Ball-milling is an effective pretreatment of glycosylation modified the foaming and gel properties of egg white protein

Wu, Yongxiang; Zhang, Yufeng; Duan, Wenshan; Qia, Wang; An, Fengping; Luo, Peng; Huang, Qun

doi:10.1016/j.jfoodeng.2021.110908

Cited by 44 publications

(31 citation statements)

References 48 publications

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“…The amide II band shifted from 1536.99 to 1548.99 cm −1 , and the absorption peak of GSPI was stronger than SPI, indicating that the glycosylation product was formed by covalent bonds. This result was consistent with the results of glycosylated modified egg white protein pretreated by ball milling ( 40 ). The absorption intensity of GSPI was higher than SPI at the wavenumber of 1057.58 cm −1 , indicating that GSPI produces a new C–N covalent bond, which was consistent with the findings of WPI and inulin ( 25 ).…”

Section: Resultssupporting

confidence: 92%

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The Effect of Glycosylated Soy Protein Isolate on the Stability of Lutein and Their Interaction Characteristics

Wang

et al. 2022

Front. Nutr.

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Lutein is a natural fat-soluble carotenoid with various physiological functions. However, its poor water solubility and stability restrict its application in functional foods. The present study sought to analyze the stability and interaction mechanism of the complex glycosylated soy protein isolate (SPI) prepared using SPI and inulin-type fructans and lutein. The results showed that glycosylation reduced the fluorescence intensity and surface hydrophobicity of SPI but improved the emulsification process and solubility. Fluorescence intensity and ultraviolet–visible (UV–Vis) absorption spectroscopy results showed that the fluorescence quenching of the glycosylated soybean protein isolate by lutein was static. Through thermodynamic parameter analysis, it was found that lutein and glycosylated SPI were bound spontaneously through hydrophobic interaction, and the binding stoichiometry was 1:1. The X-ray diffraction analysis results showed that lutein existed in the glycosylated soybean protein isolate in an amorphous form. The Fourier transform infrared spectroscopy analysis results revealed that lutein had no effect on the secondary structure of glycosylated soy protein isolate. Meanwhile, the combination of lutein and glycosylated SPI improved the water solubility of lutein and the stability of light and heat.

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Section: Resultssupporting

confidence: 92%

“…Glycosylation is a chemical method for modifying proteins by covalent bonding between the proteins and sugars ( 40 ). The fluorescent substances with characteristic peaks between 340 and 370 nm are produced during a reaction ( 42 ).…”

Section: Resultsmentioning

confidence: 99%

The Effect of Glycosylated Soy Protein Isolate on the Stability of Lutein and Their Interaction Characteristics

Wang

et al. 2022

Front. Nutr.

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“…The determination of free amino content was slightly modified according to the method of Wu et al (2022) . The 200 µL amandin was added to 4 mL OPA reagent, and the absorbance was measured at 340 nm.…”

Section: Methodsmentioning

confidence: 99%

Reducing the potential allergenicity of amandin through binding to (−)-epigallocatechin gallate

Luo¹,

Lu²,

Wu³

et al. 2022

Food Chemistry: X

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“…Wu et al. (2022) investigated the effect of several treatments on EWP characteristics and proposed that ball milling is an effective pretreatment method for glycosylation.…”

Section: Introductionmentioning

confidence: 99%

“…Chen et al (2019) proposed that ultrasound-assisted could expedite the progress of glycosylation reaction and enhance solubility, thermal stability, and emulsification properties of whey protein graft copolymer. Wu et al (2022) investigated the effect of several treatments on EWP characteristics and proposed that ball milling is an effective pretreatment method for glycosylation.…”

Section: Introductionmentioning

confidence: 99%

Effect of ball milling‐assisted glycosylation modification on the structure and foaming property of egg white protein

Liu

Qia

et al. 2022

Journal of Food Science

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The effect of different glycosylation degrees on molecular structure and foaming property of egg white protein (EWP) was investigated using ball milling-assisted glycosylation. The results showed the foaming ability (FA) and foam stability (FS) of EWP improved when the degree of glycosylation was increased. In particular, FA of ball milling-assisted glycosylation of EWP enhanced by 39.9% and 28.8%, and the FS increased by 28.7% and 24.0% compared with EWP and ball milling egg white protein (BE) at 150 min of reaction.Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analysis could reflect the grafting degree of EWP and glucose molecules from the side. When EWP was fully grafted with glucose, endogenous fluorescence and free sulfhydryl groups indicated that tertiary structure of EWP was depolymerized, and Fourier transform infrared spectroscopy showed the secondary structure tended to change from order to disorder. The results of this study indicated that ball milling-assisted glycosylation modification was a practical method to improve the foaming property of EWP.

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Ball-milling is an effective pretreatment of glycosylation modified the foaming and gel properties of egg white protein

Cited by 44 publications

References 48 publications

The Effect of Glycosylated Soy Protein Isolate on the Stability of Lutein and Their Interaction Characteristics

The Effect of Glycosylated Soy Protein Isolate on the Stability of Lutein and Their Interaction Characteristics

Reducing the potential allergenicity of amandin through binding to (−)-epigallocatechin gallate

Effect of ball milling‐assisted glycosylation modification on the structure and foaming property of egg white protein

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