@misc{oai:repo.qst.go.jp:00067009,
 author = {Amreta, Laksmi Fina and Arai, Shigeki and Tsurumaru, Hirohito and Ishibashi, Matsujiro and 新井 栄揮},
 month = {Dec},
 note = {【Purpose】D-Tagatose is a naturally occurring ketohexose considered to be a potential reduced-energy sweetener. For industrial application, we will modify L-arabinose isomerase (L-AI) from a thermophilic microorganism, Geobacillus stearothermophilus to improve its substrate specificity for D-galactose for the production of D-tagatose.
【Method and Result】Analysis of residues around the binding pocket was conducted using molecular operating environment (MOE) software, and modification of L-AI was performed using saturation mutagenesis. Among the selected residues, mutation at residue 18 produced a mutant strain, H18T, which exhibited increased activity for D-galactose compared with the wild-type (WT) enzyme. H18T exhibited higher substrate binding and catalytic efficiency of about 2.7-fold and 1.8-fold, respectively, for D-galactose. H18T demonstrated improved substrate specificity for D-galactose by up to 45.4%., 第25回日本生物工学会 九州支部鹿児島大会},
 title = {Improved substrate specificity for D-galactose of L-arabinose isomerase for industrial application},
 year = {2018}
}