Abstract

The effects of brine salting on sturgeon muscle proteins were studied during the processing of salting at different levels of NaCl . The aim was to observe conformational stability and possible degradation or denaturation of sturgeon protein by determining the biochemical characteristics of protein using Fourier-transform-infrared spectroscopy( FTIR), sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), fluorescence and other means. The salting process significantly decreased the actomyosin content, Ca2+-ATPase activity,total and reactive sulfhydryls (SHs) and increased surface hydrophobicity of actomyosin. The results showed that the processing of salting salting induced the degradation or denaturation of actomyosin. From SDS–PAGE, actin was affected by salt to a lesser extent by the process than myosin heavy chain (MHC). From the FTIR, the secondary structure of protein changed significantly ,especiallyα-helix, at different levels of NaCl .

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