Preparation of L-arabinose isomerase originated from Escherichia coli as a biocatalyst for D-tagatose production.

摘要

L-Arabinose isomerase for tagatose production from recombinant Escherichia coli was partially purified 15-fold with a specific activity of 70 U mg-1 protein. The purified enzyme had a major band when it was subjected to SDS/PAGE. With the purified L-arabinose isomerase, 17.7 g tagatose l-1 was produced from 50 g galactose l-1 in 168 h which corresponds to a 34% equilibrium.