Unlocking the secrets of crude myofibril-bound serine protease from grass carp: The role in degrading myofibrillar proteins

Abstract

Grass carp (Ctenopharyngodon idella) are used as raw material for conventional surimi products in Southern China. However, endogenous serine proteases deteriorated the texture of the surimi gel. To unlock the mechanism behind, the present study isolated the crude myofibril-bound serine protease (cMBSP) in grass carp and studied its effects on surimi gel. The cMBSP activity was the highest at 40 °C and pH 8.0, and it remained stable at 20–55 °C neutral pH. Additionally, it was susceptible to serine protease inhibitors and high concentrations of Na+. The maximum degradation of myosin heavy chain by cMBSP was observed at 50 °C. Protein unc-45 homolog B (a myosin chaperone) is one of the apparent degradation products according to mass spectrometry. The cMBSP caused lower water holding capacity and deteriorated texture in the surimi gel. This study expanded insights about the mechanism of surimi gel degradation by cMBSP, which provided theoretical basis for enhancing surimi quality.