Results 101 to 110 of about 341 (144)
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Immobilization ofAspergillus FicuumPhktase: Product Characterization of this Bioreactor

Preparative Biochemistry, 1988
Aspergillus ficuum phytase was covalently immobilized on Fractogel TSK HW-75 containing 2-oxy-l-alkylpyridinium salts. A packed-bed bioreactor was constructed with the immobilized phytase. An HPLC ion-exchange method was used to analyze the enzymatic products of the bioreactor. Immobilized fungal phytase was able to hydrolyze myo-inositol Hexa-, penta-,
A H, Ullah, B Q, Phillippy
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Sucrose hydrolysis by thermostable immobilized inulinases from aspergillus ficuum

Enzyme and Microbial Technology, 2001
The possibility of using thermostable inulinases from Aspergillus ficuum in place of invertase for sucrose hydrolysis was explored. The commercial inulinases preparation was immobilized onto porous glass beads by covalent coupling using activation by a silane reagent and glutaraldehyde before adding the enzyme.
M, Ettalibi, J C., Baratti
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Production and separation of exo- and endoinulinase from Aspergillus ficuum

Process Biochemistry, 2003
The production of both exo- and endoinulinase by Aspergillus ficuum JNSP5-06 was investigated. Optimum fermentation conditions were found to be: inulin, 2%; yeast extract, 2%; (NH4)H2PO4, 0.5%; NaCl, 0.5%; MgSO4·7H2O, 0.05%; ZnSO4·7H2O, 0.01%; initial pH 6.5.
Wang Jing   +3 more
openaire   +1 more source

The Specificity of Interactions between Endoinulinase from Aspergillus ficuum and Mono-, Di-, and Polysaccharides

Biophysics, 2023
The aim of this study was to analyze the peculiarities of spatial organization of an endoinulinase molecule from Aspergillus ficuum after its binding to mono-, di-, and polysaccharides. This study examined changes in volume and number of internal cavities upon binding of inulinase to mono- (glucose, fructose), di- (sucrose, mannose), and ...
S. M Makin   +5 more
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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
openaire   +1 more source

Aspergillus ficuum Phytase: Complete Primary Structure Elucidation by Chemical Sequencing

Biochemical and Biophysical Research Communications, 1993
The primary structure of Aspergillus ficuum phytase was deduced from overlaps in peptide sequences. The unglycosylated enzyme is a 441 residue protein with a molecular mass of 48.5-KDa, as calculated from the total covalent structure. The estimated pl of the protein is about 4.76. Of the 19 Asn residues, 9 were found to be glycosylated.
A H, Ullah, H C, Dischinger
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Microparticle-enhanced Aspergillus ficuum phytase production and evaluation of fungal morphology in submerged fermentation

open access: yesBioprocess and Biosystems Engineering, 2015
Phytase can be used in animal's diets to increase the absorption of several divalent ions, amino acids and proteins and to decrease the excessive phosphorus release in manure to prevent negative effects on the environment. This study aimed to enhance the current submerged fungal phytase productions with a novel fermentation technique by evaluating the ...
Hasan B Coban   +2 more
exaly   +5 more sources

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
openaire   +1 more source

Effect of immobilization on pH and thermal stability of Aspergillus ficuum phytase

Enzyme and Microbial Technology, 1999
Abstract The phytase from Aspergillus ficuum catalyzes the hydrolysis of phytic acid into phosphoric acid and myo -inositol. The activity of this enzyme was determined by monitoring the rate of inositol production using high-performance liquid chromography methodology. The maximum activity of the enzyme was found to be approximately pH 5 and had a
Bing-Lan Liu   +2 more
openaire   +1 more source

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   +6 more
openaire   +2 more sources

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