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Metabolomic and chemometric study of Achras sapota L. fruit extracts for identification of metabolites contributing to the inhibition of α-amylase and α-glucosidase

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Abstract

Achras sapota L. fruit extracts have previously been reported to have activities against the carbohydrate-digesting enzymes α-amylase and α-glucosidase. The present work was aimed to identify the inhibitors of α-amylase and α-glucosidase using metabolomics and chemometric approaches. Metabolite profile of Achras sapota fruit extracts at different stages of post-harvest ripening was analyzed using GC–MS-based metabolomics approach. The extracts were also assayed for their properties to inhibit the carbohydrate-digesting enzymes α-amylase and α-glucosidase in vitro. The fruit extracts just after harvesting showed maximum activities against the enzymes α-amylase and α-glucosidase. The activities declined with post-harvest ripening. It was observed from the chemometric analysis that gallic acid, chlorogenic acid, benzene-1,2,4-triol, and d-malic acid are responsible for high α-amylase inhibitory activity. Gallic acid and chlorogenic acid are positively correlated with high α-glucosidase inhibitory activity. Inhibition of the two enzymes by gallic acid, benzene-1,2,4-triol, chlorogenic acid, and α-amylase by d-malic acid supported the findings. The present experiment reports the importance of both primary and secondary metabolites for the bioactivity of plant extracts.

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Acknowledgments

The authors are grateful to the Agricultural Field Station of University of Calcutta, Baruipur, Kolkata, India, for supplying the cricket ball variety of fruits. SD acknowledges financial assistance from University Grant Commission, India (Faculty Development Programme—Teacher Fellowship Award). Financial support from DST (FIST) is also acknowledged.

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Correspondence to Bratati De.

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Das, S., Dutta, M., Chaudhury, K. et al. Metabolomic and chemometric study of Achras sapota L. fruit extracts for identification of metabolites contributing to the inhibition of α-amylase and α-glucosidase. Eur Food Res Technol 242, 733–743 (2016). https://doi.org/10.1007/s00217-015-2581-0

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  • DOI: https://doi.org/10.1007/s00217-015-2581-0

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