ISSN:
1574-6968
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Biology
Notes:
Abstract The biosynthesis of the hydantoin-hydrolysing enzymes hydantoinase and N-carbamyl amino acid amidohydrolase from Agrobacterium sp. IP I-671, a Gram-negative bacterium used as a biocatalyst for the production of enantiomerically pure (R) amino acids, was found to be highly inducible by the addition to the cultivation medium of different non-metabolizable thiolated hydantoins or pyrimidines. Among these inducers the hexacyclic pyrimidine thioderivatives were more potent than all the pentacyclic thiohydantoin compounds. Addition of 2,4-thiouracil to the cultures, at a rate of 0.1 g (g cell dry mass)−1, led to no appreciable growth inhibition and yielded a biocatalyst exhibiting a 40-fold higher hydantoinase and a 15-fold higher N-carbamyl amino acid amidohydrolase activity than the corresponding inducer-free cultures.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1574-6968.1993.tb06145.x
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