Results 151 to 160 of about 1,150 (171)

PhyA gene product of Aspergillus ficuum and Peniophora lycii produces dissimilar phytases

Biochemical and Biophysical Research Communications, 2003
PhyA gene products of Aspergillus ficuum (AF) and Peniophora lycii (PL) as expressed in industrial strains of Aspergillus niger and Aspergillus oryzae, respectively, were purified to homogeneity and then characterized for both physical and biochemical properties. The PL phytase is 26 amino acid residues shorter than the AF phytase.
Abul H J, Ullah, Kandan, Sethumadhavan
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Malformins from Aspergillus ficuum, A. awam ori and A. phoenicis

Phytochemistry, 1969
Abstract Malformins were isolated from culture filtrates of Aspergillus ficuum, A. awamori and A. phoenicis . They were characterized as malformin A (a mixture of malformins A 1 and A 2 ) on the basis of biological activity, chromatographic behavior, i.r. and mass spectrum, optical rotation and amino acid analysis.
Shinobu Iriuchijima, Roy W. Curtis
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Cloning and Nucleotide Sequence of the Endoinulinase-Encoding Gene, inu2, from Aspergillus ficuum

Biotechnology Letters, 1998
A 2.3 kb DNA fragment that contains a gene encoding endoinulinase, inu2, from Aspergillus ficuum ATCC 16882 was isolated and analyzed. It includes an open reading frame of 1,551 bp, coding for a polypeptide with calculated molecular weight of 55,790 Da, including a putative signal peptide of 22 amino acids. Alignment of amino acid sequences revealed 73.
Uhm, T. B., Chae, K.-S., Lee, D. W., Kim, H.-S., Cassart, Jean-Pol, Vandenhaute, Jean   +5 more
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Supramolecular Organization of Inulinases from Aspergillus awamori, Aspergillus ficuum and Kluyveromyces marxianus: A Comparative Aspect

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, S. M. Makin, M. S. Kondratyev, A. V. Abdullatypov, T. A. Kovaleva, V. G. Artyukhov   +5 more
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Aspergillus ficuum Extracellular Phytase Immobilization on Glutaraldehyde‐activated Silicate

Annals of the New York Academy of Sciences, 1988
Technique d'immobilisation de l'enzyme 3-phytase de Aspergillus ficuum, et construction d'un bioreacteur a lit de garnissage.
ABUL H. J. ULLAH, BARRY J. CUMMINS
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Identification and Cloning of a Second Phytase Gene (phyB) from Aspergillus niger (ficuum)

Biochemical and Biophysical Research Communications, 1993
An 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, B G, Montalbano, E J, Mullaney, H C, Dischinger, A H, Ullah   +4 more
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Crystal structure of phytase from Aspergillus ficuum at 2.5 Å resolution

Nature Structural Biology, 1997
Phytase 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, Fiona Grüninger-Leitch, Allan D′Arcy, Clemens Broger, David Mitchell, Adolphus P. G. M. van Loon   +5 more
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Enzymatic—spectrophotometric determination of phytic acid with phytase from Aspergillus ficuum

Analytica Chimica Acta, 1995
Abstract 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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The Aspergillus niger (ficuum) aphA gene encodes a pH 6.0-optimum acid phosphatase

Gene, 1995
We 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, C B, Daly, K C, Ehrlich, A H, Ullah   +3 more
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Decolorization of Direct Black 22 by Aspergillus ficuum.

Journal of environmental sciences (China), 2002
The decolorization of Direct Black 22 by Aspergillus ficuum has been studied. It was found that Aspergillus ficuum could effectively decolorize Direct Black 22 especially when grown as pelleted mycelia. Results showed that the media containing Direct Black 22 at 50 mg/L could be decolorized by 98.05% of the initial color in 24 h.
X J, Dong, Z Y, Du, Z, Chen
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