Temperature-driven divergence in molecular distribution and microbial invasion and the associated texture softening during dual-phase fermentation of Paocai.

Temperature is an important driving force that shapes the texture of fermented vegetables through driving the molecular distribution and microbial invasion between the liquid phase (brine) and the solid phase (vegetables) during fermentation. The objective of this study was to investigate the texture softening by investigating firmness, microstructure, physicochemical properties, molecular distribution and microbial community between brine and vegetables of Paocai as affected by fermentation temperatures of 10 °C, 20 °C and 30 °C. Results demonstrated that, compared with 10 °C and 30 °C, 20 °C attenuated softening of Paocai by restraining microbial invasion and suppressing pectinolysis. Moreover, at 20 °C, a balanced molecular distribution and microbial community were achieved between vegetables and brine, thus accomplishing acid-production fermentation. By contrast, 10 °C and 30 °C promoted nonfermentative microbial genera, retarding fermentation. This study provided an understanding of the divergent influence of temperature on quality formation of fermented vegetables during fermentation.

Phosphoproteomic insight into the changes in structural proteins of muscle architecture associated with texture softening of grass carp (Ctenopharyngodon idella) fillets during chilling storage.

Texture is an important sensory attribute of fish affected by modifications of structural proteins in muscle architecture. To investigate the changes in protein phosphorylation during texture softening of fish, the proteins of grass carp muscle after chilling storage of 0 day and 6 days were compared by phosphoproteomics, and their association with texture was analyzed. Totally 1026 unique phosphopeptides on 656 phosphoproteins were identified as differential. They were mainly classified as intracellular myofibril and cytoskeleton, and extracellular matrix, of which the molecular function and biological process were binding into supramolecular assembly and myofilament contraction. The concomitant dephosphorylation of kinases and assembly regulators indicated dephosphorylation and disassembly tendency of sarcomeric architecture. Correlation analysis defined the relation between texture and dephosphorylation of myosin light chain, actin, collagen and cytoskeleton. This study revealed that protein phosphorylation may affect the texture of fish muscle through regulating sarcomeric assembly of structural proteins in muscle architecture.