Characterization of two coleopteran a-amylases and molecular insights into their differential inhibition by synthetic a-amylase inhibitor, acarbose

ERA Journal ID2221
Article CategoryArticle
AuthorsChannale, Sonal M., Bhide, Amey J., Yadav, Yashpal, Kashyap, Garima, Pawar, Pankaj K., Maheshwari, V. L., Ramasamy, Sureshkumar and Giri, Ashok P.
Journal TitleInsect Biochemistry and Molecular Biology
Journal Citation74, pp. 1-11
Number of Pages11
Year2016
Place of PublicationUnited Kingdom
ISSN0965-1748
1879-0240
Digital Object Identifier (DOI)https://doi.org/10.1016/j.ibmb.2016.04.009
Web Address (URL)https://www.sciencedirect.com/science/article/pii/S0965174816300534
Abstract

Post-harvest insect infestation of stored grains makes them unfit for human consumption and leads to severe economic loss. Here, we report functional and structural characterization of two coleopteran α-amylases viz. Callosobruchus chinensis α-amylase (CcAmy) and Tribolium castaneum α-amylase (TcAmy) along with their interactions with proteinaceous and non-proteinaceous α-amylase inhibitors. Secondary structural alignment of CcAmy and TcAmy with other coleopteran α-amylases revealed conserved motifs, active sites, di-sulfide bonds and two point mutations at spatially conserved substrate or inhibitor-binding sites. Homology modeling and molecular docking showed structural differences between these two enzymes. Both the enzymes had similar optimum pH values but differed in their optimum temperature. Overall, pattern of enzyme stabilities were similar under various temperature and pH conditions. Further, CcAmy and TcAmy differed in their substrate affinity and catalytic efficiency towards starch and amylopectin. HPLC analysis detected common amylolytic products like maltose and malto-triose while glucose and malto-tetrose were unique in CcAmy and TcAmy catalyzed reactions respectively. At very low concentrations, wheat α-amylase inhibitor was found to be superior over the acarbose as far as complete inhibition of amylolytic activities of CcAmy and TcAmy was concerned. Mechanism underlying differential amylolytic reaction inhibition by acarbose was discussed.

KeywordsAcarbose; Callosobruchus chinensis; Coleoptera; Tribolium castaneum; α-amylase; α-amylase inhibitor
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FunderDepartment of Biotechnology, Ministry of Science and Technology, India
Byline AffiliationsCSIR-National Chemical Laboratory, India
Shivaji University, India
North Maharashtra University, India
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