Results 101 to 110 of about 338 (140)

DNA mediated transformation of Aspergillus ficuum

Applied Microbiology and Biotechnology, 1988
Two DNA-mediated transformation systems were successfully adapted to Aspergillus ficuum. Both the Escherichia coli hygromycin B resistance gene and the A. nidulans amdS gene transformation systems produced stable A. ficuum NRRL 3135 transformants. Cotransformation with the E. coli lacZ gene was also achieved with the hygromycin B system.
Edward J. Mullaney, Peter J. Punt, Cees A. M. J. J. Van den Hondel   +2 more
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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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Production of inulooligosaccharides by endoinulinases from Aspergillus ficuum

Food Research International, 2005
Inulooligosaccharide (IOS) production from inulin was studied using a partially purified endoinulinase and a purified endoinulinase, which originated from Aspergillus ficuum. At the optimal conditions, including 50 g/L inulin, an enzyme concentration of 10 U/g substrate, 45 °C, and pH 6.0, the inulin-degrading degree by partially purified endoinulinase
Jin Zhengyu, Wang Jing, 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 ...
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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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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Expression of the INU2 gene for an endoinulinase of Aspergillus ficuum in Saccharomyces cerevisiae

Biotechnology Letters, 1999
The INU2 gene encoding an endoinulinase of Aspergillus ficuum was expressed by the Kluyveromyces marxianus INU1 promoter in a SUC2-deleted Saccharomyces cerevisiae to produce the endoinulinase preparation free of an exoinulinase and an extracellular invertase in the culture medium. A recombinant yeast strain produced the sufficient amount of the enzyme
Hee-Seo Kim, Dong Whan Lee, Eun Ja Ryu, Tai-Boong Uhm, Moon-Sik Yang, Jung Bae Kim, Keon-Sang Chae   +6 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
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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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