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Blueberry extract inhibits carbohydrate-hydrolyzing enzymes and these inhibitory activities are not proanthocyanidin dependent

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Abstract

This study investigates the carbohydrate-hydrolyzing inhibitory potential of blueberry extract on carbohydrate-hydrolyzing enzymes and evaluates if the inhibitory activity is proanthocyanidin (PAC) or lower molecular weight phenolic dependent. Freeze-dried blueberry powder was extracted using acetone and subjected to C18 extraction (BAE). Low-molecular weight phenolics (BAE-LMW) and PACs (BAE-PAC) were separated from BAE with gel filtration chromatography using LH-20 column. Total phenolic content, PAC content, and phenolic profiles using HPLC, as well as rat α-glucosidase, sucrase, and maltase inhibitory activities, were determined for all samples. The rat alpha-glucosidase inhibitory activity of BAE (IC50 0.390 mg/mL TP basis) was enhanced in BAE-LMW (IC50 0.242 mg/mL TP basis) and reduced in BAE-PAC (IC50 0.915 mg/mL TP basis). Similar trends were observed with maltase and sucrase inhibitory activities. Our findings suggest that blueberry acetone extract has inhibitory activity on carbohydrate-hydrolyzing enzymes and this effect is dependent on LMWs rather than PAC.

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Acknowledgments

This research was funded by the 6.2 Applied Research project area “Technologies for Nutrient/Novel Delivery Systems” from the NSRDEC Combat Feeding Directorate.

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Authors and Affiliations

  1. Department of Chemistry and Food Science, Framingham State University, Framingham, MA, USA

    Bou-Hee Kang, Sarah J. Pilkenton & Emmanouil Apostolidis

  2. US Army Natick Soldier Research Engineering Center, Natick, MA, USA

    Kenneth Racicot

  3. Department of Food and Nutrition, Hannam University, Daejeon, Korea

    Young-In Kwon

Authors
  1. Bou-Hee Kang
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  2. Kenneth Racicot
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  3. Sarah J. Pilkenton
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  4. Young-In Kwon
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  5. Emmanouil Apostolidis
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Correspondence to Emmanouil Apostolidis.

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Kang, BH., Racicot, K., Pilkenton, S.J. et al. Blueberry extract inhibits carbohydrate-hydrolyzing enzymes and these inhibitory activities are not proanthocyanidin dependent. J Korean Soc Appl Biol Chem 58, 127–136 (2015). https://doi.org/10.1007/s13765-015-0001-6

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  • DOI: https://doi.org/10.1007/s13765-015-0001-6

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