๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Structure of a new alkaline serine protease (M-protease) from Bacillus sp. KSM-K16

โœ Scribed by Yamane, T. ;Kani, T. ;Hatanaka, T. ;Suzuki, A. ;Ashida, T. ;Kobayashi, T. ;Ito, S. ;Yamashita, O.

Book ID
114529143
Publisher
International Union of Crystallography
Year
1995
Tongue
English
Weight
770 KB
Volume
51
Category
Article
ISSN
0907-4449

No coin nor oath required. For personal study only.

๐Ÿ“œ SIMILAR VOLUMES

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

Cation-induced thermal stability of an a
Cation-induced thermal stability of an alkaline protease from a Bacillus sp.
โœ Nisha Paliwal; S.P. Singh; S.K. Garg ๐Ÿ“‚ Article ๐Ÿ“… 1994 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 279 KB

An alkafine protease produced from a Bacillus sp. was stimulated by the metal ions Ca 2รท, Mg 2+ and Mn2+; with Ca 2+ having the maximum effect. The thermal stability of the enzyme was also enhanced to varying degrees in the presence of these ions.