Open AccessThe effects of sodium chloride on proteins aggregation, conformation and gel properties of pork myofibrillar protein Running Head: Relationship aggregation, conformation and gel properties
Author(s) -
ZhuangLi Kang,
Xuehua Zhang,
Xiang Li,
Zhaojun Song,
Haile Ma,
Fei Lü,
Meifang Zhu,
Shengming Zhao,
Zhengrong Wang
Publication year - 2020
Publication title -
journal of food science and technology/journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.656
H-Index - 68
eISSN - 0975-8402
pISSN - 0022-1155
DOI - 10.1007/s13197-020-04736-4
Subject(s) - myofibril , chemistry , sodium , protein aggregation , chloride , zeta potential , biophysics , chromatography , food science , biochemistry , organic chemistry , chemical engineering , biology , nanoparticle , engineering
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.