Results 151 to 160 of about 482 (171)
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Identification and Cloning of a Second Phytase Gene (phyB) from Aspergillus niger (ficuum)
Biochemical and Biophysical Research Communications, 1993An Aspergillus niger (ficuum) genomic DNA lambda EMBL3 library was probed with a 354-bp DNA fragment obtained by polymerase chain reaction of A. niger DNA with oligonucleotides based on partial amino acid sequence of a pH 2.5 optimum acid phosphatase. A clone containing a 1605 bp segment (phyB) encoding the 479 amino acid enzyme was isolated and found ...
K C, Ehrlich +4 more
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Carbohydrate Polymers, 2013
An exoinulinase gene from Aspergillus ficuum JNSP5-06 was overexpressed in Escherichia coli. Two exons of the exoinulinase gene were amplified separately, joined together by an overlap PCR, and expressed in E. coli. The molecular weight of the recombinant exoinulinase was estimated to be 63 kDa.
Xiao-Ming, Chen +3 more
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An exoinulinase gene from Aspergillus ficuum JNSP5-06 was overexpressed in Escherichia coli. Two exons of the exoinulinase gene were amplified separately, joined together by an overlap PCR, and expressed in E. coli. The molecular weight of the recombinant exoinulinase was estimated to be 63 kDa.
Xiao-Ming, Chen +3 more
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Biophysics, 2018
Computer models for the dimers of inulinases from Aspergillus awamori, Aspergillus ficuum and Kluyveromyces marxianus have been developed. The inulinases dimerization mechanisms from various producers and the amino acid composition of binding sites between the monomers in dimer structure have been studied.
M. G. Holyavka +5 more
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Computer models for the dimers of inulinases from Aspergillus awamori, Aspergillus ficuum and Kluyveromyces marxianus have been developed. The inulinases dimerization mechanisms from various producers and the amino acid composition of binding sites between the monomers in dimer structure have been studied.
M. G. Holyavka +5 more
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Enzymatic—spectrophotometric determination of phytic acid with phytase from Aspergillus ficuum
Analytica Chimica Acta, 1995Abstract A method to determine phytic acid in the range 3–60 μM based on the spectrophotometric determination of inorganic phosphate with vanadate and molybdate, after liberation by enzymatic hydrolysis of phytic acid with phytase from Aspergillus ficuum at pH 2.5 and 37 °C is reported.
J.G. March, A.I. Villacampa, F. Grases
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Crystal structure of phytase from Aspergillus ficuum at 2.5 Å resolution
Nature Structural Biology, 1997Phytase is a high molecular weight acid phosphatase. The structure has an alpha/beta-domain similar to that of rat acid phosphatase and an alpha-domain with a new fold.
Dirk Kostrewa +5 more
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The Aspergillus niger (ficuum) aphA gene encodes a pH 6.0-optimum acid phosphatase
Gene, 1995We have used the Aspergillus niger (An) aphA gene as a probe and cloned the A. ficuum (Af) SRRC 265 gene encoding an extracellular pH 6.0-optimum acid phosphatase (APase6) from a genomic library. The identity of the Af aphA gene was confirmed and its nucleotide (nt) sequence verified by comparing its deduced amino acid (aa) sequence to that of purified
E J, Mullaney +3 more
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Journal of Photochemistry and Photobiology B: Biology, 2012
Aspergillus ficuum grown on plates and in liquid cultures were illuminated by a white fluorescent light and four different colour LED lights (white, blue, green and red) to evaluate the regulation of LED lights on fungal growth. Biomass conversion, pellet size and phytase activity were examined.
Chien-Wei, Cheng +3 more
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Aspergillus ficuum grown on plates and in liquid cultures were illuminated by a white fluorescent light and four different colour LED lights (white, blue, green and red) to evaluate the regulation of LED lights on fungal growth. Biomass conversion, pellet size and phytase activity were examined.
Chien-Wei, Cheng +3 more
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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, 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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