Results 111 to 120 of about 338 (140)

Purification, properties and comparison of invertase, exoinulinases and endoinulinases of Aspergillus ficuum

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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Production and Partial Purification of Tannase fromAspergillus ficuumGim 3.6

Preparative Biochemistry and Biotechnology, 2014
A novel fungal strain, Aspergillus ficuum Gim 3.6, was evaluated for its tannase-producing capability in a wheat bran-based solid-state fermentation. Thin-layer chromatography (TLC) analysis revealed that the strain was able to degrade tannic acid to gallic acid and pyrogallol during the fermentation process.
Wan-liang, Ma, Fen-fen, Zhao, Qin, Ye, Zhen-xing, Hu, Dong, Yan, Jie, Hou, Yang, Yang   +6 more
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Immobilization ofAspergillus ficuumInulinases on Porous Glass

Biocatalysis, 1992
The thermostable inulinases from the fungus Aspergillus ficuum were immobilized by covalent binding on porous glass beads of different porosities (pore diameter 125 to 1170 A). The highest retention of activity (60%) and highest activity per g of support (300 IU/g) were obtained with the support with an average pore diameter of 120 A.
Moussa Ettalibi, Jacques C. Baratti
openaire   +1 more source

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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Expression of an exoinulinase gene from Aspergillus ficuum in Escherichia coli and its characterization

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, Xue-Ming, Xu, Zheng-Yu, Jin, Han-Qing, Chen   +3 more
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An Acid Phosphatase from Aspergillus ficuum Has Homology to Penicillium chrysogenum PhoA

Biochemical and Biophysical Research Communications, 1994
Three secreted acid phosphatases had previously been characterized from Aspergillus ficuum grown under conditions of limited phosphate. One of these could not be readily separated from AFPhyB, a pH 2.5 optimum acid phosphatase with phytase activity.
K C, Ehrlich, B G, Montalbano, E J, Mullaney, H C, Dischinger, A H, Ullah   +4 more
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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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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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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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Hydrolysis of inulin: A kinetic study of the reaction catalyzed by an inulinase from Aspergillus ficuum

Biotechnology and Bioengineering, 1991
AbstractA kinetic study of the hydrolysis of inulin was performed by using as catalyst a commercial inulinase from Aspergillus ficuum. The reaction was studied carrying out initial rate as well as time course measurements. Both inulinase and invertase activities of the enzyme were taken into account, and the corresponding kinetic parameters were ...
P. CARNITI, P. L. BELTRAME, D. GUARDIONE, B. FOCHER, A. MARZETTI   +4 more
openaire   +3 more sources