The aim of industrial enzymic amoxycillin production: Characterization of a novel carbamoylase enzyme in the form of a crude, cell-free extract

Louwrier, A. and Knowles, C.J. (1997) The aim of industrial enzymic amoxycillin production: Characterization of a novel carbamoylase enzyme in the form of a crude, cell-free extract. Biotechnology and Applied Biochemistry, 25 . pp. 143-149. ISSN 0885-4513. (The full text of this publication is not available from this repository)

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Abstract

Amoxycillin production involves the generation of a racemic mixture of hydroxyphenylhydantoin by means of the Bucherer synthesis, The hydantoin is enzymically cleaved by a D-(-)-specific hydantoinase to form D-(-)-N-carbamoylhydroxyphenylglycine. This is subsequently hydrolysed by a carbamoylase enzyme that generates the amino acid derivative, D-(-)-hydroxyphenylglycine. The remaining L-(+)hydroxyphenylhydantoin spontaneously racemizes, allowing continual cleavage to continue (by the hydantoinase action) and giving a potential 100% yield of end product from the two-enzyme-catalysed process, rather than 50%, A novel carbamoylase from an Agrobacterium species has been studied in a crude (cell-free extract) form, The temperature stability was shown to be remarkable, with no loss of activity detected after 4 h at 50 degrees C. Kinetic values were calculated for the enzyme, with a variety of implications for a future industrial process, The substrate specificity, isoelectric point, pH and temperature activity profiles were elucidated, with the aim of generating a commercially beneficial method of purifying the enzyme, In addition, the concentration-dependent toxicities of several metal ions were studied; all bivalent ions studied were found to have some detrimental effect on activity.

Item Type: Article
Subjects: Q Science
Q Science > QH Natural history > QH301 Biology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: M.A. Ziai
Date Deposited: 20 Apr 2009 16:47
Last Modified: 20 Apr 2009 16:47
Resource URI: http://kar.kent.ac.uk/id/eprint/18168 (The current URI for this page, for reference purposes)
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