Analysis of β-lactoglobulin–epigallocatechin gallate interactions: the antioxidant capacity and effects of polyphenols under different heating conditions in polyphenolic–protein interactions. Issue 5 (19th May 2020)
- Record Type:
- Journal Article
- Title:
- Analysis of β-lactoglobulin–epigallocatechin gallate interactions: the antioxidant capacity and effects of polyphenols under different heating conditions in polyphenolic–protein interactions. Issue 5 (19th May 2020)
- Main Title:
- Analysis of β-lactoglobulin–epigallocatechin gallate interactions: the antioxidant capacity and effects of polyphenols under different heating conditions in polyphenolic–protein interactions
- Authors:
- Qie, Xuejiao
Chen, Yao
Quan, Wei
Wang, Zhaojun
Zeng, Maomao
Qin, Fang
Chen, Jie
He, Zhiyong - Abstract:
- Abstract : A β-Lg-EGCG covalent conjugate is formed by linking the amino group of a lysine residue and EGCG; the antioxidant capacity of EGCG induced by β-Lg–EGCG covalent conjugates causes a significant decrease. Abstract : The interaction and antioxidant capacity between epigallocatechin gallate (EGCG) and β-lactoglobulin (β-Lg) under thermal treatments at 25–121 °C were investigated in this study. Fluorescence spectroscopy analysis showed that EGCG complexed with β-Lg mainly via non-covalent interactions and the binding affinity of EGCG to β-Lg was enhanced with heat treatment. EGCG showed a strong binding affinity to β-Lg after 85 °C heat treatment was applied, with a K a of 30.69 (±0.87) × 10 5 M −1 (pH 6.8, 298 K). Circular dichroism (CD) results showed that heat treatment did not result in greatly affected changes in the β-Lg secondary structure induced by β-Lg–EGCG interactions. MALDI-TOF/TOF-MS analysis showed that β-Lg–EGCG covalent conjugates initially formed after heat was applied at 60 °C, and their proportions increased under heat treatment ranging from 85 to 121 °C. The amino group of a lysine residue was further confirmed as the covalent binding site of EGCG to β-Lg. The β-Lg–EGCG interaction showed little effect on the antioxidant capacity (ABTS and ferric reducing antioxidant power (FRAP) values) of EGCG after heat treatment at 25–60 °C, but did induce an obvious reduction at temperatures above 85 °C. This study will provide the foundation for the use ofAbstract : A β-Lg-EGCG covalent conjugate is formed by linking the amino group of a lysine residue and EGCG; the antioxidant capacity of EGCG induced by β-Lg–EGCG covalent conjugates causes a significant decrease. Abstract : The interaction and antioxidant capacity between epigallocatechin gallate (EGCG) and β-lactoglobulin (β-Lg) under thermal treatments at 25–121 °C were investigated in this study. Fluorescence spectroscopy analysis showed that EGCG complexed with β-Lg mainly via non-covalent interactions and the binding affinity of EGCG to β-Lg was enhanced with heat treatment. EGCG showed a strong binding affinity to β-Lg after 85 °C heat treatment was applied, with a K a of 30.69 (±0.87) × 10 5 M −1 (pH 6.8, 298 K). Circular dichroism (CD) results showed that heat treatment did not result in greatly affected changes in the β-Lg secondary structure induced by β-Lg–EGCG interactions. MALDI-TOF/TOF-MS analysis showed that β-Lg–EGCG covalent conjugates initially formed after heat was applied at 60 °C, and their proportions increased under heat treatment ranging from 85 to 121 °C. The amino group of a lysine residue was further confirmed as the covalent binding site of EGCG to β-Lg. The β-Lg–EGCG interaction showed little effect on the antioxidant capacity (ABTS and ferric reducing antioxidant power (FRAP) values) of EGCG after heat treatment at 25–60 °C, but did induce an obvious reduction at temperatures above 85 °C. This study will provide the foundation for the use of EGCG in processing dairy products (such as milk tea beverages) with desirable nutrition and physiological functions. … (more)
- Is Part Of:
- Food & function. Volume 11:Issue 5(2020)
- Journal:
- Food & function
- Issue:
- Volume 11:Issue 5(2020)
- Issue Display:
- Volume 11, Issue 5 (2020)
- Year:
- 2020
- Volume:
- 11
- Issue:
- 5
- Issue Sort Value:
- 2020-0011-0005-0000
- Page Start:
- 3867
- Page End:
- 3878
- Publication Date:
- 2020-05-19
- Subjects:
- Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
Nutrition -- Periodicals
664.07 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/FO ↗
http://pubs.rsc.org/en/journals/journal/fo ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/d0fo00627k ↗
- Languages:
- English
- ISSNs:
- 2042-6496
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.038457
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 13831.xml