Results 141 to 150 of about 1,150 (171)

Controlled Production of Fructose by an Exoinulinase from Aspergillus Ficuum

Applied Biochemistry and Biotechnology, 2009
An exoinulinase has been isolated, purified and characterised from a commercially available broth of Aspergillus ficuum. The enzyme was purified 4.2-fold in a 21% yield with a specific activity of 12,300 U mg(-1)(protein) after dialysis, ammonium sulphate fractionation and Sephacryl S-200 size exclusion and ion exchange chromatography.
T, Mutanda, B, Wilhelmi, C G, Whiteley
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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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Separation and Identification of Exo- and Endoinulinase from Aspergillus ficuum

Current Microbiology, 2003
A new and convenient method was developed to separate and identify exo- and endoinulinase from Aspergillus ficuum by native polyacrylamide gel electrophoresis. Eight protein bands were obtained. Three bands were identified as exoinulinase, and two bands were endoinulinase, by using TLC and HPLC.
Wang, Jing, Jin, Zhengyu, Jiang, Bo, Xu, Xueming   +3 more
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Vinegar production residue as substrates for phytase production by Aspergillus ficuum

Waste Management & Research: The Journal for a Sustainable Circular Economy, 2009
Two kinds of vinegar production residues, sorghum vinegar residue (SVR) and corn vinegar residue (CVR), were used as a substrate for phytase production in solid-state fermentation (SSF) by Aspergillus ficuum. Various process parameters influencing phytase production were evaluated by single factor design experiments; further study involved CVR and its
Zhihong, Wang, Xiaofang, Dong, Jianming, Tong, Yingying, Wu, Qi, Zhang   +4 more
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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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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, Jin Zhengyu, Jiang Bo, Adamu Augustine   +3 more
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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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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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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, A. N Dubovitskaya, D. Yu Bogomolov, M. S Kondratyev, M. G Holyavka, V. G Artyukhov   +5 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
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