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A cold-adapted lipase of an Alaskan psychrotroph, Pseudomonas sp. strain B11-1: gene cloning and enzyme purification and characterization

Article Abstract:

The cloning and sequencing of the lipase gene (lipP) from a Pseudomonas strain and the purification and characterization of the recombinant enzyme LipP were studied and reported. The amino acid sequence from the nucleotide sequence of the gene corresponded to a protein of 308 amino acid residues with a molecular weight of 33,714. The LipP enzyme was found to be stable between pH 6 and 9 while ts was unstable with temperatures higher than 45 degrees C. Various organic solvents such as dimethyl sulfoxide and methanol at concentrations of 0 to 30% activated the enzyme.

Author: Soda, Kenji, Kurihara, Tatsuo, Esaki, Nobuyoshi, Choo, Dong-Won, Suzuki, Takeshi
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
Enzymes, Pseudomonas, Cloning, Lipase

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Cold-active serine alkaline protease from the psychrotrophic bacterium Shewanella strain Ac10: gene cloning and enzyme purification and characterization

Article Abstract:

Research was conducted to examine the characteristics of a cold-active recombinant subtilisinlike protease from the psychrotrophic bacterium Shewanella strain Ac10. The amino acid sequence deduced from the 2,442-bp nucleotide sequence showed that the protein was 814 amino acids long with an estimated molecular weight of 85,113. Purification was performed from the culture supernatant of Escherichia coli recombinant cells using affinity chromatography with a bacitracin-Sepharose column.

Author: Kurihara, Tatsuo, Esaki, Nobuyoshi, Galkin, Andrey, Kulakova, Ljudmila, Yoshimura, Tohru
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1999
Proteases, Microorganisms, Serine, Temperature effects, Psychrotrophic organisms, Psychrotrophic microorganisms

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Construction of a low-temperature protein expression system using a cold-adapted bacterium, Shewanella sp. strain Ac10, as the host

Article Abstract:

A low-temperature protein expression system was constructed using an Antarctic cold-adapted bacterium Shewanella sp. strain Ac10, as the host. The maximum yield of proteins was obtained when the promoter for putative alkyl hydroperoxide reductase (ahpC) was used and the recombinant cells were grown to late stationary phase.

Author: Kato, Ikunoshin, Miyake, Ryoma, Kawamoto, Jun, Kitagawa, Masanari, Yun-Lin Wei, Kurihara, Tatsuo, Esaki, Nobuyoshi
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2007
Science & research, Physiological aspects, Gene expression, Shewanella

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Subjects list: Research, Genetic aspects, Amino acid sequence, Amino acid sequencing
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