Molecular cloning, purification, and characterization of a novel, acidic, pH-stable endoglucanase from Martelella mediterranea
Molecular cloning, purification, and characterization of a novel, acidic, pH-stable endoglucanase from Martelella mediterranea
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来自地中海 Martelella 的新型酸性、pH 稳定内切葡聚糖酶的分子克隆、纯化和表征
DOI：
10.1007/s12275-010-9361-0
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发表时间：
2010-06-01
影响因子：
3
通讯作者：
Liu, Ziduo
中科院分区：
文献类型：
--
作者：
Dong, Junli;Hong, Yuzhi;Liu, Ziduo
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 degrees 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.
