Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction

Peruško, Marija; Al-Hanish, Ayah; Mihailović, Jelena; Minić, Simeon; Trifunović, S.; Prodić, Ivana; Veličković, Tanja Ćirković

doi:10.1016/j.foodchem.2017.04.074

Cited by 40 publications

(5 citation statements)

References 40 publications

(59 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Then, K a of BBPI-G-EGCG was 5.91 × 10 4 M −1 and n was 1.02. This result showed that K a (both in the 10 4 range) and n of BBPI-G-EGCG were similar with those of BBPI-EGCG, which indicated that BBPI grafted with glucose did not affect the binding of protein and EGCG [17].…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

The Effect of (−)-Epigallocatechin-3-Gallate Non-Covalent Interaction with the Glycosylated Protein on the Emulsion Property

Feng¹,

Jin²,

Gao³

et al. 2019

Polymers

View full text Add to dashboard Cite

The effect of (−)-epigallocatechin-3-gallate (EGCG) on protein structure and emulsion properties of glycosylated black bean protein isolate (BBPI-G) were studied and compared to native black bean protein isolate (BBPI). The binding affinity of BBPI and BBPI-G with EGCG belonged to non-covalent interaction, which was determined by fluorescence quenching. EGCG attachment caused more disordered protein conformation, leading to a higher emulsification property. Among the different EGCG concentrations (0.10, 0.25, 0.50 mg/mL), the result revealed that the highest level of the emulsification property was obtained with 0.25 mg/mL EGCG. Therefore, the BBPI-EGCG and BBPI-G-EGCG prepared by 0.25 mg/mL EGCG were selected to fabricate oil-in-water (O/W) emulsions. After the addition of EGCG, the mean particle size of emulsions decreased with the increasing absolute value of zeta-potential, and more compact interfacial film was formed due to the higher percentage of interfacial protein adsorption (AP%). Meanwhile, EGCG also significantly reduced the lipid oxidation of emulsions.

show abstract

Section: Resultsmentioning

confidence: 99%

“…And then, the binding constant K a and the number of binding sites ( n ) can be calculated according to a double-logarithmic equation [17] as follows for the static quenching:log[F0−FF]=logKa+nlog[Q]…”

Section: Methodsmentioning

confidence: 99%

The Effect of (−)-Epigallocatechin-3-Gallate Non-Covalent Interaction with the Glycosylated Protein on the Emulsion Property

Feng¹,

Jin²,

Gao³

et al. 2019

Polymers

View full text Add to dashboard Cite

show abstract

“…In recent years, the research of proteins, carbohydrates and polyphenols have all became hot topics. Perusko et al 15 investigated the binding affinity of glycosylated b-lactoglobulin with EGCG through non-covalent interaction and the antioxidant properties of b-lactoglobulin-EGCG non-covalent complex. Results showed that the binding affinity between glycosylated b-lactoglobulin and EGCG was similar to that between b-lactoglobulin and EGCG.…”

Section: Introductionmentioning

confidence: 99%

Improvement of protein emulsion stability through glycosylated black bean protein covalent interaction with (−)-epigallocatechin-3-gallate

et al. 2021

View full text Add to dashboard Cite

show abstract

“…When K q is higher than diffusion‐limited rate constant (1 × 10 10 L M −1 s −1 ), it could indicate a static quenching between a protein and a quencher (Perusko et al, ). And thus, the binding parameters can be calculated according to a double‐logarithmic Stern–Volmer equation:

\log ([], ((), F_{0} - F) / F) = \log K_{a} + nlog ([], Q)

…”

Section: Methodsmentioning

confidence: 99%

Binding affinity and antioxidant activity of the complex of (‐)‐epigallocatechin‐3‐gallate and whey protein isolate: Effect of ultrasound pretreatment

Chen

Wang

et al. 2019

J Food Process Engineering

View full text Add to dashboard Cite

The binding affinity of whey protein isolate (WPI) for (-)-epigallocatechin-3-gallate (EGCG) and the antioxidant activity of the formed complexes as influenced by ultrasound pretreatment were investigated. After treated by ultrasound at 200 W for 20 min, the apparent binding constant and the number of binding sites could be increased by 10.92 times and 23.05%, respectively. This indicated that ultrasound pretreatment did enhance the binding interaction between WPI and EGCG. Ultrasound pretreatment could increase the random coil content, cause the molecular unfolding and expose more hydrophobic groups inside the molecules to be exposed to the surface. These ultrasound-induced conformational changes observed in WPI might account for its enhanced binding affinity for EGCG. Moreover, complexing with WPI could protect EGCG antioxidant activity and better protection was observed for that of ultrasound pretreated WPI. This study confirmed that ultrasound pretreatment could help the design of WPI based delivery system for EGCG. Practical applicationsDue to its good ligand-binding properties, whey protein isolate (WPI) have great potential being used as a protective carrier for (-)-epigallocatechin-3-gallate (EGCG) via the formation of WPI-EGCG complexes. As a relatively low-cost, nonhazardous, and ecofriendly technique, ultrasound has been widely applied in the modification of WPI. However, the interaction between WPI and EGCG as influenced by ultrasound pretreatment is still unknown. In this study, the effects of ultrasound pretreatment on binding capacity of WPI for EGCG and the antioxidant activity of the formed complex were investigated. The results showed that the binding interaction between WPI and EGCG could be enhanced by ultrasound pretreatment. Moreover, complexing with WPI could provide preservation of EGCG antioxidant activity and better protection were obtained by complexing EGCG with ultrasound pretreated WPI.These results were helpful for the utilization of WPI as a protective vehicle for EGCG and other polyphenols in food industry.

show abstract

Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction

Cited by 40 publications

References 40 publications

The Effect of (−)-Epigallocatechin-3-Gallate Non-Covalent Interaction with the Glycosylated Protein on the Emulsion Property

The Effect of (−)-Epigallocatechin-3-Gallate Non-Covalent Interaction with the Glycosylated Protein on the Emulsion Property

Improvement of protein emulsion stability through glycosylated black bean protein covalent interaction with (−)-epigallocatechin-3-gallate

Binding affinity and antioxidant activity of the complex of (‐)‐epigallocatechin‐3‐gallate and whey protein isolate: Effect of ultrasound pretreatment

Contact Info

Product

Resources

About