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  • 1
    Electronic Resource
    Electronic Resource
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 13 (1993), S. 351-359 
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: α-Galactosidase (E.C.3.2.1.22) from Penicillium janthinellum was purified by precipitation and fractionation with ammonium sulphate, cold acetone or ethanol, calcium phosphate gel, and column chromatographies on Sephadex G-100 and G-200. The enzyme was purified about 110.39-fold when Sephadex G-100 was used. α-Galactosidase exhibited the optimum pH and temperature at 4.5 and 60°C, respectively. The optimum enzyme stability was obtained at pH 3.5 for 24 h (at room temperature). The enzyme was found to be thermostable below 65°C up to 40 minutes and was gradually inactivated by increasing the temperature above this degree. The MICHAELIS constant was 0.55 mM for p-nitrophenyl-α-D-galactoside. The α-galactosidase activity was strongly inhibited by Hg++ and slightly activated by Mn++. The results show the possibility of producing a thermostable enzyme from a low-priced agricultural product, for instance, lupine.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 9 (1989), S. 295-298 
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The aim of this work is to study the IR spectra of the different lignins precipitated from the produced liquor of different pulping conditions of bagasse and cotton stalks, also to study their antimicrobial activities towards some bacteria and fungi.
    Additional Material: 1 Tab.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 11 (1991), S. 227-233 
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Cell-free extracts of 3-4 days old mats of nitrate-grown Penicillium citrinum catalyze the hydrolytic cleavage of the N-glycosidic bonds of inosine, guanosine and adenosine optimally at pH 4, 0.1 M citrate buffer. The same extracts catalyze the hydrolytic deamination of cytidine at a maximum rate in 0.08 M Tris-acetate buffer pH 6.5, 40°C and 50°C were the most suitable degrees for purine nucleoside hydrolysis and cytidine deamination, respectively. The incubation of the extracts at 60°C, in the absence of cytidine caused a loss in the deaminating activity, while freezing and thawing had no effect on both activities. The deaminating activity seems to be cytidine specific as neither cytosine, adenine, adenosine nor guanosine could be deaminated. Uridine competively inhibited this activity, while ammonia had no effect. The apparent Km value of this enzyme for cytidine was 1.57×10-3M and its Ki value for uridine was 7.8×10-3M. The apparent Km values of the N-glycosidic bond cleaving enzyme for inosine, guanosine and adenosine were 13.3, 14.2 and 20×10-3 M, respectively.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 9 (1989), S. 479-483 
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Ten Aspergilli and Penicillia were tested for the capabilities of their extracts in degrading L-arabinose or L-arabonate nonphosphorolytically. L-arabonate dehydratase was nearly absent, while the reverse reaction of 2-keto-3-deoxy-L-arabonate (KDA) aldolase was operative in extracts of all the tested organisms grown on L-arabinose or L-arabonate as the sole carbon source. Degradation of different related substrates by cell-free extracts of Aspergillus ustus showed that L-arabonate, D-gluconate, D-galactonate and D-galactonic acid-γ-lactone were degraded under these conditions. Chromatographic studies identified the L-arabonate degrading products of such degradation in A. ustus as KDA (traces), pyruvic acid and α-ketoglutaric acid.
    Additional Material: 4 Tab.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 9 (1989), S. 485-489 
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The degradation of fifteen sugars, sugar acids and related substrates were examined using cellfree extracts of Aspergillus ustus growing on D-glucose, D-mannose, D-galactose or D-gluconate as the only carbon source. D-gluconate was superior for the induction of the enzymes capable for the degradation of some of these substrates. The addition of 0.5% malt extract with D-gluconate to the growth medium or the presence of shaking conditions resulted to an increase in the degradation of those substrates, whileas the incorporation of 0.5% malt extract alone to the medium has no effect. Extracts of D-gluconate-grown mycelia of A. ustus degraded D-gluconate 〉 D-galactonate 〉 1 : 5 gluconolactone and 〉 L-arabonate nonphosphorolytically more effectively. Optimum pH and temperature for the degradation of D-gluconate were found to be 8.0 and 40°C, respectively. Thermal stability studies on the behaviour of D-gluconate dehydratase showed that this enzyme was stable at 50°C and 60°C for 30 and 5 minutes, respectively. Specific activity of this enzyme was increased three times when cell-free extracts were incubated at 60°C for 5 minutes. MgCl2 and CoSO4 were good activators, while CaCl2 p-mercurychlorobenzoate (PMCB), sodium arsenite, ZnSO4, CuSO4, iodoacetic acid, MnCl2 and FeSO4 were potent inhibitors for D-gluconate dehydratase activity. Km was calculated for D-gluconate and found to be 2.5 × 10-2 M.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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