SOME ENZYMIC PROPERTIES OF A PARTIALLY PURIFIED AMINOACYLASE OBTAINED FROM A POLISH VARIETY OF RAPESEED (BRASSICA CAMPESTRIS L.)

Publisher Website
Google Scholar
Abstract
Aminoacylase, which hydrolyzes N-acetyl amino acids, has been demonstrated in rapeseed. The enzyme was purified 150-fold by fractionation with ammonium sulphate and calcium phosphate gel. The purified preparation hydrolyzed N-acetyl amino acids and in addition certain dipeptides and chloracetyl-L-tyrosine. The enzyme was stable at −20 °C and had a wide pH optimum (7.2 to 8.8). Cobalt ion was found to be an activator, while sulphydryl-reacting agents such as p-chloromercuribenzoate and some metal-chelating agents inhibited the hydrolysis. The enzyme showed rigorous specificity for the L-isomer. A comparison of the ratio of activities obtained for different enzyme preparations indicates that more than one enzyme is concerned in the hydrolysis of the different substrates.

This publication has 16 references indexed in Scilit: