Biochemical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolases): catalytic properties
Article Abstract:
Research was conducted to examine the biochemical characterization of wild-type phytases which include fungal phytases and the Escherichia coli phytase. The fungal phytases were derived from Aspergillus terreus, Aspergllus fumigatus, Myceliophthora thermophila, Emericella nidulans and Escherichia coli. Results based on time course experiments indicate that phytases with broad substrate specificity are appropriate for animal nutrition purposes than phytases with narrow substrate specificity.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1999
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Biophysical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolases): molecular size, glycosylation pattern, and engineering of proteolytic resistance
Article Abstract:
Research was conducted to examine the biophysical characterization of fungal phytases. Phytases from six different fungi, namely, Aspergillus terreus, Aspergillus niger, Emericella nidulans, Aspergillus fumigatus, Talaromyces thermophilus and Myceliophthora were purified and compared with a prokaryotic phytase from Escherichia coli. Results indicate that all of the fungal phytases including the E. coli phytase are monomeric proteins.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1999
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Expression, gene cloning, and characterization of five novel phytases from four basidiomycete fungi: Peniophora lycii, Agrocybe pediades, a Ceriporia sp., and Trametes pubescens
Article Abstract:
Researchers show that the phytases from four different fungi all hydrolyze phytate by initially attacking the 6-phosphate group of phytic acid. For this reason, the fungal phytases should be characterized as 6-phytases.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2001
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