Glutathione-mediated formation of disulfide bonds modulates the properties of myofibrillar protein gels at different temperatures-Reference-Cited by-同舟云学术

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Glutathione-mediated formation of disulfide bonds modulates the properties of myofibrillar protein gels at different temperatures

Published:2021-12 Issue: Volume:364 Page:130356
ISSN:0308-8146
Container-title:Food Chemistry
language:en
Short-container-title:Food Chemistry

Author:

Chen Bo,Zhou Kai,Xie Yong,Nie Wen,Li Peijun,Zhou Hui,Xu Baocai

Funder

National Natural Science Foundation of China

Natural Science Foundation of Anhui Province

National Key Research and Development Program of China

Fundamental Research Funds for the Central Universities

Publisher

Elsevier BV

Subject

General Medicine,Food Science,Analytical Chemistry

Reference40 articles.

1. Raman spectroscopy of disulfide bridges in thrombin;Brandt;Biomedical Spectroscopy and Imaging,2014

2. Do sulfhydryl groups affect aggregation and gelation properties of ovalbumin?;Broersen;Journal of Agricultural and Food Chemistry,2006

3. Modulating the aggregation of myofibrillar protein to alleviate the textural deterioration of protein gels at high temperature: The effect of hydrophobic interactions;Chen;Food Chemistry,2021

4. Insight into the mechanism of textural deterioration of myofibrillar protein gels at high temperature conditions;Chen;Food Chemistry,2020

5. Globular protein gelation-theory and experiment;Clark;Food Hydrocolloids,2001

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