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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.