Efficient production of the industrial biocatalysts hydantoinase and N -carbamyl amino acid amidohydrolase: Novel non-metabolizable inducers
1993; Oxford University Press; Volume: 109; Issue: 1 Linguagem: Inglês
10.1111/j.1574-6968.1993.tb06145.x
ISSN1574-6968
AutoresPatrick C. MEYER, Serge Runser,
Tópico(s)Microbial Metabolites in Food Biotechnology
ResumoThe 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.
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