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An Alkaline Amylopullulanase from Alkalophilic Bacillus sp. KSM-1378; Kinetic Evidence for Two Independent Active Sites for the α-1,4 and α-1,6 Hydrolytic Reactions
- K. Ara, K. Igarashi, K. Saeki, S. Ito
- Chemistry
- 23 April 1995
TLDR
The Crystal Structure of an Oxidatively Stable Subtilisin-like Alkaline Serine Protease, KP-43, with a C-terminal β-Barrel Domain*
- T. Nonaka, M. Fujihashi, K. Miki
- ChemistryJournal of Biological Chemistry
- 5 November 2004
TLDR
Purification and Some Properties of an Alkaline Pullulanase from Alkalophilic Bacillus sp.KSM-1876
- K. Ara, K. Igarashi, K. Saeki, S. Kawai, S. Ito
- Biology
- 23 January 1992
A novel alkaline pullulanase (pullulan 6-glucanohydrolase, EC 3.2.1.41) was purified to homogeneity from the culture filtrate of the alkalophilic Bacillus sp. KSM-1876. The pullulanase had an optimum…
Purification and characterization of an alkaline isoamylase from an alkalophilic strain of Bacillus
Summary: Alkaline isoamylase (glycogen 6-glucanohydrolase, EC 3.2.1.68) activity was detected in the culture medium of an alkalophilic strain of Bacillus sp., designated KSM-3309, which was isolated…
Nucleotide and deduced amino acid sequences of mutanase-like genes from Paenibacillus isolates: proposal of a new family of glycoside hydrolases.
- Y. Hakamada, Nobuyuki Sumitomo, Tohru Kobayashi
- BiologyBiochimie
- 1 March 2008
Detergent alkaline proteases: enzymatic properties, genes, and crystal structures.
- K. Saeki, K. Ozaki, Tohru Kobayashi, S. Ito
- BiologyJournal of bioscience and bioengineering
- 1 June 2007
TLDR
Enzymatic Properties of a Novel Liquefying α-Amylase from an Alkaliphilic Bacillus Isolate and Entire Nucleotide and Amino Acid Sequences
- K. Igarashi, Y. Hatada, S. Ito
- BiologyApplied and Environmental Microbiology
- 1 September 1998
TLDR
A novel species of alkaliphilic Bacillus that produces an oxidatively stable alkaline serine protease
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