The function of uridine diphosphate glucose pyrophosphorylase in the lyophilization-stress response of Lactobacillus acidophilus

Abstract Purpose Uridine diphosphate glucose pyrophosphorylase (UGPase) plays an important role in metabolism, catalyzing the reversible formation and decomposition of UDP-glucose (UDPG). In previous work, we found that UGPase is a key enzyme lyophilization response for Lactobacillus acidophilus ( L. ). However, its function regulatory mechanism freeze-drying stress are unknown. Herein, effect on survival rate Staphylococcus carnosus S. ) was studied. Methods this genes LBA 1719 encoding ATCC4356 were inserted into plasmid pMG-36e to construct recombinant pMG-LBA1719 then overexpressed ; control group transformed by pMG-36e. The lyophilization-survival determined, differentially expressed (DEGs) analyzed transcriptome disclose regulating rate. Results Compared with group, activities increased 35.49%, while rates decreased 11.17% p < 0.05). Overexpression expression gap A, B, pgi A carbohydrate metabolism dap E amino acid significantly changing physiological characteristics decreasing Conclusion summary, overexpression accelerated growth reduced rates. Gap vital protection lactic bacteria (LAB). These findings provide new theoretical basis analyzing molecular mechanisms resistance LABs.