索引于
  • 学术期刊数据库
  • Genamics 期刊搜索
  • 学术钥匙
  • 期刊目录
  • 中国知网(CNKI)
  • 西马戈
  • 访问全球在线农业研究 (AGORA)
  • 电子期刊图书馆
  • 参考搜索
  • 研究期刊索引目录 (DRJI)
  • 哈姆达大学
  • 亚利桑那州EBSCO
  • OCLC-WorldCat
  • SWB 在线目录
  • 虚拟生物学图书馆 (vifabio)
  • 普布隆斯
  • 米亚尔
  • 大学教育资助委员会
  • 日内瓦医学教育与研究基金会
  • 欧洲酒吧
  • 谷歌学术
分享此页面
期刊传单
Flyer image

抽象的

Purification, Amino Acid sequencing and Thermostability of an Extracellular Low Molecular Weight Esterase Produced by Bacillus Subtilis NRRL 41270 in Fermentation

Papagianni M and Papamichael EM

Extracellular esterase activity in Bacillus subtilis NRRL 41270 fermentation broths was found to reside in a small protein with a molecular weight less than 10 kDa. Following purification, esterase activity on fluorescein dibutyrate was estimated at 12 U/min/mg proteins. Enzyme saturation was observed at 5 μM substrate concentration. The produced esterase hydrolysed tributyrin. Its specific activity was estimated to be 17.8 μmol acid released/min/mg proteins. The small protein was subjected to size exclusion chromatography, SDS-PAGE and amino acid sequencing. Analysis revealed a sequence of the following amino acid residues: eevaetysfyhitphdystshispapvqffspap, according to which the molecule has 34 amino acid residues and a calculated molecular mass of 3853, which was in accordance with the gel filtration and SDS-PAGE results. Sequence based analysis and use of bioinformatics tools showed no significant similarity with known proteins while revealed a strongly hydrophobic molecule, with a α-helical conformation in the N-terminal, the rest of the molecule being β-sheet-rich. The enzyme appeared to be thermostable with more than 85% of the original activity maintained after 120 h incubation at 60°C. The producer organism and the features of the micro enzyme, suggest the case of a biotechnologically interesting biocatalyst that should be further researched in terms of its stability and production characteristics.

免责声明: 此摘要通过人工智能工具翻译,尚未经过审核或验证