Enzymatic properties of a novel liquefying alpha-amylase from an alkaliphilic Bacillus isolate and entire nucleotide and amino acid sequences
Article Abstract:
Research was conducted to examine the isolation of a novel liquefying alpha-amylase (LAMY) from cultures of the alkaline amylopullulanase producer Bacillus sp. strain KSM-1378. The enzyme performed efficient hydrolysis on several carbohydrates to afford maltotriose, maltohexaose, maltopentaose and maltose as primary end products. Results provide evidence that the sequence of LAMY was consistent with the tertiary structures of amylolytic enzymes. An analysis of the gene for the alpha-amylase indicates that LAMY displays low amino acid identity to the reported liquefying alpha-amylases.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
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Novel allylic oxidation of a alpha-cedrene to sec-cedrenol by a Rhodococcus strain
Article Abstract:
The allylic oxidation of alpha-cedrene by a Rhodococcus strain was described. The strain, designated KSM-7358, could hydroxylate alpha-cedrene to sec-cedrenol regiospecifically with a very high yield. The optimization of the oxidation reaction by resting cells was also examined. A possible pathway for the formation of sec-cedrenol and alpha-curcumene from alpha-cedrene by the organism was proposed.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1993
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Novel alpha-amylase that is highly resistant to chelating reagents and chemical oxidants from the alkaliphilic Bacillus isolate KSM-K38
Article Abstract:
Researchers have discovered a bacterial alpha-amylase that could be used in detergents. It is resistant to chelating agents and chemical oxidants and has an optimal pH of 8 to 9.5. Most detergents range between a pH of 8 and 11.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2001
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