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Food Science and Human Wellness 2022, 11(4): 992-998 https://doi.org/10.1016/j.fshw.2022.03.026
Research Article | Open Access | Issue | Published: 28 April 2022

Suppression of postprandial blood glucose elevation by buckwheat (Fagpopyrum esculentum) albumin hydrolysate and identification of the peptide responsible to the function

Show Author's Information Kazumi Ninomiyaa,  Yusuke Yamaguchib,  Fumie Shinmachib,  Hitoshi Kumagaia,  Hitomi Kumagaib( )
Department of Food Science and Nutrition, Kyoritsu Women's University, 2-2-1 Hitotsubashi, Chiyoda-ku, Tokyo 101-8347, Japan
College of Bioresource Sciences, Nihon University, 1866 Kameino, Fujisawa-shi 252-0880, Japan

Peer review under responsibility of KeAi Communications Co., Ltd.

Keywords:
Type 2 diabetes, Buckwheat-albumin hydrolysate, Bioactive peptide, α-Amylase inhibitor, Postprandial hyperglycemia
Cite this article:
Ninomiya K, Yamaguchi Y, Shinmachi F, et al. Suppression of postprandial blood glucose elevation by buckwheat (Fagpopyrum esculentum) albumin hydrolysate and identification of the peptide responsible to the function. Food Science and Human Wellness, 2022, 11(4): 992-998. https://doi.org/10.1016/j.fshw.2022.03.026
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Abstract Full text About this article

The objective of this study is to evaluate the suppressive effect of buckwheat-albumin hydrolysate on postprandial hyperglycemia and identify the peptide responsible to the function. Buckwheat-albumin hydrolysate was prepared by using digestive enzymes and was orally administered to rats together with soluble starch. The blood was taken from the tail vein up to 90 min after oral administration to measure blood-glucose and plasma-insulin levels. The peptide with α-amylase inhibitory activity was purified from the buckwheat-hydrolysate by gel-filtration chromatography, α-amylase affinity chromatography, and high performance liquid chromatography (HPLC). The amino-acid sequence of the peptide was identified by a protein sequencer and was compared with that in the buckwheat-genome database. Buckwheat-albumin hydrolysate significantly suppressed the elevation of blood glucose level 15 min after starch administration. The amino-acid sequence of the peptide with α-amylase inhibitory activity was YVEPDCGNLGCCYHC in the parental protein of molecular mass 17.8 kDa and theoretical pI 4.77. The amino-acid sequence, molecular weight, and pI of the parental protein in buckwheat albumin were different from those of α-amylase inhibitor in wheat albumin. This study suggests that the novel α-amylase inhibitor identified in buckwheat albumin is a potential candidate for a functional food material to suppress postprandial blood glucose elevation.


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About this article

Suppression of postprandial blood glucose elevation by buckwheat (Fagpopyrum esculentum) albumin hydrolysate and identification of the peptide responsible to the function

Show Author's information Kazumi Ninomiyaa, Yusuke Yamaguchib, Fumie Shinmachib, Hitoshi Kumagaia, Hitomi Kumagaib( )
Department of Food Science and Nutrition, Kyoritsu Women's University, 2-2-1 Hitotsubashi, Chiyoda-ku, Tokyo 101-8347, Japan
College of Bioresource Sciences, Nihon University, 1866 Kameino, Fujisawa-shi 252-0880, Japan

Peer review under responsibility of KeAi Communications Co., Ltd.

Abstract

The objective of this study is to evaluate the suppressive effect of buckwheat-albumin hydrolysate on postprandial hyperglycemia and identify the peptide responsible to the function. Buckwheat-albumin hydrolysate was prepared by using digestive enzymes and was orally administered to rats together with soluble starch. The blood was taken from the tail vein up to 90 min after oral administration to measure blood-glucose and plasma-insulin levels. The peptide with α-amylase inhibitory activity was purified from the buckwheat-hydrolysate by gel-filtration chromatography, α-amylase affinity chromatography, and high performance liquid chromatography (HPLC). The amino-acid sequence of the peptide was identified by a protein sequencer and was compared with that in the buckwheat-genome database. Buckwheat-albumin hydrolysate significantly suppressed the elevation of blood glucose level 15 min after starch administration. The amino-acid sequence of the peptide with α-amylase inhibitory activity was YVEPDCGNLGCCYHC in the parental protein of molecular mass 17.8 kDa and theoretical pI 4.77. The amino-acid sequence, molecular weight, and pI of the parental protein in buckwheat albumin were different from those of α-amylase inhibitor in wheat albumin. This study suggests that the novel α-amylase inhibitor identified in buckwheat albumin is a potential candidate for a functional food material to suppress postprandial blood glucose elevation.

Keywords: Type 2 diabetes, Buckwheat-albumin hydrolysate, Bioactive peptide, α-Amylase inhibitor, Postprandial hyperglycemia

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Received: 01 November 2020
Revised: 13 February 2021
Accepted: 16 March 2021
Published: 28 April 2022
Issue date: July 2022

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© 2022 Beijing Academy of Food Sciences. Publishing services by Elsevier B.V. on behalf of KeAi Communications Co., Ltd.

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