๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

An alkaline proteinase of an alkalophilicBacillussp.

โœ Scribed by Osamu Tsuchida; Yohei Yamagata; Takehiko Ishizuka; Teruyoshi Arai; Jun-Ichi Yamada; Michio Takeuchi; Eiji Ichishima

Book ID
105243324
Publisher
Springer
Year
1986
Tongue
English
Weight
755 KB
Volume
14
Category
Article
ISSN
0343-8651

No coin nor oath required. For personal study only.

๐Ÿ“œ SIMILAR VOLUMES

Partial purification and some properties
Partial purification and some properties of an alkaline cellulase from an alkalophilicBacillussp.
โœ H. Khyami-Horani ๐Ÿ“‚ Article ๐Ÿ“… 1996 ๐Ÿ› Springer ๐ŸŒ English โš– 532 KB

A newly isolated Bacillus species, which grew optimally at 30ยฐC and pH 10, produced a carboxymethylcellulase in a medium containing 10 g CM-cellulose/l. The enzyme, when partially purified by gel filtration, had a mass of about 29 kDa as determined by both SDS-PAGE and gel filtration chromatography.

A new alkaline serine protease from alka
A new alkaline serine protease from alkalophilicBacillussp.: Cloning, sequencing, and characterization of an intracellular protease
โœ Youhei Yamagata; Eiji Ichishima ๐Ÿ“‚ Article ๐Ÿ“… 1995 ๐Ÿ› Springer ๐ŸŒ English โš– 848 KB

To obtain a new serine protease from alkalophilic Bacillus sp. NKS-21, shotgun cloning was carried out. As a result, a new protease gene was obtained. It encoded an intracellular serine protease (ISP-1) in which there was no signal sequence. The molecular weight was 34,624. The protease showed about