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Determination of the modes of action and synergies of xylanases by analysis of xylooligosaccharide profiles over time using fluorescence-assisted carbohydrate electrophoresis
Gong, Weili1; Zhang, Huaiqiang1; Tian, Li1; Liu, Shijia2; Wu, Xiuyun1; Li, Fuli3; Wang, Lushan1
2016-07-01
发表期刊ELECTROPHORESIS
卷号37期号:12页码:1640-1650
摘要The structure of xylan, which has a 1,4-linked beta-xylose backbone with various substituents, is much more heterogeneous and complex than that of cellulose. Because of this, complete degradation of xylan needs a large number of enzymes that includes GH10, GH11, and GH3 family xylanases together with auxiliary enzymes. Fluorescence-assisted carbohydrate electrophoresis (FACE) is able to accurately differentiate unsubstituted and substituted xylooligosaccharides (XOS) in the heterogeneous products generated by different xylanases and allows changes in concentrations of specific XOS to be analyzed quantitatively. Based on a quantitative analysis of XOS profiles over time using FACE, we have demonstrated that GH10 and GH11 family xylanases immediately degrade xylan into sizeable XOS, which are converted into smaller XOS in a much lower speed. The shortest substituted XOS produced by hydrolysis of the substituted xylan backbone by GH10 and GH11 family xylanases were MeGlcA(2)Xyl(3) and MeGlcA(2)Xyl(4), respectively. The unsubstituted xylan backbone was degraded into xylose, xylobiose, and xylotriose by both GH10 and GH11 family xylanases; the product profiles are not family-specific but, instead, depend on different subsite binding affinities in the active sites of individual enzymes. Synergystic action between xylanases and beta-xylosidase degraded MeGlcA(2)Xyl(4) into xylose and MeGlcA(2)Xyl(3) but further degradation of MeGlcA(2)Xyl(3) required additional enzymes. Synergy between xylanases and beta-xylosidase was also found to significantly accelerate the conversion of XOS into xylose.
文章类型Article
关键词Beta-xylosidase Fluorescence-assisted Carbohydrate Electrophoresis Mode Of Action Synergies Xylanase
WOS标题词Science & Technology ; Life Sciences & Biomedicine ; Physical Sciences
DOI10.1002/elps.201600041
关键词[WOS]ASPERGILLUS-NIGER ; POLYSACCHARIDE ANALYSIS ; GEL-ELECTROPHORESIS ; TRICHODERMA-REESEI ; THERMOMYCES-LANUGINOSUS ; INDUSTRIAL APPLICATIONS ; XYLO-OLIGOSACCHARIDES ; GLYCOSIDE HYDROLASES ; SECRETOME ANALYSIS ; PICHIA-PASTORIS
收录类别SCI
语种英语
WOS研究方向Biochemistry & Molecular Biology ; Chemistry
WOS类目Biochemical Research Methods ; Chemistry, Analytical
WOS记录号WOS:000379132300005
引用统计
文献类型期刊论文
条目标识符http://ir.qibebt.ac.cn/handle/337004/8360
专题分子微生物工程研究组
作者单位1.Shandong Univ, State Key Lab Microbial Technol, 27 Shandanan Rd, Jinan 250100, Shandong, Peoples R China
2.Shandong Univ, Taishan Coll, Jinan, Shandong, Peoples R China
3.Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, Key Lab Biofuels, Qingdao, Peoples R China
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Gong, Weili,Zhang, Huaiqiang,Tian, Li,et al. Determination of the modes of action and synergies of xylanases by analysis of xylooligosaccharide profiles over time using fluorescence-assisted carbohydrate electrophoresis[J]. ELECTROPHORESIS,2016,37(12):1640-1650.
APA Gong, Weili.,Zhang, Huaiqiang.,Tian, Li.,Liu, Shijia.,Wu, Xiuyun.,...&Wang, Lushan.(2016).Determination of the modes of action and synergies of xylanases by analysis of xylooligosaccharide profiles over time using fluorescence-assisted carbohydrate electrophoresis.ELECTROPHORESIS,37(12),1640-1650.
MLA Gong, Weili,et al."Determination of the modes of action and synergies of xylanases by analysis of xylooligosaccharide profiles over time using fluorescence-assisted carbohydrate electrophoresis".ELECTROPHORESIS 37.12(2016):1640-1650.
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