Abstract
SUMMARY The amidohydrolase formed in the later stages of growth on glucose pep- tone medium by Candida utilis was purified 60-fold from cell-free extracts. The purified enzyme hydrolysed mono- and di-carboxylic acid amides, benzamide, nicotinamide, pyrazinamide and certain P-hydroxyl substituted fatty acid amides, was inactive on L-asparagine and L-glutamine and was competitively inhibited by urea and N-methylurea. Acetamide and nico- tinamide together showed mutual competition.

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