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Improved substrate specificity for D-galactose of L-arabinose isomerase for industrial application
https://repo.qst.go.jp/records/67009
https://repo.qst.go.jp/records/6700931f8d811-9602-4b41-8df9-723563c1b46a
| Item type | 会議発表用資料 / Presentation(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2018-11-28 | |||||
| タイトル | ||||||
| タイトル | Improved substrate specificity for D-galactose of L-arabinose isomerase for industrial application | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_c94f | |||||
| 資源タイプ | conference object | |||||
| アクセス権 | ||||||
| アクセス権 | metadata only access | |||||
| アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||
| 著者 |
Amreta, Laksmi Fina
× Amreta, Laksmi Fina× Arai, Shigeki× Tsurumaru, Hirohito× Ishibashi, Matsujiro× 新井 栄揮 |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | 【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%. |
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| 会議概要（会議名, 開催地, 会期, 主催者等） | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | 第25回日本生物工学会 九州支部鹿児島大会 | |||||
| 発表年月日 | ||||||
| 日付 | 2018-12-01 | |||||
| 日付タイプ | Issued | |||||
