The effects of sodium chloride on proteins aggregation, conformation and gel properties of pork myofibrillar protein Running Head: Relationship aggregation, conformation and gel properties
JOURNAL OF FOOD SCIENCE AND TECHNOLOGY-MYSORE(2020)
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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Key words
Myofibrillar,Sodium chloride,Aggregation,Texture,Gel properties
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