A high-molecular-weight, alkaline, and thermostable beta-1,4-xylanase of a subseafloor Microcella alkaliphila

作者：Kuramochi Koki; Uchimura Kohsuke; Kurata Atsushi; Kobayashi Tohru^*; Hirose Yuu; Miura Takeshi; Kishimoto Noriaki; Usami Ron; Horikoshi Koki

来源：Extremophiles, 2016, 20(4): 471-478.

DOI：10.1007/s00792-016-0837-7

• Xylanase
• Deep subseafloor
• Alkaline
• Thermostable
• Microcella alkaliphila
• Chikyu

An endo beta-1,4-xylanase (XynE15) from a culture broth of a deep subseafloor microorganism, Microcella alkaliphila JAM-AC0309, was purified to homogeneity. The molecular mass of XynE15 was approximately 150 kDa as judged by SDS-PAGE. The optimal pH and temperature for hydrolysis of xylan were pH 8 and 65 A degrees C. The enzyme was stable to incubation for 30 min at up to 75 A degrees C, and the half-life at 50 A degrees C was 48 h. XynE15 hydrolyzed arabinoxylan, oat spelt xylan, and birchwood xylan well, but not avicel, carboxymethylcellulose, or arabinan. Xylooligosaccharides were hydrolyzed to mainly xylobiose from higher than xylotetraose. The genome sequencing analysis of strain JAM-AC03039 revealed that XynE15 was composed of 1,319 amino acids with one catalytic domain and three carbohydrate-binding domains belonging to glycoside hydrolase (GH) family 10 and carbohydrate-binding module (CBM) family 4, respectively.

• 出版日期2016-7