Characterization of a thermostable endo-1,3(4)-beta-glucanase from Caldicellulosiruptor sp strain F32 and its application for yeast lysis | |
Meng, Dong-Dong; Wang, Bing; Ma, Xiao-Qing; Ji, Shi-Qi; Lu, Ming; Li, Fu-Li | |
2016-06-01 | |
发表期刊 | APPLIED MICROBIOLOGY AND BIOTECHNOLOGY |
卷号 | 100期号:11页码:4923-4934 |
摘要 | beta-1,3-Glucans, important structural components of cell wall or nutritional components of the endosperm, are extensively found in bacteria, fungi, yeast, algae, and plants. The structural complexity of beta-1,3-glucans implies that the enzymatic depolymerization of polysaccharides needs combined activities of distinct enzymes. In this study, Lam16A-GH, the catalytic module of a putative glycoside hydrolase (GH) family 16 laminarinase/lichenase from thermophilic bacterium Caldicellulosiruptor sp. F32, was purified and characterized through heterologous expression in Escherichia coli. Lam16A-GH can hydrolyze both beta-1,3-glucan (laminarin) and beta-1,3-1,4-glucan (barley beta-glucan) revealed by analysis of the products of polysaccharide degradation using thin-layer chromatography (TLC). The time required for the loss of 50 % of its activity is 45 h under the optimal condition of 75 A degrees C and pH 6.5. Oligosaccharides degradation assay indicated that Lam16A-GH can catalyze endo-hydrolysis of the beta-1,4 glycosidic linkage adjacent to a 3-O-substituted glucosyl residue in the mixed linked beta-glucans, as well as the beta-1,3 linkage. The survival rate of Saccharomyces cerevisiae cells depends on the addition of Lam16A-GH, and the cytoplasm protein was released from the apparently deconstructed yeast cells. These results indicate that the bi-functional thermostable Lam16A-GH exhibits unique enzymatic properties and potential for yeast lysis. |
文章类型 | Article |
关键词 | Thermostable Endo-1 Caldicellulosiruptor 3(4)-beta-glucanase Yeast Lysis Glycoside Hydrolase |
WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
DOI | 10.1007/s00253-016-7334-x |
关键词[WOS] | CELL-WALL ; CLOSTRIDIUM-THERMOCELLUM ; BIOCHEMICAL-CHARACTERIZATION ; THERMOPHILIC BACTERIUM ; MARINE BACTERIUM ; PAENIBACILLUS SP ; BINDING ; ENZYME ; BETA-1,3-GLUCANASE ; PURIFICATION |
收录类别 | SCI |
语种 | 英语 |
WOS研究方向 | Biotechnology & Applied Microbiology |
项目资助者 | Shandong Province Natural Science Funds for Distinguished Young Scholar(JQ201507) ; Key Scientific and Technological project of Shandong province(2015ZDXX0403A01) ; National Basic Research Program of China(2011CB707404) |
WOS类目 | Biotechnology & Applied Microbiology |
WOS记录号 | WOS:000376255200017 |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://ir.qibebt.ac.cn/handle/337004/8279 |
专题 | 分子微生物工程研究组 |
作者单位 | Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, Shandong Prov Key Lab Energy Genet, Key Lab Biofuels, Qingdao 266101, Peoples R China |
推荐引用方式 GB/T 7714 | Meng, Dong-Dong,Wang, Bing,Ma, Xiao-Qing,et al. Characterization of a thermostable endo-1,3(4)-beta-glucanase from Caldicellulosiruptor sp strain F32 and its application for yeast lysis[J]. APPLIED MICROBIOLOGY AND BIOTECHNOLOGY,2016,100(11):4923-4934. |
APA | Meng, Dong-Dong,Wang, Bing,Ma, Xiao-Qing,Ji, Shi-Qi,Lu, Ming,&Li, Fu-Li.(2016).Characterization of a thermostable endo-1,3(4)-beta-glucanase from Caldicellulosiruptor sp strain F32 and its application for yeast lysis.APPLIED MICROBIOLOGY AND BIOTECHNOLOGY,100(11),4923-4934. |
MLA | Meng, Dong-Dong,et al."Characterization of a thermostable endo-1,3(4)-beta-glucanase from Caldicellulosiruptor sp strain F32 and its application for yeast lysis".APPLIED MICROBIOLOGY AND BIOTECHNOLOGY 100.11(2016):4923-4934. |
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