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Enzymology and Protein Engineering

A C-Terminal Proline-Rich Sequence Simultaneously Broadens the Optimal Temperature and pH Ranges and Improves the Catalytic Efficiency of Glycosyl Hydrolase Family 10 Ruminal Xylanases

Zhongyuan Li, Xianli Xue, Heng Zhao, Peilong Yang, Huiying Luo, Junqi Zhao, Huoqing Huang, Bin Yao
F. E. Löffler, Editor
Zhongyuan Li
aKey Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing, People's Republic of China
bKey Laboratory of Industrial Fermentation Microbiology, Tianjin University of Science and Technology, Tianjin, People's Republic of China
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Xianli Xue
aKey Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing, People's Republic of China
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Heng Zhao
aKey Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing, People's Republic of China
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Peilong Yang
aKey Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing, People's Republic of China
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Huiying Luo
aKey Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing, People's Republic of China
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Junqi Zhao
cNational Engineering Laboratory for Industrial Enzymes, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, People's Republic of China
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Huoqing Huang
aKey Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing, People's Republic of China
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Bin Yao
aKey Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing, People's Republic of China
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F. E. Löffler
Roles: Editor
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DOI: 10.1128/AEM.00016-14
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ABSTRACT

Efficient degradation of plant polysaccharides in rumen requires xylanolytic enzymes with a high catalytic capacity. In this study, a full-length xylanase gene (xynA) was retrieved from the sheep rumen. The deduced XynA sequence contains a putative signal peptide, a catalytic motif of glycoside hydrolase family 10 (GH10), and an extra C-terminal proline-rich sequence without a homolog. To determine its function, both mature XynA and its C terminus-truncated mutant, XynA-Tr, were expressed in Escherichia coli. The C-terminal oligopeptide had significant effects on the function and structure of XynA. Compared with XynA-Tr, XynA exhibited improved specific activity (12-fold) and catalytic efficiency (14-fold), a higher temperature optimum (50°C versus 45°C), and broader ranges of temperature and pH optima (pH 5.0 to 7.5 and 40 to 60°C versus pH 5.5 to 6.5 and 40 to 50°C). Moreover, XynA released more xylose than XynA-Tr when using beech wood xylan and wheat arabinoxylan as the substrate. The underlying mechanisms responsible for these changes were analyzed by substrate binding assay, circular dichroism (CD) spectroscopy, isothermal titration calorimetry (ITC), and xylooligosaccharide hydrolysis. XynA had no ability to bind to any of the tested soluble and insoluble polysaccharides. However, it contained more α helices and had a greater affinity and catalytic efficiency toward xylooligosaccharides, which benefited complete substrate degradation. Similar results were obtained when the C-terminal sequence was fused to another GH10 xylanase from sheep rumen. This study reveals an engineering strategy to improve the catalytic performance of enzymes.

FOOTNOTES

    • Received 3 January 2014.
    • Accepted 17 March 2014.
    • Accepted manuscript posted online 21 March 2014.
  • Supplemental material for this article may be found at http://dx.doi.org/10.1128/AEM.00016-14.

  • Copyright © 2014, American Society for Microbiology. All Rights Reserved.
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A C-Terminal Proline-Rich Sequence Simultaneously Broadens the Optimal Temperature and pH Ranges and Improves the Catalytic Efficiency of Glycosyl Hydrolase Family 10 Ruminal Xylanases
Zhongyuan Li, Xianli Xue, Heng Zhao, Peilong Yang, Huiying Luo, Junqi Zhao, Huoqing Huang, Bin Yao
Applied and Environmental Microbiology May 2014, 80 (11) 3426-3432; DOI: 10.1128/AEM.00016-14

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A C-Terminal Proline-Rich Sequence Simultaneously Broadens the Optimal Temperature and pH Ranges and Improves the Catalytic Efficiency of Glycosyl Hydrolase Family 10 Ruminal Xylanases
Zhongyuan Li, Xianli Xue, Heng Zhao, Peilong Yang, Huiying Luo, Junqi Zhao, Huoqing Huang, Bin Yao
Applied and Environmental Microbiology May 2014, 80 (11) 3426-3432; DOI: 10.1128/AEM.00016-14
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