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Heterologous expression of the benzoate para-hydroxylase encoding gene (CYP53B1) from Rhodotorula minuta by Yarrowia lipolytica Inra
Shiningavamwe, A.; Obiero, G.; Albertyn, J.; Nicaud, J.M.; Smit, M..
There is currently an increasing number of cytochrome P450 (CYP450) monooxygenase encoding genes becoming available from various genome-sequencing projects. These enzymes require association with cytochrome P450 reductase (CPR) to achieve optimal activities. In this study, the CYP53B1 gene, which encodes a benzoate para-hydroxylase, was successfully cloned from Rhodotorula minuta and overexpressed in Yarrowia lipolytica E150. Multiple copies of the CYP53B1 cDNA were cloned under the POX2 promoter, while the Y. lipolytica CPR was cloned under the isocitrate lyase promoter. Whole cell biotransformation of benzoic acid to para-hydroxybenzoic acid (pHBA) was used to analyse the hydroxylase activity of the recombinant Y. lipolytica UOFS Y-2366. Different...
Tipo: Journal Article Palavras-chave: CYTOCHROME P450; BENZOATE PARA-HYDROXYLASE; OVEREXPRESSION; BIOTRANSFORMATION; RECOMBINANT PROTEIN.
Ano: 2006 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2007ef204447&uri=/notices/prodinra1/2010/09/
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Natural and recombinant fungal laccases for paper pulp bleaching Inra
Sigoillot, C.; RECORD, E.; Belle, V.; ROBERT, J.L.; LEVASSEUR, A.; Punt, P.J.; Van Den Hondel, C.A.M.J.J.; Fournel, A.; Sigoillot, J.C.; ASTHER, M..
Three laccases, a natural form and two recombinant forms obtained from two different expression hosts, were characterized and compared for paper pulp bleaching. Laccase from Pycnoporus cinnabarinus, a well known lignolytic fungus, was selected as a reference for this study. The corresponding recombinant laccases were produced in Aspergillus oryzae and A. niger hosts using the lacI gene from P. cinnabarinus to develop a production process without using the expensive laccase inducers required by the native source. In flasks, production of recombinant enzymes by Aspergilli strains gave yields close to 80 mg l–1. Each protein was purified to homogeneity and characterized, demonstrating that the three hosts produced proteins with similar physico-chemical...
Tipo: Journal Article Palavras-chave: PULPE DE PAPIER; BIOTECHNOLOGIE INDUSTRIELLE; PROPRIETE PHYSICOCHIMIQUE LACCASE; RECOMBINANT PROTEIN.
Ano: 2004 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2007a0177074&uri=/notices/prodinra1/2010/09/
Registros recuperados: 2
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