A novel thermostable α-1,3-glucanase from Streptomyces thermodiastaticus HF 3-3

The Journal of General and Applied Microbiology

Wasana Suyotha¹  Kazuyoshi Takagi²  Shigekazu Yano³  Mamoru Wakayama⁴  Hidehisa Fujiki⁴  Vipavee Cherdvorapong⁴ 

[1] Biotechnology for Bioresource Utilization Laboratory, Department of Industrial Biotechnology, Faculty of Agro-industry, Prince of Songkla University;Department of Applied Chemistry, Faculty of Life Sciences, Ritsumeikan University;Department of Biochemical Engineering, Graduate School of Sciences and Engineering, Yamagata University;Department of Biotechnology, Faculty of Life Sciences, Ritsumeikan University

关键词: α-1,3-glucanase;    mycodextranase;    Streptomyces thermodiastaticus;    thermal stability;   

DOI  :  10.2323/jgam.2017.02.001

学科分类：微生物学和免疫学

来源: Applied Microbiology, Molecular and Cellulrar Biosciences Research Foundation

【 摘 要 】

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.

【 授权许可】

Unknown