Biotechnology Letters, Vol.22, No.3, 197-199, 2000
Preparation of L-arabinose isomerase originated from Escherichia coli as a biocatalyst for D-tagatose production
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.