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Optimization of medium and cultivation conditions for l-amino acid oxidase production by Aspergillus fumigatus

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A fungal strain was selected from the microbial repository of the North-East Institute of Science and Technology, Jorhat, India, which could produce a high yield of l-amino acid oxidase. 18SrRNA, ITS1, 5.8SrRNA ITS2, and partial 28 S rRNA sequencing and phenotypic characteristics indicate that it belong to the species Aspergillus fumigatus (designated as P13). Maximum production of enzyme (59.55 × 10−3 U/mg dry cell mass) was obtained in a medium containing 10 g/L glucose, 4 g/L yeast extract, and 4 g/L ammonium sulfate, with 20 mmol/L of l-threonine as the inducer. The optimum temperature for enzyme production was 30 °C at pH 7.0, with a shaking speed of 200 r/min. At 96 h, the enzyme activity was maximum. The A. fumigatus P13 l-amino acid oxidase accepts a broad substrate range, and the maximum enzyme activity (20.41 × 10−3 U/mg dry cell mass) was obtained with 50 mmol/L of dl-tyrosine. In the literature, no reports have been found regarding the production of l-amino acid oxidase by A. fumigatus. The enzyme showed enantiomerically pure amino acid formation, which has tremendous demand in industrial applications.

Une souche fongique qui pouvait produire de grandes quantités de l-amino acide oxydase a été sélectionnée à partir du référentiel microbien du North-East Institute of Science and Technology, Jorhat, Inde. Le séquençage de l’ARNr 18S, de l’ITS1, de l’ARNr 5.8S, de l’ITS2 et le séquençage partiel de l’ARNr28S ainsi que les caractéristiques phénotypiques indiquent qu’elle appartient à l’espèce Aspergillus fumigatus (appelée P13). La production maximale d’enzyme (59.55 × 10-3 U/mg poids sec de cellules) a été obtenue dans du milieu contenant 10 g/L de glucose, 4 g/L d’extrait de levure et 4 g/L d’ammonium sulfate, et 20 mmol/L de l-thréonine comme inducteur. La température optimale de production d’enzyme était 30 °C à pH 7.0, à une vitesse de rotation de 200 r/min. L’activité enzymatique était maximale après 96 h. La l-amino acide oxydase d’A. fumigatus P13 accepte un large spectre de substrats et l’activité maximale de l’enzyme (20.41 × 10-3 U/mg poids sec de cellules) a été obtenue avec 50 mmol/L de dl-tyrosine. Dans la littérature, aucune donnée n’a été trouvée relativement à la production de l-amino acide oxydase par A. fumigatus. L’enzyme catalysait la formation d’acides aminés énantiomériquement purs, lesquels sont en grande demande dans l’industrie.

Document Type: Research Article

Publication date: 2009-09-01

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  • Published since 1954, this monthly journal contains new research in the field of microbiology including applied microbiology and biotechnology; microbial structure and function; fungi and other eucaryotic protists; infection and immunity; microbial ecology; physiology, metabolism and enzymology; and virology, genetics, and molecular biology. It also publishes review articles and notes on an occasional basis, contributed by recognized scientists worldwide.
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