Gelation properties of myofibrillar protein under malondialdehyde-induced oxidative stress

Wang, Lin, Zhang, Min, Fang, Zhongxiang and Bhandari, Bhesh (2016) Gelation properties of myofibrillar protein under malondialdehyde-induced oxidative stress. Journal of the Science of Food and Agriculture, 97 1: 50-57. doi:10.1002/jsfa.7680


Author Wang, Lin
Zhang, Min
Fang, Zhongxiang
Bhandari, Bhesh
Title Gelation properties of myofibrillar protein under malondialdehyde-induced oxidative stress
Journal name Journal of the Science of Food and Agriculture   Check publisher's open access policy
ISSN 1097-0010
0022-5142
Publication date 2016-04-13
Year available 2016
Sub-type Article (original research)
DOI 10.1002/jsfa.7680
Open Access Status Not Open Access
Volume 97
Issue 1
Start page 50
End page 57
Total pages 8
Place of publication Chichester, West Sussex, United Kingdom
Publisher John Wiley & Sons
Collection year 2017
Language eng
Formatted abstract
Background: The structure of myofibrillar protein (MP) can be readily altered by oxidation, leading to the unfolding of MP structure, which further promotes protein-protein interactions, and thus influences the MP gelling properties. The objective of the study was to investigate the effect of malondialdehyde-induced oxidative stress on the gelation properties of myofibrillar protein (MP). Structural changes of the oxidised MPs were evaluated by the contents of carbonyl and total sulfhydryls, surface hydrophobicity, SDS-PAGE and Fourier transform infrared spectroscopy. The oxidative stability of the MP gels as indicated by lipid hydroperoxide was also determined.

Results: With the addition of an MDA concentration less than 10mmolL-1, the MP gels showed an improved elasticity, gel strength, water holding capacity, and oxidative stability. Nevertheless, higher MDA concentration (25-50mmolL-1) significantly reduced the gel quality, probably due to the formation of excessive covalent bonds in the system.

Conclusion: Results suggested that protein aggregation occurred in the oxidised system. Myosin was involved in gel formation through non-disulfide covalent bond.
Keyword Gelation
Malondialdehyde
Myofibrillar protein
Protein oxidation
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
School of Agriculture and Food Sciences
 
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