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Structures and properties of chicken myofibrillar protein gel induced by microwave heating
Author(s) -
Wei Sumeng,
Yang Yuling,
Feng Xiao,
Li Shanshan,
Zhou Lei,
Wang Jingyu,
Tang Xiaozhi
Publication year - 2020
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.14522
Subject(s) - myofibril , microwave , microwave power , chemistry , materials science , morphology (biology) , biophysics , chemical engineering , crystallography , biochemistry , biology , physics , quantum mechanics , engineering , genetics
Summary Structures and properties of myofibrillar protein gel prepared at different power (300–800 W) were evaluated. Amino acid analysis demonstrated that changes in microwave power did not alter primary structure of gel. However, an increase in microwave power could change higher structures of gel. As microwave power increased, α‐helix content decreased and β‐sheet content increased. Increased microwave power probably facilitated protein to unfold and expose the internal groups, causing surface hydrophobicity and the formation of disulphide bonds were enhanced, which indicated changes in tertiary and quaternary structures of protein. At 500 W, gel had the best ultrastructure where surface morphology, springiness and water holding capacity reached the optimum. Our findings suggested that microwave at an appropriate power (500 W) could change higher structures of myofibrillar protein gel to achieve desired processing and quality protein gel characteristics.