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  • 1
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The Lipomyces starkeyiα-amylase (LSA) gene encoding soluble starch-degrading α-amylase was cloned and characterized from a derepressed and partially constitutive mutant for both dextranase and amylase activities. The nucleotide (nt) sequence of the cDNA fragment reveals an open reading frame of 1944 bp encoding a 619 amino acid (aa) mature protein (LSA) with a calculated molecular weight of 68.709 kDa that was estimated to be about 73 kDa, including His tag (4 kDa) based on SDS–PAGE (10% acrylamide gel), activity staining, and the Western blotting, using anti-amylase-Ab. LSA had a sequence similar to other α-amylases in four conserved regions of the α-amylase family: (I) 287DIVVNH292, (II) 372GLRIDTVKH380, (III) 399GEVFD403, (IV) 462FLENQD467. Polymerase chain reaction and sequence analysis showed one intron of 60 nucleotides in the genomic lsa at positions between 966 and 967 of cDNA. The cloned LSA amylase showed a maximum activity at pH 6 and optimum temperature of 40 °C, with greater than 90% stability between pH 5 and pH 8 for 16 h. It was inhibited by Cu2+ and stimulated by Ca2+ and Mg2+. Enzyme activity was not affected by 1 mM EGTA but was inhibited by 1 mM EDTA. LSA did not hydrolyze maltodextrins of G2 to G4, yet formed G2 + G3 from G5, G2 + G4 or G3 + G3 from G6, and G3 + G4 from G7. LSA did not hydrolyze soluble starch in the present of 2% (w/v) of acarbose. Kinetics of LSA was carried out by using starch as a substrate and the inhibition type of acarbose was the mixed non-competitive type (Ki=3.4 μM).
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 799 (1996), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-6784
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract After irradiation with photons in the energy range of 70-1000 eV using the synchrotron radiation facility at Pohang, Korea, dextransucrase constitutive and hyper-producing mutants from Leuconostoc mesenteroides were isolated. The mutant (B-512FMCM) produced 13 times higher activity and showed complete constitutivity for dextransucrase production. It synthesized the same dextran as B-512FMC. The dextransucrase of the mutant transferred glucose from dextran to maltose. This novel method is a new technique for the development of industrial microorganisms.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1573-6784
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A new process for the production of small size dextran is developed in which dextran is produced by cultures of Leuconostoc mesenteroides in the presence of a partially constitutive mutant of Lipomyces starkeyi producing dextranase. Mixed cultures were examined by scanning electron microscopy with ruthenium to show the effects of the mixed culture on low molecular weight dextran (M.W. of 5,000 – 100,000) formation. The presence of the size variation in dextran was confirmed by gel permeation chromatography.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1573-6776
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Mixed culture fermentations containing a dextranase-producing yeast, Lipomyces starkeyi, and a dextransucrase-producing bacterium, Leuconostoc mesenteroides, produced dextrans of selected size using sucrose and starch. Dextran and starch hydrolyzates, produced by a Lipomyces starkeyi dextranase and amylase, were incorporated into the dextran and formed small size dextran (Mr = 40kDa). The yields of total and clinical dextran in mixed culture fermentation using 12% sucrose and 3% starch were higher, 84 and 79% of theoretical yield, than those using 15% sucrose only, 73 and 69% of theoretical yield, respectively.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 26 (1984), S. 905-910 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Inulin, a polyfruction, is found as the reserve carbohydrate in the roots and tubers of various plants (i.e. Jerusalem artichoke, chicory, and dahlia tubers). The β-fructofuranosidase (inulase) from the yeast Kluyveromyces fragilis is of interest because of its industrial potential in fructose syrup and alcohol production from inulin containing plants. We have found that the inulase of K. fragilis can be immobilized in the yeast cells by glutaraldehyde treatment. These cells are resistant to physical and enzymatic destruction. Although the exact nature of the immobilization is not fully understood, the kinetic parameters of the immobilized enzyme are similar to those of the soluble enzyme. No reduction of enzyme activity was observed after glutaraldehyde treatment and glutaraldehyde concentration did not affect enzyme activity. A 96% hydrolysis of dahlia inulin was achieved in 10.5 h with a 9.5% (w/v) fixed enzyme suspension. A Jerusalem artichoke extract containing 16.8%polyfructan was completely hydrolyzed in 3.5 h with a 0.24% (w/v)fixed enzyme suspension. This is a time frame feasible for industrial consideration.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Current microbiology 7 (1982), S. 93-98 
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The lipopolysaccharide (LPS) ofPseudomonas aeruginosa (ATCC 9027) exhibited gross changes in both the amount of LPS produced per cell and the composition of the LPS in response to changes in magnesium ion concentrations. Compositional variation in the LPS was detected under both batch and continuous culture conditions, and was particularly apparent as changes in the levels of heptose in the molecule. Compositional changes in the molecule were also reflected as functional alterations in the LPS. However, functionally, these alterations were counterbalanced by increased production of the lipopolysaccharide. We propose that LPS composition changed in accordance with environmental factors, and that cells responded to these changes by increasing or decreasing the amount of LPS produced.
    Type of Medium: Electronic Resource
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