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
Language eng
Subject 1305 Biotechnology
1106 Food Science
1102 Agronomy and Crop Science
2916 Nutrition and Dietetics
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 10 mmol L, the MP gels showed an improved elasticity, gel strength, water holding capacity, and oxidative stability. Nevertheless, higher MDA concentration (25–50 mmol L) 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.
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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