Comparative Study on the N-acylase Activity of Mammalian Kidney Acetone Powders (KAP's)

The N-acylase activity and enantioselectivity of mammalian kidney acetone powders (KAP's) or their enzyme extract was dem- onstrated on (rac)-N-acetylmethionine; used as reference substrate. It was showed hydrolysis exclusively on the (S)-enantiomer. The bio- catalyzed reaction allowed us, to categorize the KAPs regarding the animal source, sheep, pig, calf, bovine, dog and guinea pig as fast biocatalysts reaching equilibrium in around 4 to 5 h; and rat, mouse and hamster were slower biocatalysts, since they did it in around 24 h. In most of the reactions the kidney crude preparations gave a better conversion than the enzyme extract, this fact demonstrated that the longer stirring during the reaction in an aqueous medium, allowed a greater dissolution of the enzyme. These readily available and inexpensive crude biocatalysts have a great potential application in organic synthesis.