A structural explanation for enhanced binding behaviors between β-lactoglobulin and alkene-aldehydes upon heat- and ultrasonication-induced protein unfolding

Author:

Xu Le,Zheng Yuanrong,Zhou Changyu,Pan DaodongORCID,Geng FangORCID,Cao Jinxuan,Xia QiangORCID

Funder

National Natural Science Foundation of China

Zhejiang Province Natural Science Foundation

Publisher

Elsevier BV

Subject

General Chemical Engineering,General Chemistry,Food Science

Reference41 articles.

1. Binding parameters and molecular dynamics of β-lactoglobulin-vanillic acid complexation as a function of pH - Part A: Acidic pH;Abdollahi;Food Chemistry,2021

2. Covalent adduct formation between flavor compounds of various functional group classes and the model protein β-lactoglobulin;Anantharamkrishnan;Journal of Agricultural and Food Chemistry,2020

3. Method to characterize and monitor covalent interactions of flavor compounds with β-lactoglobulin using mass spectrometry and proteomics;Anantharamkrishnan;Journal of Agricultural and Food Chemistry,2020

4. The effects of high-intensity ultrasound on the structural and functional properties of α-lactalbumin, β-lactoglobulin and their mixtures;Chandrapala;Food Research International,2012

5. Structure, oligomerisation and interactions of β-lactoglobulin. Milk proteins-from structure to biological properties and health aspects;Crowther,2016

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