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Purification and characterization of the recombinant Thermus sp. strain T2 alpha-galactosidase expressed in Escherichia coli

Article Abstract:

The properties of alpha-galactosidase from the thermophilic bacterium Thermus sp. strain T2 are described. The enzyme is an octamer and is 70% homologous to the alpha-galactosidase from Thermus brockianus.

Author: Ishiguro, Mitsunori, Kaneko, Satoshi, Kuno, Atsushi, Koyama, Yoshinori, Yoshida, Shigeki, Park, Gwi-Gun, Sakakibara, Yoshikiyo, Kusakabe, Isao, Kobayashi, Hideyuki
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2001
Bacteria, Thermophilic, Microbial enzymes, Thermophiles

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Purification and substrate specificities of two alpha-L-arabinofuranosidases from Aspergillus awamori IFO 4033

Article Abstract:

A study was conducted to analyze the purification and substrate characteristics of two alpha-L-arabinofuranosidases determined from the culture filtrate of Aspergillus awamori IFO 4033. The influence of pH on the activity and stability of alpha-L-AFases were obtained in a series of McIlvaine buffers. A culture filtrate was then dialyzed against deionized water. In addition, sodium dodecyl sulfate-polyacrylamide gel electrophoresis was carried out in a polyacrylamide gel.

Author: Kaneko, Satoshi, Kusakabe, Isao, Kobayashi, Hideyuki, Ishii, Tadashi, Arimoto, Mitsue, Ohba, Misako
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
Aspergillus, Hydrogen-ion concentration

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Cloning and high-level expression of alpha-galactosidase cDNA from Penicillium purpurogenum

Article Abstract:

Research was conducted to examine the cloning of Penicillium purpurogenum alpha-Gal cDNA, its expression in Saccharomyces cerevisiae and the purification and characterization of the recombinant enzyme. The mature enzyme consisted of 419 amino acid residues with a molecular mass of 46,334 Da as shown by the deduced amino acid sequence of the alpha-GAl cDNA. The purified recombinant enzyme showed slightly higher specific activity and properties that were almost identical to those of the native enzymes from P. purpurogenum.

Author: Kaneko, Satoshi, Yoshida, Shigeki, Kusakabe, Isao, Kobayashi, Hideyuki, Shibuya, Hajime, Nagasaki, Hiroaki, Park, Gwi Gun
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
Genetic aspects, Cloning, Gene expression, Circular DNA, Saccharomyces cerevisiae

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Subjects list: Research
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