The effects of sodium chloride on proteins aggregation, conformation and gel properties of pork myofibrillar protein Running Head: Relationship aggregation, conformation and gel properties

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ID: 111773
2020
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Abstract
The objective of this study was to evaluate relationship with aggregation, secondary structures and gel properties of pork myofibrillar protein with different sodium chloride (1%, 2% and 3%). When the sodium chloride increased from 1 to 3%, the active sulfhydryl, surface hydrophobicity, hardness and cooking yield of myofibrillar protein were increased significantly (p < 0.05), the particle size, total sulfhydryl and Zeta potential were decreased significantly (p < 0.05), these meant the aggregations of pork myofibrillar protein were decreased. The changes of proteins aggregation induced the strongest intensity band of Amide I shifted up from 1660 cm−1 to 1661 cm−1, meanwhile, the β-sheet structure content was increased significantly (p < 0.05) with the sodium chloride increased. From the above, the lower proteins aggregation and higher β-sheet structure content could improve the water holding capacity and texture of pork myofibrillar protein gel.
Reference Key
kang2020journalthe Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Zhuang-Li Kang;Xue-hua Zhang;Xiang Li;Zhao-jun Song;Han-jun Ma;Fei Lu;Ming-ming Zhu;Sheng-ming zhao;Zheng-rong Wang;Zhuang-Li Kang;Xue-hua Zhang;Xiang Li;Zhao-jun Song;Han-jun Ma;Fei Lu;Ming-ming Zhu;Sheng-ming zhao;Zheng-rong Wang;
Journal Journal of food science and technology
Year 2020
DOI
doi:10.1007/s13197-020-04736-4
URL
https://link.springer.com/article/10.1007/s13197-020-04736-4
Keywords
food science nutrition general chemistry/food science

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