Effects of malondialdehyde-induced protein modification on water functionality and physicochemical state of fish myofibrillar protein gel

Wang, Lin, Zhang, Min, Bhandari, Bhesh and Gao, Zhongxue (2016) Effects of malondialdehyde-induced protein modification on water functionality and physicochemical state of fish myofibrillar protein gel. Food Research International, 86 131-139. doi:10.1016/j.foodres.2016.06.007

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Author Wang, Lin
Zhang, Min
Bhandari, Bhesh
Gao, Zhongxue
Title Effects of malondialdehyde-induced protein modification on water functionality and physicochemical state of fish myofibrillar protein gel
Journal name Food Research International   Check publisher's open access policy
ISSN 0963-9969
1873-7145
Publication date 2016-08-01
Year available 2016
Sub-type Article (original research)
DOI 10.1016/j.foodres.2016.06.007
Open Access Status File (Author Post-print)
Volume 86
Start page 131
End page 139
Total pages 9
Place of publication Kidlington, Oxford United Kingdom
Publisher Pergamon Press
Collection year 2017
Language eng
Formatted abstract
Effects of malondialdehyde (MDA)-induced modification on water distribution in fish myofibrillar proteins (MP) gels were investigated using nuclear magnetic resonance (NMR) and magnetic resonance imaging (MRI). The oxidative modifications of MP gels were evaluated by surface hydrophobicity, gel strength, water holding capacity (WHC), scanning electron microscopy (SEM) and SDS-PAGE. Influence of heating procedure on water distribution and functional properties of modified MP gels was also investigated. Results from NMR and MRI indicated that the water functionality was strongly affected by the modification level, which corresponded to the changes of water holding capacity of MP upon MDA modification. Compared with unmodified MP gels, the T2 relaxation times of modified sample increased significantly, indicating an alteration of water-protein interaction upon MDA-induced modification. The fraction of P23 declined from 7.66% to 0.15% as the MDA addition increased from 0 to 50 mM. Moreover, the relaxation components T2b disappeared with the addition of MDA mainly due to enhanced protein flexibility and surface hydrophobicity. Besides, the P23 (free water) of heated MP samples increased by 5.41 times compared with that of unheated MP samples.
Keyword Myofibrillar protein
Oxidation
Water mobility
Low-field NMR
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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