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

Content Provider	Europe PMC
Author	Kang, Zhuang-Li Zhang, Xue-hua Li, Xiang Song, Zhao-jun Ma, Han-jun Lu, Fei Zhu, Ming-ming zhao, Sheng-ming Wang, Zheng-rong
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.
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ISSN	00221155
Volume Number	58
DOI	10.1007/s13197-020-04736-4
PubMed Central reference number	PMC8076348
Issue Number	6
PubMed reference number	33967322
Journal	Journal of Food Science and Technology [J Food Sci Technol]
e-ISSN	09758402
Language	English
Publisher	Springer India
Publisher Date	2020-08-25
Publisher Place	New Delhi
Access Restriction	Open
Rights License	© Association of Food Scientists & Technologists (India) 2020
Subject Keyword	Myofibrillar Sodium chloride Aggregation Texture Gel properties
Content Type	Text
Resource Type	Article
Subject	Food Science