Elucidation of Interaction between Whey Proteins and Proanthocyanidins and Its Protective Effects on Proanthocyanidins during In-Vitro Digestion and Storage

Whey proteins and oligomeric proanthocyanidins have nutritional value and are widely used in combination as food supplements. However, the effect of the interactions between proanthocyanidins and whey proteins on their stability has not been studied in depth. In this work, we aimed to characterize t...

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Main Authors: Chenyu Tang, Bing Tan, Xiangjun Sun
Format: Article
Language:English
Published: MDPI AG 2021-09-01
Series:Molecules
Subjects:
Online Access:https://www.mdpi.com/1420-3049/26/18/5468
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spelling doaj-f8928ad9576e4dc0aa9b3194e5ca10192021-09-26T00:45:50ZengMDPI AGMolecules1420-30492021-09-01265468546810.3390/molecules26185468Elucidation of Interaction between Whey Proteins and Proanthocyanidins and Its Protective Effects on Proanthocyanidins during In-Vitro Digestion and StorageChenyu Tang0Bing Tan1Xiangjun Sun2Department of Food Science and Engineering, School of Agriculture and Biology, Shanghai Jiaotong University, Shanghai 200240, ChinaDepartment of Food Science and Engineering, School of Agriculture and Biology, Shanghai Jiaotong University, Shanghai 200240, ChinaDepartment of Food Science and Engineering, School of Agriculture and Biology, Shanghai Jiaotong University, Shanghai 200240, ChinaWhey proteins and oligomeric proanthocyanidins have nutritional value and are widely used in combination as food supplements. However, the effect of the interactions between proanthocyanidins and whey proteins on their stability has not been studied in depth. In this work, we aimed to characterize the interactions between β-Lactoglobulin (β-LG) and α-lactalbumin (α-LA) and oligomeric proanthocyanidins, including A1, A2, B1, B2, B3, and C1, using multi-spectroscopic and molecular docking methods. Fluorescence spectroscopic data revealed that all of the oligomeric proanthocyanidins quenched the intrinsic fluorescence of β-LG or α-LA by binding-related fluorescence quenching. Among the six oligomeric proanthocyanidins, A1 showed the strongest affinity for β-LG (K<sub>a</sub> = 2.951 (±0.447) × 10<sup>4</sup> L∙mol<sup>−1</sup>) and α-LA (K<sub>a</sub> = 1.472 (±0.236) × 10<sup>5</sup> L∙mol<sup>−1</sup>) at 297 K. β-LG/α-LA and proanthocyanidins can spontaneously form complexes, which are mainly induced by hydrophobic interactions, hydrogen bonds, and van der Waals forces. Fourier-transform infrared spectroscopy (FTIR) and circular dichroism spectroscopy showed that the secondary structures of the proteins were rearranged after binding to oligomeric proanthocyanidins. During in vitro gastrointestinal digestion, the recovery rate of A1 and A2 increased with the addition of WPI by 11.90% and 38.43%, respectively. The addition of WPI (molar ratio of 1:1) increased the retention rate of proanthocyanidins A1, A2, B1, B2, B3, and C1 during storage at room temperature by 14.01%, 23.14%, 30.09%, 62.67%, 47.92%, and 60.56%, respectively. These results are helpful for the promotion of protein–proanthocyanidin complexes as functional food ingredients in the food industry.https://www.mdpi.com/1420-3049/26/18/5468proanthocyanidinswhey proteininteractionspectroscopymolecular dockingstability
collection DOAJ
language English
format Article
sources DOAJ
author Chenyu Tang
Bing Tan
Xiangjun Sun
spellingShingle Chenyu Tang
Bing Tan
Xiangjun Sun
Elucidation of Interaction between Whey Proteins and Proanthocyanidins and Its Protective Effects on Proanthocyanidins during In-Vitro Digestion and Storage
Molecules
proanthocyanidins
whey protein
interaction
spectroscopy
molecular docking
stability
author_facet Chenyu Tang
Bing Tan
Xiangjun Sun
author_sort Chenyu Tang
title Elucidation of Interaction between Whey Proteins and Proanthocyanidins and Its Protective Effects on Proanthocyanidins during In-Vitro Digestion and Storage
title_short Elucidation of Interaction between Whey Proteins and Proanthocyanidins and Its Protective Effects on Proanthocyanidins during In-Vitro Digestion and Storage
title_full Elucidation of Interaction between Whey Proteins and Proanthocyanidins and Its Protective Effects on Proanthocyanidins during In-Vitro Digestion and Storage
title_fullStr Elucidation of Interaction between Whey Proteins and Proanthocyanidins and Its Protective Effects on Proanthocyanidins during In-Vitro Digestion and Storage
title_full_unstemmed Elucidation of Interaction between Whey Proteins and Proanthocyanidins and Its Protective Effects on Proanthocyanidins during In-Vitro Digestion and Storage
title_sort elucidation of interaction between whey proteins and proanthocyanidins and its protective effects on proanthocyanidins during in-vitro digestion and storage
publisher MDPI AG
series Molecules
issn 1420-3049
publishDate 2021-09-01
description Whey proteins and oligomeric proanthocyanidins have nutritional value and are widely used in combination as food supplements. However, the effect of the interactions between proanthocyanidins and whey proteins on their stability has not been studied in depth. In this work, we aimed to characterize the interactions between β-Lactoglobulin (β-LG) and α-lactalbumin (α-LA) and oligomeric proanthocyanidins, including A1, A2, B1, B2, B3, and C1, using multi-spectroscopic and molecular docking methods. Fluorescence spectroscopic data revealed that all of the oligomeric proanthocyanidins quenched the intrinsic fluorescence of β-LG or α-LA by binding-related fluorescence quenching. Among the six oligomeric proanthocyanidins, A1 showed the strongest affinity for β-LG (K<sub>a</sub> = 2.951 (±0.447) × 10<sup>4</sup> L∙mol<sup>−1</sup>) and α-LA (K<sub>a</sub> = 1.472 (±0.236) × 10<sup>5</sup> L∙mol<sup>−1</sup>) at 297 K. β-LG/α-LA and proanthocyanidins can spontaneously form complexes, which are mainly induced by hydrophobic interactions, hydrogen bonds, and van der Waals forces. Fourier-transform infrared spectroscopy (FTIR) and circular dichroism spectroscopy showed that the secondary structures of the proteins were rearranged after binding to oligomeric proanthocyanidins. During in vitro gastrointestinal digestion, the recovery rate of A1 and A2 increased with the addition of WPI by 11.90% and 38.43%, respectively. The addition of WPI (molar ratio of 1:1) increased the retention rate of proanthocyanidins A1, A2, B1, B2, B3, and C1 during storage at room temperature by 14.01%, 23.14%, 30.09%, 62.67%, 47.92%, and 60.56%, respectively. These results are helpful for the promotion of protein–proanthocyanidin complexes as functional food ingredients in the food industry.
topic proanthocyanidins
whey protein
interaction
spectroscopy
molecular docking
stability
url https://www.mdpi.com/1420-3049/26/18/5468
work_keys_str_mv AT chenyutang elucidationofinteractionbetweenwheyproteinsandproanthocyanidinsanditsprotectiveeffectsonproanthocyanidinsduringinvitrodigestionandstorage
AT bingtan elucidationofinteractionbetweenwheyproteinsandproanthocyanidinsanditsprotectiveeffectsonproanthocyanidinsduringinvitrodigestionandstorage
AT xiangjunsun elucidationofinteractionbetweenwheyproteinsandproanthocyanidinsanditsprotectiveeffectsonproanthocyanidinsduringinvitrodigestionandstorage
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