Production and synthetic dyes decolourization capacity of a recombinant laccase from Pichia pastoris
نویسندگان
چکیده
منابع مشابه
Production of a recombinant laccase from Pichia pastoris and biodegradation of chlorpyrifos in a laccase/vanillin system.
The recombinant strain P. pastoris GS115-lccC was used to produce laccase with high activity. Factors influencing laccase expression, such as pH, methanol concentration, copper concentration, peptone concentration, shaker rotate speed, and medium volume were investigated. Under the optimal conditions, laccase activity reached 12,344 U/L on day 15. The recombinant enzyme was purified by precipit...
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BACKGROUND Laccases are blue multi-copper oxidases and catalyze the oxidation of phenolic and non-phenolic compounds. There is considerable interest in using these enzymes for dye degradation as well as for synthesis of aromatic compounds. Laccases are produced at relatively low levels and, sometimes, as isozymes in the native fungi. The investigation of properties of individual enzymes therefo...
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Background: The methylotrophic yeast Pichia pastoris is an appealing production host for a variety of recombinant, including biologics. In this sense, various genetic- and non-genetic-based techniques have been implemented to improve the production efficiency of this expression platform. Los1 (loss of supression) encodes a non-essential nuclear tRNA exporter in Saccharomyces cerevisiae, which i...
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متن کاملCloning and heterologous expression of Laccase in pichia pastoris and determination some of biochemical properties
Laccase (EC 1.10.3.2) are multi-copper oxidase which catalyze the oxidation aromatic and non- aromatic compounds with electron reduction of molecular oxygen to water. Nucleotide sequence of laccase (accession number : ) was optimized according codon preference of Pichia pastoris. Gene was synthesized and cloned into pPICZalpha A. laccase under control of AOX1 promoter was transformed to P.pasto...
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ژورنال
عنوان ژورنال: Journal of Applied Microbiology
سال: 2009
ISSN: 1364-5072
DOI: 10.1111/j.1365-2672.2009.04291.x