Impacts of Proanthocyanidin Binding on Conformational and Functional Properties of Decolorized Highland Barley Protein
The impacts of interaction between proanthocyanidin (PC) and decolorized highland barley protein (DHBP) at pH 7 and 9 on the functional and conformational changes in DHBP were investigated. It was shown that PC strongly quenched the intrinsic fluorescence of DHBP primarily through static quenching....
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-01-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/12/3/481 |
| _version_ | 1797624611450388480 |
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| author | Juan Li Xin Zhang Wenju Zhou Zhaoxin Tu Xijuan Yang Jing Hao Feng Liang Zhengxing Chen Yan Du |
| author_facet | Juan Li Xin Zhang Wenju Zhou Zhaoxin Tu Xijuan Yang Jing Hao Feng Liang Zhengxing Chen Yan Du |
| author_sort | Juan Li |
| collection | DOAJ |
| description | The impacts of interaction between proanthocyanidin (PC) and decolorized highland barley protein (DHBP) at pH 7 and 9 on the functional and conformational changes in DHBP were investigated. It was shown that PC strongly quenched the intrinsic fluorescence of DHBP primarily through static quenching. PC and DHBP were mainly bound by hydrophobic interactions. Additionally, free sulfhydryl groups and surface hydrophobicity obviously decreased in DHBP after combining with PC. The zeta potential of DHBP–PC complexes at pH 7 increased significantly. A change in the structure of DHBP was caused by interactions with PC, resulting in an increase in the number of β-sheets, a decrease in the number of α-helixes, and a spectral shift in the amide Ⅱ band. Furthermore, the presence of PC enhanced the foaming properties and antioxidant activity of DHBP. Overall, this study suggests that DHBP–PC complexes at pH 7 could be designed as a stable additive, and illustrates the potential applications of DHBP–PC complexes in the food industry. |
| first_indexed | 2024-03-11T09:44:57Z |
| format | Article |
| id | doaj.art-6761c18bf5d44e0ebcad86f65e345224 |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-11T09:44:57Z |
| publishDate | 2023-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-6761c18bf5d44e0ebcad86f65e3452242023-11-16T16:39:58ZengMDPI AGFoods2304-81582023-01-0112348110.3390/foods12030481Impacts of Proanthocyanidin Binding on Conformational and Functional Properties of Decolorized Highland Barley ProteinJuan Li0Xin Zhang1Wenju Zhou2Zhaoxin Tu3Xijuan Yang4Jing Hao5Feng Liang6Zhengxing Chen7Yan Du8National Engineering Research Center of Cereal Fermentation and Food Biomanufacturing, Jiangnan University, Wuxi 214122, ChinaNational Engineering Research Center of Cereal Fermentation and Food Biomanufacturing, Jiangnan University, Wuxi 214122, ChinaQinghai Tianyoude Technology Investment Management Group Co., Ltd., Qinghai Engineering Technology Research Institute for Comprehensive Utilization of Highland Barley Resources, Xining 810016, ChinaQinghai Tianyoude Technology Investment Management Group Co., Ltd., Qinghai Engineering Technology Research Institute for Comprehensive Utilization of Highland Barley Resources, Xining 810016, ChinaQinghai Tibetan Plateau Key Laboratory of Agric-Product Processing, Qinghai Academy of Agricultural and Forestry Sciences, Xining 810016, ChinaQinghai Tianyoude Technology Investment Management Group Co., Ltd., Qinghai Engineering Technology Research Institute for Comprehensive Utilization of Highland Barley Resources, Xining 810016, ChinaQinghai Tianyoude Technology Investment Management Group Co., Ltd., Qinghai Engineering Technology Research Institute for Comprehensive Utilization of Highland Barley Resources, Xining 810016, ChinaNational Engineering Research Center of Cereal Fermentation and Food Biomanufacturing, Jiangnan University, Wuxi 214122, ChinaNational Engineering Research Center of Cereal Fermentation and Food Biomanufacturing, Jiangnan University, Wuxi 214122, ChinaThe impacts of interaction between proanthocyanidin (PC) and decolorized highland barley protein (DHBP) at pH 7 and 9 on the functional and conformational changes in DHBP were investigated. It was shown that PC strongly quenched the intrinsic fluorescence of DHBP primarily through static quenching. PC and DHBP were mainly bound by hydrophobic interactions. Additionally, free sulfhydryl groups and surface hydrophobicity obviously decreased in DHBP after combining with PC. The zeta potential of DHBP–PC complexes at pH 7 increased significantly. A change in the structure of DHBP was caused by interactions with PC, resulting in an increase in the number of β-sheets, a decrease in the number of α-helixes, and a spectral shift in the amide Ⅱ band. Furthermore, the presence of PC enhanced the foaming properties and antioxidant activity of DHBP. Overall, this study suggests that DHBP–PC complexes at pH 7 could be designed as a stable additive, and illustrates the potential applications of DHBP–PC complexes in the food industry.https://www.mdpi.com/2304-8158/12/3/481functional propertiesdecolorized proteinhighland barleyproanthocyanidinstructural changes |
| spellingShingle | Juan Li Xin Zhang Wenju Zhou Zhaoxin Tu Xijuan Yang Jing Hao Feng Liang Zhengxing Chen Yan Du Impacts of Proanthocyanidin Binding on Conformational and Functional Properties of Decolorized Highland Barley Protein Foods functional properties decolorized protein highland barley proanthocyanidin structural changes |
| title | Impacts of Proanthocyanidin Binding on Conformational and Functional Properties of Decolorized Highland Barley Protein |
| title_full | Impacts of Proanthocyanidin Binding on Conformational and Functional Properties of Decolorized Highland Barley Protein |
| title_fullStr | Impacts of Proanthocyanidin Binding on Conformational and Functional Properties of Decolorized Highland Barley Protein |
| title_full_unstemmed | Impacts of Proanthocyanidin Binding on Conformational and Functional Properties of Decolorized Highland Barley Protein |
| title_short | Impacts of Proanthocyanidin Binding on Conformational and Functional Properties of Decolorized Highland Barley Protein |
| title_sort | impacts of proanthocyanidin binding on conformational and functional properties of decolorized highland barley protein |
| topic | functional properties decolorized protein highland barley proanthocyanidin structural changes |
| url | https://www.mdpi.com/2304-8158/12/3/481 |
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