Biochemical, structural and functional diversity between two digestive α-amylases from Helicoverpa armigera

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Bhide, Amey J., Channale, Sonal M., Patil, Sucheta S., Gupta, Vidya S., Ramasamy, Sureshkumar and Giri, Ashok P.. 2015. "Biochemical, structural and functional diversity between two digestive α-amylases from Helicoverpa armigera." Biochimica et Biophysica Acta (BBA): General Subjects. 1850 (9), pp. 1719-1728. https://doi.org/10.1016/j.bbagen.2015.04.008
Article Title

Biochemical, structural and functional diversity between two digestive α-amylases from Helicoverpa armigera

ERA Journal ID36838
Article CategoryArticle
AuthorsBhide, Amey J., Channale, Sonal M., Patil, Sucheta S., Gupta, Vidya S., Ramasamy, Sureshkumar and Giri, Ashok P.
Journal TitleBiochimica et Biophysica Acta (BBA): General Subjects
Journal Citation1850 (9), pp. 1719-1728
Number of Pages10
Year2015
Place of PublicationNetherlands
ISSN0304-4165
1872-8006
Digital Object Identifier (DOI)https://doi.org/10.1016/j.bbagen.2015.04.008
Web Address (URL)https://www.sciencedirect.com/science/article/pii/S0304416515001130
Abstract

Background: Helicoverpa armigera (Lepidoptera) feeds on various plants using diverse digestive enzymes as one of the survival tool-kit. The aim of the present study was to understand biochemical properties of recombinant α-amylases of H. armigera viz., HaAmy1 and HaAmy2.

Methods: The open reading frames of HaAmy1 and HaAmy2 were cloned in Pichia pastoris and expressed heterologously. Purified recombinant enzymes were characterized for their biochemical and biophysical attributes using established methods.

Results: Sequence alignment and homology modeling showed that HaAmy1 and HaAmy2 were conserved in their amino acid sequences and structures. HaAmy1 and HaAmy2 showed optimum activity at 60°C; however, they differed in their optimum pH. Furthermore, HaAmy2 showed higher affinity for starch and amylopectin whereas HaAmy1 had higher catalytic efficiency. HaAmy1 and HaAmy2 were inhibited to the same magnitude by a synthetic amylase inhibitor (acarbose) while wheat amylase inhibitor showed about 2-fold higher inhibition of HaAmy1 than HaAmy2 at pH 7 while 6-fold difference at pH 11. Interactions of HaAmy1 and HaAmy2 with wheat amylase inhibitor revealed 2:1 stoichiometric ratio and much more complex interaction with HaAmy1.

Conclusions: The diversity of amylases in perspective of their biochemical and biophysical properties, and their differential interactions with amylase inhibitors signify the potential role of these enzymes in adaptation of H. armigera on diverse plant diets. General significance Characterization of digestive enzymes of H. armigera provides the molecular basis for the polyphagous nature and thus could assist in designing future strategies for the insect control.

KeywordsAmylase inhibitors; Digestive enzymes; Enzyme activity; Helicoverpa armigera; α-amylases
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FunderCouncil of Scientific and Industrial Research, India
Byline AffiliationsCSIR-National Chemical Laboratory, India
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