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Production and biochemical characterization of a type B ferulic acid esterase from Streptomyces ambofaciens

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Abstract:

For the first time, the presence of a ferulic acid esterase (FAE) was demonstrated in Streptomyces ambofaciens. This extracellular enzyme was produced on a range of lignocellulosic substrates. The maximal level of activity was detected in the presence of either destarched wheat bran or oat spelt xylan as the sole carbon source. We found that 1% (m/v) of destarched wheat bran was the optimal concentration to induce its production. With this inducer, no ferulic acid dimers were released from the cell wall by the produced FAE. Interestingly, rape cattle cake (Brassica napus), which does not contain esterified ferulic acid, was also shown to induce the production of the FAE from S. ambofaciens. The FAE was partially purified from the culture supernatant. The purified enzyme was optimally active at pH 7 and 40 °C. The substrate specificity of the FAE from S. ambofaciens was investigated: the highest activity was determined with methyl p-coumarate, methyl ferulate, and methyl cinnamate. Furthermore, the FAE required a certain distance between the benzene ring and the ester bond to be active. According to these biochemical characteristics, the FAE from S. ambofaciens has been classified as a type B FAE.

La présence d’une acide férulique estérase (AFE) a été démontrée pour la première fois chez Streptomyces ambofaciens. Cette enzyme extracellulaire a été produite sur une gamme de substrats lignocellulosiques. Le niveau maximal d’activité a été détecté en présence de son de blé désamidonné ou de xylane d’avoine utilisés comme unique source de carbone. Une concentration de 1 % (p/v) de son de blé désamidonné était optimale pour induire sa production. Avec cet inducteur, aucun dimère d’acide férulique n’a été libéré de la paroi cellulaire par l’AFE. De façon intéressante, le tourteau de colza (Brassica napus) qui ne contient pas d’acide férulique estérifié induisait la production d’AFE chez S. ambofaciens. L’AFE a été partiellement purifiée du surnageant de culture. L’enzyme purifiée était active de façon optimale à pH 7 et à 40 °C. La spécificité de substrat de l’AFE de S. ambofaciens a été étudiée : l’activité la plus élevée a été obtenue avec le p-coumarate de méthyle, le férulate de méthyle et le cinnamate de méthyle. De plus, une certaine distance entre le cycle benzénique et la liaison ester était requise pour que l’AFE soit active. À partir de ces caractéristiques biochimiques, l’AFE de S. ambofaciens a été classée parmi les AFE de type B.

Document Type: Research Article

Publication date: 2009-06-01

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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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