Comparative analysis of physicochemical properties, ginsenosides content and α-amylase inhibitory effects in white ginseng and red ginseng

Ginseng (Panax ginseng C.A. Meyer) as a common dietary adjunct is widely applied in Traditional Chinese Medicine due to its health-promoting properties, but the differences between white ginseng and red ginseng was rarely studied. In the present study, color parameters and scanning electron microsco...

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Main Authors: Huairui Wang, Yao Cheng, Xue Zhang, Yingping Wang, Hui Zhao
Format: Article
Language:English
Published: Tsinghua University Press 2023-01-01
Series:Food Science and Human Wellness
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Online Access:http://www.sciencedirect.com/science/article/pii/S2213453022001215
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author Huairui Wang
Yao Cheng
Xue Zhang
Yingping Wang
Hui Zhao
author_facet Huairui Wang
Yao Cheng
Xue Zhang
Yingping Wang
Hui Zhao
author_sort Huairui Wang
collection DOAJ
description Ginseng (Panax ginseng C.A. Meyer) as a common dietary adjunct is widely applied in Traditional Chinese Medicine due to its health-promoting properties, but the differences between white ginseng and red ginseng was rarely studied. In the present study, color parameters and scanning electron microscope (SEM) were determined to evaluate the differences of ginseng color and microstructure induced by processing procedure. Quantitative analysis of multi-components by a single-marker (QAMS) method and anti-α-amylase activity test were used to assess variations of chemical ingredients and pharmacological activity between white and red ginseng. Finally, molecular docking studies were carried out to screen out the most effective compound against α-amylase. Results indicated that processing had a significant impact on the physicochemical properties and pharmacological activity of white and red ginseng. After processing, the color value of L* declined significantly. Red ginseng sample displayed a compact structure and presented of a gel layer on the surface compared to white ginseng. Additionally, the content of ginsenosides and the activity of anti-α-amylase decreased. The contents of total ginsenosides were positively correlated with the anti-α-amylase activities of ginseng, and ginsenoside Rb1 might be the most effective compound to inhibit the activity of α-amylase.
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publishDate 2023-01-01
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series Food Science and Human Wellness
spelling doaj-art-8f84a8ed1a6d458e9f09a5292e114f912025-02-03T06:55:36ZengTsinghua University PressFood Science and Human Wellness2213-45302023-01-011211427Comparative analysis of physicochemical properties, ginsenosides content and α-amylase inhibitory effects in white ginseng and red ginsengHuairui Wang0Yao Cheng1Xue Zhang2Yingping Wang3Hui Zhao4State Local Joint Engineering Research Center of Ginseng Breeding and Application, College of Chinese Medicinal Materials, Jilin Agricultural University, Changchun 130033, ChinaSchool of Biotechnology and Food Science, Tianjin University of Commerce, Tianjin 300134, ChinaSchool of Pharmaceutical Science and Technology, Health Sciences Platform, Tianjin University, Tianjin 300072, ChinaState Local Joint Engineering Research Center of Ginseng Breeding and Application, College of Chinese Medicinal Materials, Jilin Agricultural University, Changchun 130033, China; Corresponding authors.School of Biotechnology and Food Science, Tianjin University of Commerce, Tianjin 300134, China; Corresponding authors.Ginseng (Panax ginseng C.A. Meyer) as a common dietary adjunct is widely applied in Traditional Chinese Medicine due to its health-promoting properties, but the differences between white ginseng and red ginseng was rarely studied. In the present study, color parameters and scanning electron microscope (SEM) were determined to evaluate the differences of ginseng color and microstructure induced by processing procedure. Quantitative analysis of multi-components by a single-marker (QAMS) method and anti-α-amylase activity test were used to assess variations of chemical ingredients and pharmacological activity between white and red ginseng. Finally, molecular docking studies were carried out to screen out the most effective compound against α-amylase. Results indicated that processing had a significant impact on the physicochemical properties and pharmacological activity of white and red ginseng. After processing, the color value of L* declined significantly. Red ginseng sample displayed a compact structure and presented of a gel layer on the surface compared to white ginseng. Additionally, the content of ginsenosides and the activity of anti-α-amylase decreased. The contents of total ginsenosides were positively correlated with the anti-α-amylase activities of ginseng, and ginsenoside Rb1 might be the most effective compound to inhibit the activity of α-amylase.http://www.sciencedirect.com/science/article/pii/S2213453022001215GinsengColorMicrostructureGinsenosidesα-Amylase
spellingShingle Huairui Wang
Yao Cheng
Xue Zhang
Yingping Wang
Hui Zhao
Comparative analysis of physicochemical properties, ginsenosides content and α-amylase inhibitory effects in white ginseng and red ginseng
Food Science and Human Wellness
Ginseng
Color
Microstructure
Ginsenosides
α-Amylase
title Comparative analysis of physicochemical properties, ginsenosides content and α-amylase inhibitory effects in white ginseng and red ginseng
title_full Comparative analysis of physicochemical properties, ginsenosides content and α-amylase inhibitory effects in white ginseng and red ginseng
title_fullStr Comparative analysis of physicochemical properties, ginsenosides content and α-amylase inhibitory effects in white ginseng and red ginseng
title_full_unstemmed Comparative analysis of physicochemical properties, ginsenosides content and α-amylase inhibitory effects in white ginseng and red ginseng
title_short Comparative analysis of physicochemical properties, ginsenosides content and α-amylase inhibitory effects in white ginseng and red ginseng
title_sort comparative analysis of physicochemical properties ginsenosides content and α amylase inhibitory effects in white ginseng and red ginseng
topic Ginseng
Color
Microstructure
Ginsenosides
α-Amylase
url http://www.sciencedirect.com/science/article/pii/S2213453022001215
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