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RISS 인기검색어
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- 저자 : Ziduo Liu (검색결과 3 건)
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Junli Dong,Yuzhi Hong,Ziduo Liu,Zongze Shao 한국미생물학회 2010 The journal of microbiology Vol.48 No.3
A novel gene encoding an endoglucanase designated Cel5D was cloned from a marine bacterium Martelella mediterranea by genomic library. The gene had a 1,113 bp opening reading frame encoding a 371-amino-acid protein with a molecular mass of 40,508 Da and containing a putative signal peptide (41 amino acids). Cel5D had low similarity (48-51% identity) with other known endoglucanases and consisted of one single catalytic domain, which belonged to the glycosyl hydrolase family 5. The maximum activity of Cel5D was observed at 60°C and pH 5.0. Cel5D displayed broad pH stability within the range of pH 3.0-11.0 and retained hydrolytic activity in the presence of a wide variety of metal ions and some chemical reagents. These characteristics suggest that the enzyme has considerable potential in industrial applications.
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Lu Li,Jiawen Zhu,Kui Yang,Zhuofei Xu,Ziduo Liu,Rui Zhou 한국미생물학회 2014 The journal of microbiology Vol.52 No.6
Actinobacillus pleuropneumoniae is an important porcinerespiratory pathogen causing great economic losses in thepig industry worldwide. Oxygen deprivation is a stress thatA. pleuropneumoniae will encounter during both early infectionand the later, persistent stage. To understand modulationof A. pleuropneumoniae gene expression in responseto the stress caused by anaerobic conditions, gene expressionprofiles under anaerobic and aerobic conditions werecompared in this study. The microarray results showed that631 genes (27.7% of the total ORFs) were differentially expressedin anaerobic conditions. Many genes encoding proteinsinvolved in glycolysis, carbon source uptake systems,pyruvate metabolism, fermentation and the electron respirationtransport chain were up-regulated. These changes ledto an increased amount of pyruvate, lactate, ethanol and acetatein the bacterial cells as confirmed by metabolite detection. Genes encoding proteins involved in cell surface structures,especially biofilm formation, peptidoglycan biosynthesisand lipopolysaccharide biosynthesis were up-regulatedas well. Biofilm formation was significantly enhancedunder anaerobic conditions. These results indicate that inductionof central metabolism is important for basic survivalof A. pleuropneumoniae after a shift to an anaerobic environment. Enhanced biofilm formation may contribute tothe persistence of this pathogen in the damaged anaerobichost tissue and also in the early colonization stage. Thesediscoveries give new insights into adaptation mechanismsof A. pleuropneumoniae in response to environmental stress.
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Xiaoluo Huang,Fei Huang,Hui Wang,Zongze Shao,Yuzhi Hong,Ling Lin,Chanjuan Li,Ziduo Liu 한국미생물학회 2010 The journal of microbiology Vol.48 No.3
A recombinant Escherichia coli clone expressing an endoglucanase was identified from a genomic library of the halophilic bacterium Halomonas sp. S66-4, and the enzyme was designated Cel8H. The cel8H gene consisted of 1,053 bp and encoded 350 amino acids sharing the highest identity of 48% to other known endoglucanases. The protein was expressed in E. coli BL21 (DE3) and purified to homogeneity. The purified recombinant enzyme had an optimal activity of 4.9 U/mg at pH 5 and 45°C toward the substrate carboxymethylcellulose. It exhibited extraordinary properties which differed from endoglucanases reported previously at the point of high salt tolerance above 5 M, simultaneously with high pH stability at pH 4-12 and high temperature stability at 40-60°C. Various substrate tests indicated that the enzyme hydrolyzes β-1,4-glucosidic bonds specifically.
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