Utilize este identificador para referenciar este registo: http://hdl.handle.net/10400.21/5116
Título: Production, purification and characterization of laccase from pleurottus ostreatus grown on tomato pomace
Autor: Freixo, Maria do Rosário
Karmali, Amin Mahamede Vissanji
Arteiro, José Maria Santos
Palavras-chave: Laccase from Pleurotus Ostreatus
Lignocellulosic Enzymes
Affinity Chromatography
Reverse IMAC
Epoxy-Activated Sepharose 6B-urea
Tomato Pomace
Chromatographic behavior
Affinity-chromatography
Pseudomonas-aeruginosa
Versicolor
Xylanase
Adsorption
Industrial
Strains
Amidades
Lignin
Data: Jan-2012
Editora: Springer
Citação: FREIXO, M. do R.; KARMALI, A.; ARTEIRO, J. M. – Production, purification and characterization of laccase from pleurottus ostreatus grown on tomato pomace. World Journal of Microbiology & Biotechnology. ISSN: 0959-3993. Vol. 28, nr. 1 (2012), pp. 245-254
Resumo: A strain of Pleurotus ostreatus was grown in tomato pomace as sole carbon source for production of laccase. The culture of P. ostreatus revealed a peak of laccase activity (147 U/L of fermentation broth) on the 4th day of culture with a specific activity of 2.8 U/mg protein. Differential chromatographic behaviour of laccase was investigated on affinity chromatographic matrices containing either urea, acetamide, ethanolamine or IDA as affinity ligands. Laccase exhibited retention on such affinity matrices and it was purified on a Sepharose 6B-BDGE-urea column with final enzyme recoveries of about 60%, specific activity of 6.0 and 18.0 U/mg protein and purification factors in the range of 14-46. It was also possible to demonstrate that metal-free laccase did not adsorb to Sepharose 6B-BDGE-urea column which suggests that adsorption of native laccase on this affinity matrix was apparently due to the specific interaction of carbonyl groups available on the matrix with the active site Cu (II) ions of laccase. The kinetic parameters (V (max), K (m) , K (cat), and K (cat)/K (m) ) of the purified enzyme for several substrates were determined as well as laccase stability and optimum pH and temperature of enzyme activity. This is the first report describing the production of laccase from P. ostreatus grown on tomato pomace and purification of this enzyme based on affinity matrix containing urea as affinity ligand.
Peer review: yes
URI: http://hdl.handle.net/10400.21/5116
DOI: 10.1007/s11274-011-0813-4
ISSN: 0959-3993
Aparece nas colecções:ISEL - Eng. Quim. Biol. - Artigos



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