Effect of covalent modification by (−)-epigallocatechin-3-gallate on physicochemical and functional properties of whey protein isolate

Zhang, Jia; Zheng, Min; Tao, Fei; Chen, Wenwei; Huang, Guangrong; Jiang, Jiaxin

doi:10.1016/j.lwt.2015.10.054

Cited by 133 publications

(68 citation statements)

References 35 publications

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“…In addition, they are also one of the most popular natural antioxidant sources in food industry, as they are label free (clean label); (Xie et al 2017). As discussed previously, phenolic compounds can interact with proteins and these protein-phenol interactions are likely to alter the physiochemical and functional properties of proteins such as the antioxidant activity and surface hydrophobicity, which opens new opportunities for functional ingredients (Ali et al, 2013;Cao & Xiong, 2017;Cao, Xiong, Cao, & True, 2018;Gan et al, 2016;Jia et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

Covalent Whey Protein–Rosmarinic Acid Interactions: A Comparison of Alkaline and Enzymatic Modifications on Physicochemical, Antioxidative, and Antibacterial Properties

Ali

Keppler

Coenye

et al. 2018

Journal of Food Science

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The covalent interactions between whey protein isolate (WPI) and rosmarinic acid (RosA) at two different conditions, alkaline (pH 9) and enzymatic (in the presence of tyrosinase, PPO), at room temperature with free atmospheric air were studied. The conjugates formed between WPI and RosA were characterized in terms of their physicochemical and functional properties. The changes in protein structure were analyzed by intrinsic fluorescence and binding of 8-anilino-1-naphthalenesulfonic acid. The findings show that the covalent interactions caused a decrease in free amino and thiol groups and tryptophan content at both conditions. The decrease at enzymatic conditions was lower than at alkaline conditions. In addition, modified WPI at alkaline conditions exhibited higher antioxidative capacity compared to the modification at enzymatic conditions. However, WPI modified at enzymatic condition showed mild antimicrobial activity against Staphylococcus aureus LMG 10147 and MU50 compared to WPI modified at alkaline conditions and unmodified WPI (control). The modified WPI can be used as multifunctional ingredient into various food products with an additional health promoting effect of the bound phenolic compounds.

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Section: Introductionmentioning

confidence: 99%

Covalent Whey Protein–Rosmarinic Acid Interactions: A Comparison of Alkaline and Enzymatic Modifications on Physicochemical, Antioxidative, and Antibacterial Properties

Ali

Keppler

Coenye

et al. 2018

Journal of Food Science

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“…The specific acidity condition, for example, alkaline pH, could affect the degree of binding, the formation of covalent bond and noncovalent interaction through inducing radicals or quinones from autoxidation (Mori and others ; Schwartz and others ). Alkaline‐modulated covalent binding of EGCG to WPI reportedly enhanced protein foaming and emulsifying properties of WPI (Jia and others ).…”

Section: Introductionmentioning

confidence: 99%

Interaction of Whey Proteins with Phenolic Derivatives Under Neutral and Acidic pH Conditions

Cao

Xiong

2017

Journal of Food Science

167

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Integration of gallic acid (GA) and its derivative epigallocatechin gallate (EGCG; 20, 120, and 240 μmol/g, protein basis) into whey protein isolate (WPI) at room temperature and pH 3.0 and pH 7.0 was investigated. At pH 7.0, both phenolics caused significant structural changes and EGCG induced greater digestibility of WPI. Total sulfhydryl in WPI decreased from 28.6 to 7.6 μmol/g and surface hydrophobicity declined by nearly 50% with 240 μmol/g EGCG at pH 7.0. Similar but less appreciable changes were produced by GA and at pH 3.0. Isothermal titration and fluorescence quenching tests showed moderately weak binding of WPI with GA but strong binding with EGCG at pH 7.0. Both phenolics at high concentrations lowered the thermal transition temperature of β-lactoglobulin by 0.5 °C to 1.4 °C and promoted its digestion. The phenolics also displayed a remarkable synergism with peptides in the WPI digest exerting radical scavenging activity.

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“…Various researchers have revealed the structural changes in proteins upon phenolic interaction (Ali et al 2013;Rawel et al 2002b;Jia et al 2016). Modification of protein structure upon phenolic interaction has direct implication on the behaviour of protein during processing, preparation, consumption and storage in food systems.…”

Section: Introductionmentioning

confidence: 99%

Effect of removal of phenolic compounds on structural and thermal properties of sunflower protein isolate

2016

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The present study evaluated the effect of removal of polyphenols on the structural properties of protein isolates extracted from sunflower seed and kernel. The structural and thermal changes in protein upon phenolic interaction were studied using circular dichroism, differential scanning calorimetry, thermal gravimetric analysis, X-ray diffraction, sodium dodecyl sulphatepolyacrylamide gel electrophoresis (SDS-PAGE), and Fourier Transform Infrared (FT-IR) spectroscopy. Presence of phenolic compounds in proteins decreased the ordered structure content with parallel increase in unordered structure content. Denaturation temperature was higher for protein isolates with phenolic compounds while, enthalpy decreased upon phenolic interaction. In the presence of phenolic compounds, higher mass loss was observed upon heating. Crystalinity and crystal size got increased after removal of phenolic compounds. Protein isolates from kernels had higher percentage of crystalinity and crystal size as compared to seed protein isolates. Higher molecular weights were observed for protein isolates with phenolic compounds. Presence of polyphenols reduced the hydrophobicity as well the sulfhydryl content and increased the particle size of proteins.

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Effect of covalent modification by (−)-epigallocatechin-3-gallate on physicochemical and functional properties of whey protein isolate

Cited by 133 publications

References 35 publications

Covalent Whey Protein–Rosmarinic Acid Interactions: A Comparison of Alkaline and Enzymatic Modifications on Physicochemical, Antioxidative, and Antibacterial Properties

Covalent Whey Protein–Rosmarinic Acid Interactions: A Comparison of Alkaline and Enzymatic Modifications on Physicochemical, Antioxidative, and Antibacterial Properties

Interaction of Whey Proteins with Phenolic Derivatives Under Neutral and Acidic pH Conditions

Effect of removal of phenolic compounds on structural and thermal properties of sunflower protein isolate

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