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Myosin affects the structure and volatile flavour compounds binding of G‐actin in grass carp
Author(s) -
Lin Rufei,
Xiao Xiao,
Yue Yi,
Wang Ying,
Pan Daodong,
Wang Daoying,
Yang Qiuli,
He Jun,
Cao Jinxuan
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.14586
Subject(s) - myosin , chemistry , actin , biophysics , biochemistry , biology
Summary The effects of myosin (0, 0.2, 0.4, and 0.6 mg mL −1 ) on the protein structure and volatiles adsorption capacity of G‐actin from grass carp were investigated. The results showed that the myosin addition increased the surface hydrophobicity and sulfhydryl contents of G‐actin. The Raman spectroscopy analysis showed that the α‐helix and β‐sheet of G‐actin were converted into β‐turn and random coil with 0.2 and 0.4 mg mL −1 of myosin, while only the β‐turn content increased with 0.6 mg mL −1 of myosin. The GC‐MS analysis indicated that with myosin addition, the adsorption capacities of G‐actin on alcohols (1‐pantanol, 1‐hexanol, 1‐octen‐3‐ol, and 1‐octanol) and ketones (2‐pentanone, 2‐heptanone, 2‐octanone, and 2‐nonanone) were enhanced; meanwhile, the binding of G‐actin to aldehydes (pentanal, hexanal, octanal, and nonanal) was weakened. It was probably due to the formation of actomyosin, and also the excess myosin when treated with high concentrations (0.4 and 0.6 mg mL −1 ) of myosin.