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Isobutylidenediurea degradation by Rhodococcus erythropolis

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Abstract

A new enzyme (isobutylidenediurea amidinohydrolase) catalyzing the hydrolysis of isobutylidenediurea (a condensation product of urea and isobutyraldehyde widely used as a slow-release nitrogeneous fertilizer) was characterized from a strain of Rhodococcus erythropolis. The enzyme was purified 1250-fold to apparent homogeneity and shown to hydrolyze the fertilizer to urea and isobutyraldehyde at a molar ratio of 2 : 1. No activity was observed with ureido- or other structurally related compounds. Its molecular mass was determined by native polyacrylamide gelelectrophoresis and matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry to be 15 kDa (±2 kDa) and 16.4 kDa, respectively. Growth of the bacterium in the presence of isobutylidenediurea led to an increased expression of the constitutively synthetized enzyme.

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  1. Fachrichtung 8.3 Mikrobiologie, Universität des Saarlandes, Postfach 151150, D-66041, Saarbrücken, F.R.G. Author for Correspondence E-mail

    Thomas Jahns & Roswitha Schepp

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  1. Thomas Jahns
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  2. Roswitha Schepp
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Correspondence to Thomas Jahns.

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Jahns, T., Schepp, R. Isobutylidenediurea degradation by Rhodococcus erythropolis . Biodegradation 12, 317–323 (2001). https://doi.org/10.1023/A:1014335602141

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