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.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2001
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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.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
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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.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
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