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Purification and characterization of a novel thermostable alpha-L-Arabinofuranosidase from a color-variant strain of Aureobasidium pullulans

Article Abstract:

Research was performed to analyze the purification and characterization of alpha-L-Arabinofuranosidase from a color-variant strain of the yeast-like fungus Aureobasidium pullulans. Results revealed that a color-variant strain of A. pullulans produced an extracellular highly thermostable alpha-L-Arabinofuranosidase, which was able to hyrolyze both 1->3 and 1->5 linkages in arabinan, when grown in liquid culture on oat spelt xylan. Evidence also suggested that the enzyme did not necessitate metal ion for activity and was not affected by p-chloromercuribenzoate and dithiothreitol.

Author: Saha, Badal C., Bothast, Rodney J.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
Enzymes, Fungi, Reproduction (Biology), Hydrolysis, Enzyme structure-activity relationships

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Production of galacto-oligosaccharide from lactose by Sterigmatomyces elviae CBS8119

Article Abstract:

The yeast Sterigmatomyces elviae CBS8119 is the most efficient strain for the production of galacto-oligosaccharide (Gal-OS) form lactose, out of the 574 bacteria and yeast strains analyzed in stock culture. The transgalactosylation activity in the yeast is of high level. The Gal-OS productivity of toluene-treated cells of the yeast is low. Transgalactosylation is inhibited by its by-product glucose, bringing down Gal-OS yield. This inhibition can be removed if the enzyme activity follows growth.

Author: Yokozeki, Kenzo, Onishi, Norimasa, Yamashiro, Akihiro
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1995
Oligosaccharides, Microbiology, Cultures (Biology)

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Purification and properties of a novel thermostable galacto-oligosaccharide-producing beta-galactosidase from Sterigmatomyces elviae CBS8119

Article Abstract:

The enzyme beta-galactosidase is purified from the yeast Sterigmatomyces elviae by chromatography on DEAE-Toyopearl, Butyl-Toyopearl, Chromatofocusing, and p-aminobenzyl 1-thio-beta-D-galactopyranoside agarose columns. The enzyme shows an isoelectric point 4.1, an optimal temperature of 85 degrees celsius, and optimal pH range of 4.5-5.0. It has maximum velocities of 96 micro mole per minute per milligram of protein for o-nitrophenyl-beta-D-galactopyranoside, and 240 for lactose.

Author: Tanaka, Takashi, Onishi, Norimasa
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1995
Proteins, Enzyme kinetics, Chromatography, Protein separation

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Subjects list: Research, Usage, Microbial enzymes, Yeast, Yeast (Food product)
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