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  • 1
    Electronic Resource
    Electronic Resource
    Genetic Engineering of Extracellular Enzyme Systems of Bacilli (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 469 (1986), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1986.tb26480.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Secretion and processing of the Bacillus subtilis endo-β-1,3-1,4-glucanase in Escherichia coli (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 2 (1988), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The endo-β-1,3-1,4-glucanase enzyme of Bacillus subtilis C120, when synthesized in Escherichia coli, is located mainly in the cytoplasm, but enzyme activity is also detected in the periplasmic space and in the extracellular medium. The proportion recovered in the extracellular medium is not altered by changes in the levels of synthesis of the enzyme. Lysis of E. coli cells is ruled out as the cause of the secretion by the normal localization of β-galactosidase, an intracellular protein. However, β-lactamase, which is normally found in the periplasmic space, is detected in the extracellular medium of E. coli transformants containing β-glucanase plasmids, suggesting that the presence of β-glucanase in the cell alters the permeability of the outer membrane. The β-glucanase proteins found in the extracellular medium, the periplasmic space and the cytoplasm have the same electrophoretic mobilities as the secreted enzyme of B. subtilis. Amino-terminal sequencing has shown that the β-glucanase enzyme in the intracellular fraction of E. coli is processed at a site two amino acids distant from the processing site used in B. subtilis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1988.tb00093.x
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  • 3
    Electronic Resource
    Electronic Resource
    Molecular cloning and characterization of a Candida tsukubaensis α-glucosidase gene in the yeast Saccharomyces cerevisiae (1991)
    Springer
    Current genetics 20 (1991), S. 45-52 
    Details
    ISSN: 1432-0983
    Keywords: Candida tsukubaensis ; α-glucosidase gene ; Amylolytic enzyme ; S. cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The molecular cloning of an α-glucosidase gene isolated from a Candida tsukubaensis (CBS 6389) genomic library in Saccharomyces cerevisiae is reported. The cloned gene is contained within a 6.2 kb Sau3A DNA fragment and directs the synthesis and secretion of an amylolytic enzyme into the extracellular medium of the recombinant host, S. cerevisiae. The cloned enzyme was found to have an unusually broad substrate specificity and is capable of hydrolysing α-1,2, α-1,3, α-1,4 and α1,6 linked, as well as aryl and alkyl, d-glucosides. On the basis of its substrate specificity profile, the cloned enzyme was classified as an α-glucosidase (E.C. 3.2.1.20). It has a pH optimum in the range 4.2–4.6, a temperature optimum of 58°C and is readily inactivated at pasteurization temperature (60°C). Southern blot analysis failed to reveal any homology between the cloned gene and genomic DNA isolated from other well characterized amylolytic yeasts. A rapid plate-assay, based on the utilization of a chromogenic substrate X-α-d-glucoside to detect the expression of the cloned α-glucosidase in S. cerevisiae transformants, was developed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00312764
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  • 4
    Electronic Resource
    Electronic Resource
    Analysis of the expression and secretion of the Candida tsukubaensis α-glucosidase gene in the yeast Saccharomyces cerevisiae (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 7 (1991), S. 445-454 
    Details
    ISSN: 0749-503X
    Keywords: Heterologous expression ; S. cerevisiae ; α-glucosidase ; secretion ; maltose utilization ; novel promoter ; Candida tsukubaensis ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The α-glucosidase gene of Candida tsukubaensis is contained within a 3·47 kb BamH1-Mlu1 fragment which, when introduced into Saccharomyces cerevisiae AH22 on a yeast-Escherichia coli shuttle vector, allows the transformants to utilize maltose as sole carbon source. Thus, the cloned gene confers a dominant selectable phenotype on transformed strains of S. cerevisiae which are otherwise unable to grow in nutrient media containing maltose, dextrin or other α-1,4-linked α-D-glucopyranosides, specifically hydrolysed by the α-glucosidase. The cloned enzyme expressed in yeast is secreted into the extracellular medium in a glycosylated form which accounts for up to 60% of the secreted protein and has a molecular size of 70-80 kilodalton (kDa). Deglycosylation of the α-glucosidase showed that the enzyme is composed of two distinct polypeptides with subunit molecular weights of 63-65 kDa (peptide 1) and 50-52 kDa (peptide 2). An increase in the level of expression of the α-glucosidase by yeast transformants in selective minimal medium was obtained by using a vector with increased copy number containing the leu2-d gene as selectable marker. The α-glucosidase gene promoter functions more effectively than the Gal1-10 promoter in directing α-glucosidase expression in S. cerevisiae. It also directs the expression of high levels of β-galactosidase activity in yeast when fused to a promoterless E. coli lacZ gene. Expression of the α-glucosidase gene under the control of its own promoter is constitutive, orientation dependent and not subject to catabolite repression.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320070503
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    Paper (German National Licenses)
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