Determination of the modes of action and synergies of xylanases by analysis of xylooligosaccharide profiles over time using fluorescence-assisted carbohydrate electrophoresis
文献类型：期刊论文
| 作者 | Gong, Weili1; Zhang, Huaiqiang1; Tian, Li1; Liu, Shijia2; Wu, Xiuyun1; Li, Fuli3 ; Wang, Lushan1
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| 刊名 | ELECTROPHORESIS
 |
| 出版日期 | 2016-07-01 |
| 卷号 | 37期号:12页码:1640-1650 |
| 关键词 | beta-Xylosidase Fluorescence-assisted carbohydrate electrophoresis Mode of action Synergies Xylanase |
| 英文摘要 | 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. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine ; Physical Sciences |
| 类目[WOS] | Biochemical Research Methods ; Chemistry, Analytical |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Chemistry |
| 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记录号 | WOS:000379132300005 |
| 源URL | [http://ir.qibebt.ac.cn/handle/337004/8360]  |
| 专题 | 青岛生物能源与过程研究所_微生物资源团队 |
| 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 |
| 推荐引用方式 GB/T 7714 | 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. |
入库方式： OAI收割
来源：青岛生物能源与过程研究所
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