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- 저자 : JunPei Zhou (검색결과 2 건)
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Phylogenetic Diversity of Bacteria in an Earth-Cave in Guizhou Province, Southwest of China
JunPei Zhou,YingQi Gu,ChangSong Zou,MingHe Mo 한국미생물학회 2007 The journal of microbiology Vol.45 No.2
The objective of this study was to analyze the phylogenetic composition of bacterial community in the soil of an earth-cave (Niu Cave) using a culture-independent molecular approach. 16S rRNA genes were amplified directly from soil DNA with universally conserved and Bacteria-specific rRNA gene primers and cloned. The clone library was screened by restriction fragment length polymorphism (RFLP), and representative rRNA gene sequences were determined. A total of 115 bacterial sequence types were found in 190 analyzed clones. Phylogenetic sequence analyses revealed novel 16S rRNA gene sequence types and a high diversity of putative bacterial community. Members of these bacteria included Proteobacteria (42.6%), Acidobacteria (18.6%), Planctomycetes (9.0%), Chloroflexi (Green nonsulfur bacteria, 7.5%), Bacteroidetes (2.1%), Gemmatimonadetes (2.7%), Nitrospirae (8.0%), Actinobacteria (High G+C Gram-positive bacteria, 6.4%) and candidate divisions (including the OP3, GN08, and SBR1093, 3.2%). Thirty-five clones were affiliated with bacteria that were related to nitrogen, sulfur, iron or manganese cycles. The comparison of the present data with the data obtained previously from caves based on 16S rRNA gene analysis revealed similarities in the bacterial community components, especially in the high abundance of Proteobacteria and Acidobacteria. Furthermore, this study provided the novel evidence for presence of Gemmatimonadetes, Nitrosomonadales, Oceanospirillales, and Rubrobacterales in a karstic hypogean environment.
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JunPei Zhou,Yanyan Dong,Yajie Gao,Xianghua Tang,Junjun Li,YUN-JUAN YANG,Bo Xu,Zhenrong Xie,Zunxi Huang 한국생물공학회 2012 Biotechnology and Bioprocess Engineering Vol.17 No.4
The 774-bp pectate lyase gene plyAI4 from Bacillus sp. I4 was cloned and expressed in E. coli. The gene encodes a 257-residue polypeptide (PlyAI4, 28.3 kDa)with the highest identities of 97.3% with a putative pectate lyase from Bacillus subtilis BSn5 (ADV94306) and 60.3%with an identified pectate lyase of the polysaccharide lyase family (PL) 3 from Paenibacillus amylolyticus 27C64(ADB78774). The purified recombinant PlyAI4 (rPlyAI4)exhibited apparently optimal activity at pH 10.5 ~ 11.0 and 50oC. Compared with the majority of reported alkaline pectate lyases, rPlyAI4 exhibited more residual enzyme activity at 20oC (~45%) or at 70oC (~50%) and better thermostability at 70oC (~60 min half-life at 70oC). In the presence of 20% (v/v) ethanol, pectate lyase activity was enhanced by 0.2 fold. After incubation in 40% (v/v)ethanol at 37oC and pH 8.5 for 1 h, the purified rPelAI4retained more than 75% of the initial activity. Sequence analysis proposed a new signature block, A-D-G-[V/I]-H,for PL 3 pectate lyases. These properties may prove to be important with regards to PlyAI4 for basic research and industrial application.
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