Function of aspartic acid residues in optimum pH control of l-arabinose isomerase from Lactobacillus fermentum

@article{Xu2013FunctionOA,
  title={Function of aspartic acid residues in optimum pH control of l-arabinose isomerase from Lactobacillus fermentum},
  author={Zheng Xu and Sha Li and Xiaohai Feng and Yijing Zhan and Hong A Xu},
  journal={Applied Microbiology and Biotechnology},
  year={2013},
  volume={98},
  pages={3987-3996}
}
l-Arabinose isomerase (l-AI) catalyzes the isomerization of l-arabinose to l-ribulose and d-galactose to d-tagatose. Most reported l-AIs exhibit neutral or alkaline optimum pH, which is less beneficial than acidophilic ones in industrial d-tagatose production. Lactobacillus fermentum l-AI (LFAI) is a thermostable enzyme that can achieve a high conversion rate for d-galactose isomerization. However, its biocatalytic activity at acidic conditions can still be further improved. In this study, we… CONTINUE READING