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 ° 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.
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