Myosin affects the structure and volatile flavour compounds binding of G‐actin in grass carp
Rufei Lin, Xiao Xiao, Yue Yi, Ying Wang, Daodong Pan, Daoying Wang, Qiuli Yang, Jun He, Jinxuan Cao
Abstract
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.