Biocatalytic Properties and Substrate-binding Ability of a Modular GH10 β-1,4-Xylanase from an Insect-symbiotic Bacterium, Streptomyces mexicanus HY-14

Do Young Kim; Dong-Ha Shin; Sora Jung; Jong Suk Lee; Han-Young Cho; Kyung Sook Bae; Chang-Keun Sung; Young Ha Rhee; Kwang-Hee Son; Ho-Yong Park

doi:10.1007/s12275-014-4390-8

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Research Support, Non-U.S. Gov't
Biocatalytic Properties and Substrate-binding Ability of a Modular GH10 β-1,4-Xylanase from an Insect-symbiotic Bacterium, Streptomyces mexicanus HY-14: Do Young Kim ¹, Dong-Ha Shin ^2,3, Sora Jung ¹, Jong Suk Lee ⁴, Han-Young Cho ¹, Kyung Sook Bae ⁵, Chang-Keun Sung ³, Young Ha Rhee ⁶, Kwang-Hee Son ¹, Ho-Yong Park ¹; Journal of Microbiology 2014;52(10):863-870.
DOI: https://doi.org/10.1007/s12275-014-4390-8
Published online: October 1, 2014

¹Industrial Bio-materials Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon 305-806, Republic of Korea, ²Insect Biotech Co. Ltd., Daejeon 305-811, Republic of Korea, ³Department of Food Science and Technology, Chungnam National University, Daejeon 305-764, Republic of Korea, ⁴Gyeonggi Bio-Center, Gyeonggi Institute of Science & Technology Promotion, Suwon 443-270, Republic of Korea, ⁵Microbial Resource Center, KRIBB, Daejeon 305-806, Republic of Korea, ⁶Department of Microbiology and Molecular Biology, Chungnam National University, Daejeon 305-764, Republic of Korea¹Industrial Bio-materials Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon 305-806, Republic of Korea, ²Insect Biotech Co. Ltd., Daejeon 305-811, Republic of Korea, ³Department of Food Science and Technology, Chungnam National University, Daejeon 305-764, Republic of Korea, ⁴Gyeonggi Bio-Center, Gyeonggi Institute of Science & Technology Promotion, Suwon 443-270, Republic of Korea, ⁵Microbial Resource Center, KRIBB, Daejeon 305-806, Republic of Korea, ⁶Department of Microbiology and Molecular Biology, Chungnam National University, Daejeon 305-764, Republic of Korea

Corresponding author: Kwang-Hee Son , Tel: +82-42-860-4650,
Ho-Yong Park , Tel: +82-42-860-4650,

Received: 2 July 2014 • Revised: 11 September 2014 • Accepted: 15 September 2014

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Abstract

The gene (1350-bp) encoding a modular β-1,4-xylanase (XylU), which consists of an N-terminal catalytic GH10 domain and a C-terminal carbohydrate-binding module 2 (CBM 2), from Streptomyces mexicanus HY-14 was cloned and functionally characterized. The purified His-tagged recombinant enzyme (rXylU, 44.0 kDa) was capable of efficiently hydrolyze diverse xylosidic compounds, p-nitrophenyl-cellobioside, and pnitrophenyl- xylopyranoside when incubated at pH 5.5 and 65°C. Especially, the specific activities (649.8 U/mg and 587.0 U/mg, respectively) of rXylU toward oat spelts xylan and beechwood xylan were relatively higher than those (<500.0 U/mg) of many other GH10 homologs toward the same substrates. The results of enzymatic degradation of birchwood xylan and xylooligosaccharides (xylotriose to xylohexaose) revealed that rXylU preferentially hydrolyzed the substrates to xylobiose (>75%) as the primary degradation product. Moreover, a small amount (4%<) of xylose was detected as the degradation product of the evaluated xylosidic substrates, indicating that rXylU was a peculiar GH10 β-1,4- xylanase with substrate specificity, which was different from its retaining homologs. A significant reduction of the binding ability of rXylU caused by deletion of the C-terminal CBM 2 to various insoluble substrates strongly suggested that the additional domain might considerably contribute to the enzyme-substrate interaction.

Keywords: Streptomyces mexicanus HY-14;β-1;4-xylanase;GH family 10;modular enzyme;binding ability

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Biocatalytic Properties and Substrate-binding Ability of a Modular GH10 β-1,4-Xylanase from an Insect-symbiotic Bacterium, Streptomyces mexicanus HY-14

J. Microbiol. 2014;52(10):863-870. Published online October 1, 2014

DOI: https://doi.org/10.1007/s12275-014-4390-8

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