Purification, characterization and hypoglycemic activity of glycoproteins obtained from pea (Pisum sativum L.)

This study aimed to isolate and characterize the structures of glycoproteins from peas and determine their hypoglycemic activity. The crude pea glycoproteins (PGP) were extracted by hot water and purified by diethylaminoethyl (DEAE)-Sepharose chromatography and Sephadex G-100 size-exclusion chromato...

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Main Authors: Gaoyixin Qin, Wu Xu, Junping Liu, Liyan Zhao, Guitang Chen
Format: Article
Language:English
Published: Tsinghua University Press 2021-05-01
Series:Food Science and Human Wellness
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Online Access:http://www.sciencedirect.com/science/article/pii/S2213453021000306
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author Gaoyixin Qin
Wu Xu
Junping Liu
Liyan Zhao
Guitang Chen
author_facet Gaoyixin Qin
Wu Xu
Junping Liu
Liyan Zhao
Guitang Chen
author_sort Gaoyixin Qin
collection DOAJ
description This study aimed to isolate and characterize the structures of glycoproteins from peas and determine their hypoglycemic activity. The crude pea glycoproteins (PGP) were extracted by hot water and purified by diethylaminoethyl (DEAE)-Sepharose chromatography and Sephadex G-100 size-exclusion chromatography in sequence. Then three main fractions were obtained, namely PGP1, PGP2 and PGP3, with molecular weights of 897 615, 846 740 and 1 194 692 Da, respectively. The physical and chemical properties of the three fractions were evaluated and compared by Fourier transform infrared spectroscopy (FT-IR), nuclear magnetic resonance (NMR), scanning electron microscope (SEM), high performance liquid chromatography (HPLC) and other analytical techniques. The fraction PGP2 with the highest hypoglycemic activity, was screened using the Caco-2 monolayer cell model. It can inhibit the uptake of glucose in the small intestine, as well as the activities of maltase and sucrase. After simulated gastrointestinal digestion, PGP2 significantly enhanced the inhibitory effect of α-glucosidase, and slightly reduced the inhibitory ability of α-amylase. In summary, PGP2 possessed strong hypoglycemic activity after digestion. These results indicated that PGP2 has the potential to be developed into a functional food or natural medicine for the treatment of type 2 diabetes mellitus.
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series Food Science and Human Wellness
spelling doaj-art-d2f2f84e607943fe90c6e0e367bf8b592025-02-03T07:02:05ZengTsinghua University PressFood Science and Human Wellness2213-45302021-05-01103297307Purification, characterization and hypoglycemic activity of glycoproteins obtained from pea (Pisum sativum L.)Gaoyixin Qin0Wu Xu1Junping Liu2Liyan Zhao3Guitang Chen4Department of Food Quality and Safety/National R&D Center for Chinese Herbal Medicine Processing, China Pharmaceutical University, Nanjing 210009, ChinaDepartment of Food Quality and Safety/National R&D Center for Chinese Herbal Medicine Processing, China Pharmaceutical University, Nanjing 210009, ChinaDepartment of Food Quality and Safety/National R&D Center for Chinese Herbal Medicine Processing, China Pharmaceutical University, Nanjing 210009, ChinaCollege of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaDepartment of Food Quality and Safety/National R&D Center for Chinese Herbal Medicine Processing, China Pharmaceutical University, Nanjing 210009, China; Corresponding author. Department of Food Quality and Safety/National R&D Center for Chinese Herbal Medicine Processing, China Pharmaceutical University, Nanjing 210009, China.This study aimed to isolate and characterize the structures of glycoproteins from peas and determine their hypoglycemic activity. The crude pea glycoproteins (PGP) were extracted by hot water and purified by diethylaminoethyl (DEAE)-Sepharose chromatography and Sephadex G-100 size-exclusion chromatography in sequence. Then three main fractions were obtained, namely PGP1, PGP2 and PGP3, with molecular weights of 897 615, 846 740 and 1 194 692 Da, respectively. The physical and chemical properties of the three fractions were evaluated and compared by Fourier transform infrared spectroscopy (FT-IR), nuclear magnetic resonance (NMR), scanning electron microscope (SEM), high performance liquid chromatography (HPLC) and other analytical techniques. The fraction PGP2 with the highest hypoglycemic activity, was screened using the Caco-2 monolayer cell model. It can inhibit the uptake of glucose in the small intestine, as well as the activities of maltase and sucrase. After simulated gastrointestinal digestion, PGP2 significantly enhanced the inhibitory effect of α-glucosidase, and slightly reduced the inhibitory ability of α-amylase. In summary, PGP2 possessed strong hypoglycemic activity after digestion. These results indicated that PGP2 has the potential to be developed into a functional food or natural medicine for the treatment of type 2 diabetes mellitus.http://www.sciencedirect.com/science/article/pii/S2213453021000306Pea (Pisum sativum L.)GlycoproteinStructural characterizationHypoglycemic activitySimulated gastrointestinal digestion
spellingShingle Gaoyixin Qin
Wu Xu
Junping Liu
Liyan Zhao
Guitang Chen
Purification, characterization and hypoglycemic activity of glycoproteins obtained from pea (Pisum sativum L.)
Food Science and Human Wellness
Pea (Pisum sativum L.)
Glycoprotein
Structural characterization
Hypoglycemic activity
Simulated gastrointestinal digestion
title Purification, characterization and hypoglycemic activity of glycoproteins obtained from pea (Pisum sativum L.)
title_full Purification, characterization and hypoglycemic activity of glycoproteins obtained from pea (Pisum sativum L.)
title_fullStr Purification, characterization and hypoglycemic activity of glycoproteins obtained from pea (Pisum sativum L.)
title_full_unstemmed Purification, characterization and hypoglycemic activity of glycoproteins obtained from pea (Pisum sativum L.)
title_short Purification, characterization and hypoglycemic activity of glycoproteins obtained from pea (Pisum sativum L.)
title_sort purification characterization and hypoglycemic activity of glycoproteins obtained from pea pisum sativum l
topic Pea (Pisum sativum L.)
Glycoprotein
Structural characterization
Hypoglycemic activity
Simulated gastrointestinal digestion
url http://www.sciencedirect.com/science/article/pii/S2213453021000306
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