国际标准期刊号: 2155-952X

生物技术与生物材料

开放获取

我们集团组织了 3000 多个全球系列会议 每年在美国、欧洲和美国举办的活动亚洲得到 1000 多个科学协会的支持 并出版了 700+ 开放获取期刊包含超过50000名知名人士、知名科学家担任编委会成员。

开放获取期刊获得更多读者和引用
700 种期刊 15,000,000 名读者 每份期刊 获得 25,000 多名读者

索引于
  • 哥白尼索引
  • 谷歌学术
  • 夏尔巴·罗密欧
  • 打开 J 门
  • Genamics 期刊搜索
  • 学术钥匙
  • 研究圣经
  • 中国知网(CNKI)
  • 访问全球在线农业研究 (AGORA)
  • 电子期刊图书馆
  • 参考搜索
  • 哈姆达大学
  • 亚利桑那州EBSCO
  • OCLC-世界猫
  • SWB 在线目录
  • 虚拟生物学图书馆 (vifabio)
  • 普布隆斯
  • 日内瓦医学教育与研究基金会
  • 欧洲酒吧
  • ICMJE
分享此页面

抽象的

Properties of Alkaline Protease C45 Produced by Alkaliphilic Bacillus Sp. Isolated from Chitu, Ethiopian Soda Lake

Gizachew Haile and Amare Gessesse

A total of 240 alkaliphilic bacteria were isolated from samples collected from alkaline soda lakes of Ethiopia and were screened for the production of alkaline proteases. Of these, 30% were protease positive indicating the abundance of protease producing microorganisms in these habitats. The Bacillus sp. designated as C45 that grow in solid state medium was selected based on the property of the enzyme for further study. The protease produced by the Bacillus sp. was active in the pH range of 6.5-11.5, with optimum activity at pH 8-9; and stable at alkaline pH. The optimum temperature for activity was 40°C and 50°C in absence and presence of 5 mM of Ca+2, respectively. The enzyme displayed appreciable activity and stability at low temperature. These properties suggest that protease C45 could find potential application for dehairing and detergent at moderate temperature. When protease C45 was added to raw hide it enabled dehairing, suggesting the potential usefulness of the enzyme in the leather industry.

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。