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  • 1
    Electronic Resource
    Electronic Resource
    Expression of an Erwinia pectate lyase in three species of Aspergillus (1996)
    Springer
    Current genetics 29 (1996), S. 474-481 
    Details
    ISSN: 1432-0983
    Keywords: Keywords Proteolytic degradation ; Expression ; Processing ; Glycosylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Transgenic filamentous fungi of the species Aspergillus niger, A. nidulans and A. awamori expressing and secreting Erwinia carotovora subsp. atroseptica pectate lyase 3 (PL3) were generated. Correct processing of the pre-enzyme was achieved using the A. niger pectin lyase A (PEL A) signal peptide. With the prepro-peptide of A. niger polygalacturonase II, secreted enzymes still possessed the 6- aa pro-sequence, indicating the importance of the conformation of the precursor protein for correct cleavage of the signal sequence. PL3 expression was markedly increased in media optimized for limited protease activity, and reached 0.4, 0.8 and 2.0 mg/l for expression in A. niger, A. awamori and A. nidulans, respectively. Glycans attached to the PL3 enzymes exhibited species-specific differences, and an increase of molecular mass coincided with reduced specific activities of the enzymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050074
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Expression of anErwinia pectate lyase in three species ofAspergillus (1996)
    Springer
    Current genetics 29 (1996), S. 474-481 
    Details
    ISSN: 1432-0983
    Keywords: Proteolytic degradation ; Expression ; Processing ; Glycosylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Transgenic filamentous fungi of the speciesAspergillus niger, A. nidulans andA. awamori expressing and secretingErwinia carotovora subsp.atroseptica pectate lyase 3 (PL3) were generated. Correct processing of the pre-enzyme was achieved using theA. niger pectin lyase A (PEL A) signal peptide. With the prepro-peptide ofA. niger polygalacturonase II, secreted enzymes still possessed the 6- aa pro-sequence, indicating the importance of the conformation of the precursor protein for correct cleavage of the signal sequence. PL3 expression was markedly increased in media optimized for limited protease activity, and reached 0.4, 0.8 and 2.0 mg/l for expression inA. niger, A. awamori andA. nidulans, respectively. Glycans attached to the PL3 enzymes exhibited species-specific differences, and an increase of molecular mass coincided with reduced specific activities of the enzymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02221517
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
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