A novel thermostable alpha-1,3-glucanase from Streptomyces thermodiastaticus HF 3-3
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- Suyotha Wasana
- Biotechnology for Bioresource Utilization Laboratory, Department of Industrial Biotechnology, Faculty of Agro-industry, Prince of Songkla University
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- Fujiki Hidehisa
- Department of Biotechnology, Faculty of Life Sciences, Ritsumeikan University
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- Cherdvorapong Vipavee
- Department of Biotechnology, Faculty of Life Sciences, Ritsumeikan University
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- Takagi Kazuyoshi
- Department of Applied Chemistry, Faculty of Life Sciences, Ritsumeikan University
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- Yano Shigekazu
- Department of Biochemical Engineering, Graduate School of Sciences and Engineering, Yamagata University
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- Wakayama Mamoru
- Department of Biotechnology, Faculty of Life Sciences, Ritsumeikan University
書誌事項
- タイトル別名
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- A novel thermostable α-1,3-glucanase from <i>Streptomyces thermodiastaticus</i> HF 3-3
抄録
<p>Thermally stable α-1,3-glucanase HF65 was purified from culture filtrate of Streptomyces thermodiastaticus HF3-3. The molecular mass of this enzyme was estimated to be 65 kDa and 45.7 kDa by using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and size exclusion chromatography, respectively. The purified enzyme retained more than 50% of maximum activity even after incubation at 65°C more than 2 h. Moreover, α-1,3-glucanase HF65 was stable in the presence of chemicals like SDS, benzethonium chloride, and sodium fluoride at a concentration of 1%. The enzyme also exhibited salt tolerance at a concentration up to 20%. The observed stability of α-1,3-glucanase HF65 to salt and surfactants is a great advantage for its addition to commercial oral care products. Interestingly, the N-terminal amino acid sequence did not show any similarity to those of known α-1,3-glucanases, while the sequence of internal eight amino acid residues of this enzyme was homologous with those of mycodextranases. Nevertheless, the enzyme exhibited high specificity against α-1,3-glucan. According to these results, the enzyme purified from S. thermodiastaticus HF3-3 was classified as α-1,3-glucanase which was highly homologous to mycodextranase in amino acid sequence.</p>
収録刊行物
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- The Journal of General and Applied Microbiology
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The Journal of General and Applied Microbiology 63 (5), 296-304, 2017
公益財団法人 応用微生物学・分子細胞生物学研究奨励会