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Purification and Characterization of an Adipamidase from a Mutant Strain of Brevibacterium sp. Involved in Dinitrile
J L Moreau1, S Azza1, A Arnaud1
1a Chaire de Microbiologie Industrielle et de Génétique des Microorganismes , Ecole Nationale Supérieure Agronomique de Montpellier , Place Viala, 34060 Montpellier Cedex , France.
Abstract:
The adipamidase of a mutant strain of Brevibacterium sp. involved in the degradation of adiponitrile into adipic acid was purified and characterized. The molecular wight of the native enzyme was estimated at 120,000 and that of the sub-units at 58,000, suggesting that this is a dimer structure. This enzyme has a large activity spectrum; all the amides tested were found to be substrates of the adipamidase. An acyltransferase activity was also detected for short chain substrates (acetamide, acetic acid), as well as long chain substrates (oleic acid).
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