@article{oai:repo.qst.go.jp:00049206,
 author = {Amreta, Laksmi Fina and 新井, 栄揮 and Tsurumaru, Hirohito and Nakamura, Yoshitaka and Saksono, Budi and Tokunaga, Masao and Ishibashi, Matsujiro and 新井 栄揮},
 journal = {BBA Proteins and Proteomics},
 month = {Oct},
 note = {L-Arabinose isomerase isolated from Geobacillus stearothermophilus (GSAI) was modified to improve its substrate specificity for D-galactose for the production of D-tagatose, a potential reduced-energy sweetener. 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. Analysis of the substrate specificity of H18T showed a 45.4% improvement for D-galactose. Replacing histidine with threonine at residue 18 resulted in approximately 2.7-fold and 1.8-fold higher substrate binding and catalytic efficiency, respectively, for D-galactose. Further enhancement of the specific activity and catalytic efficiency of H18T for D-galactose by up to 2.7-fold and 4.3- fold, respectively, was achieved by adding borate during L-arabinose isomerase catalysis. Moreover, H18T showed thermostability and no destabilization was detected, which is promising for the industrial production of D-tagatose},
 pages = {1084--1091},
 title = {Improved substrate specificity for D-galactose of L-arabinose isomerase for industrial application},
 volume = {1866},
 year = {2018}
}