Improved substrate specificity for D-galactose of L-arabinose isomerase for industrial application
| Autor: | Amreta, Laksmi Fina, Arai, Shigeki, Tsurumaru, Hirohito, Ishibashi, Matsujiro |
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| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Popis: | 【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 |
| Databáze: | OpenAIRE |
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