Results 161 to 170 of about 1,150 (171)
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Preparative Biochemistry, 1988
Purified Aspergillus ficuum phytase's partial primary structure and amino acid and sugar composition were elucidated. Determination of kinetic parameters of the enzyme at different pH values and temperatures indicated no significant alteration of the Km for phytate while the Kcat was affected.
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Purified Aspergillus ficuum phytase's partial primary structure and amino acid and sugar composition were elucidated. Determination of kinetic parameters of the enzyme at different pH values and temperatures indicated no significant alteration of the Km for phytate while the Kcat was affected.
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1993
ABSTRACT Nine β -fructosidases were purified from a commercial inulinase preparation of the thermotolerant fungus Aspergillus ficuum. All enzymes were active towards inulin and sucrose, with an I/S ratio lower than 1 (except two enzymes). They were all glycoproteins with a high sugar content.
J. BARATTI, M. ETTALIBI
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ABSTRACT Nine β -fructosidases were purified from a commercial inulinase preparation of the thermotolerant fungus Aspergillus ficuum. All enzymes were active towards inulin and sucrose, with an I/S ratio lower than 1 (except two enzymes). They were all glycoproteins with a high sugar content.
J. BARATTI, M. ETTALIBI
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Preparative Biochemistry, 1987
Extracellular phytase from Aspergillus ficuum, a glycoprotein, was purified to homogeneity in 3 column chromatographic steps using ion exchange and chromatofocusing. Results of gel filtration chromatography and SDS-polyacrylamide gel electrophoresis indicated the approximate molecular weight of the native protein to be 85-100-KDa.
A H, Ullah, D M, Gibson
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Extracellular phytase from Aspergillus ficuum, a glycoprotein, was purified to homogeneity in 3 column chromatographic steps using ion exchange and chromatofocusing. Results of gel filtration chromatography and SDS-polyacrylamide gel electrophoresis indicated the approximate molecular weight of the native protein to be 85-100-KDa.
A H, Ullah, D M, Gibson
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Applied Microbiology and Biotechnology, 1987
One invertase (Inv), five exoinulinases (Exo I; II; III; IV; V) and three endoinulinases (Endo I; II; III) were isolated from a commercial inulinase preparation derived from Aspergillus ficuum using ammonium sulfate precipitation, ion exchange chromatography on DEAE-Sephacel and DEAE-Trisacryl, gel filtration on Ultrogel and Fast Protein Liquid ...
Moussa Ettalibi, Jacques C. Baratti
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One invertase (Inv), five exoinulinases (Exo I; II; III; IV; V) and three endoinulinases (Endo I; II; III) were isolated from a commercial inulinase preparation derived from Aspergillus ficuum using ammonium sulfate precipitation, ion exchange chromatography on DEAE-Sephacel and DEAE-Trisacryl, gel filtration on Ultrogel and Fast Protein Liquid ...
Moussa Ettalibi, Jacques C. Baratti
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Biochemical and Biophysical Research Communications, 1993
Primary structure elucidation of peptides generated by cyanogen bromide, endoproteinase Glu-C, and clostripain cleavage of an Aspergillus ficuum extracellular pH optimum 2.5 acid phosphatase identified a region which contains the active site of the enzyme.
A H, Ullah, H C, Dischinger
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Primary structure elucidation of peptides generated by cyanogen bromide, endoproteinase Glu-C, and clostripain cleavage of an Aspergillus ficuum extracellular pH optimum 2.5 acid phosphatase identified a region which contains the active site of the enzyme.
A H, Ullah, H C, Dischinger
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Preparative Biochemistry, 1988
A rapid purification scheme utilizing three chromatographic steps resulted in 6 fold purification of Aspergillus ficuum phytase (myo-inositol-hexakisphosphate 3-phosphohydrolase, EC 3.1.3.8). At pH 5.0 and 60 degrees C the enzyme performed acceptably for 2.0 hr with only 30% diminished catalytic rate at the end.
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A rapid purification scheme utilizing three chromatographic steps resulted in 6 fold purification of Aspergillus ficuum phytase (myo-inositol-hexakisphosphate 3-phosphohydrolase, EC 3.1.3.8). At pH 5.0 and 60 degrees C the enzyme performed acceptably for 2.0 hr with only 30% diminished catalytic rate at the end.
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Aspergillus ficuum Extracellular Phytase
Annals of the New York Academy of Sciences, 1990A H, Ullah, H C, Dischinger
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Identification of Residues Involved in Active‐Site Formation in Aspergillus ficuum Phytase
Annals of the New York Academy of Sciences, 1992A H, Ullah, H C, Dischinger
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Aspergillus ficuum Phytase Active Site: Involvement of Arg and Trp Residues
Annals of the New York Academy of Sciences, 1995A H, Ullah, H C, Dischinger
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