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
刊名APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
2016-06-01
卷号100期号:11页码:4923-4934
关键词Endo-1,3(4)-beta-glucanase Thermostable Caldicellulosiruptor Yeast lysis Glycoside hydrolase
英文摘要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.
WOS标题词Science & Technology ; Life Sciences & Biomedicine
类目[WOS]Biotechnology & Applied Microbiology
研究领域[WOS]Biotechnology & Applied Microbiology
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记录号WOS:000376255200017
内容类型期刊论文
源URL[http://ir.qibebt.ac.cn/handle/337004/8279]  
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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