Purification and Characterization of a Novel Peroxidase from Geotrichum candidum Dec 1 Involved in Decolorization of Dyes
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چکیده
منابع مشابه
Purification and characterization of a novel peroxidase from Geotrichum candidum dec 1 involved in decolorization of dyes.
A peroxidase (DyP) involved in the decolorization of dyes and produced by the fungus strain Geotrichum candidum Dec 1 was purified. DyP, a glycoprotein, is glycosylated with N-acetylglucosamine and mannose (17%) and has a molecular mass of 60 kDa and an isoelectric point (pI) of 3.8. The absorption spectrum of DyP exhibited a Soret band at 406 nm corresponding to a hemoprotein, and its Na2S2O4-...
متن کاملEfficient heterologous expression in Aspergillus oryzae of a unique dye-decolorizing peroxidase, DyP, of Geotrichum candidum Dec 1.
Efficient expression of the dye-decolorizing peroxidase, DyP, from Geotrichum candidum Dec 1 in Aspergillus oryzae M-2-3 was achieved by fusing mature cDNA encoding dyp with the A. oryzae alpha-amylase promoter (amyB). The activity yield of the purified recombinant DyP (rDyP) was 42-fold compared with that of the purified native DyP from Dec 1. No exogenous heme was necessary for the expression...
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Background: Alkaline proteases is the important group of enzymes having numerous industrial applications including dairy food formulations. Objectives: The current study deals with the purification and characterization of an alkaline serine protease produced by Geotrichum candidum QAUGC01, isolated from indigenous fermented milk product, Dahi.<br...
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to discuss my point, i have collected quite a number of articles, anthologies, and books about "wuthering heights" applying various ideas and theories to this fantastic story. hence, i have come to believe that gadamer and jauss are rightful when they claim that "the individaul human mind is the center and origin of all meaning," 3 that reading literature is a reader-oriented activity, that it ...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 1999
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.65.3.1029-1035.1999