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

Abstract

The N-acylase activity and enantioselectivity of mammalian kidney acetone powders (KAP’s) or their enzyme extract was demonstrated on (<em>rac</em>)-N-acetylmethionine; used as reference substrate. It was showed hydrolysis exclusively on the (<em>S</em>)-enantiomer. The biocatalyzed 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.

Assessment of genetically modified oilseed rape 73496 for food and feed uses, under Regulation (EC) No 1829/2003 (application EFSA‐GMO‐NL‐2012‐109)

“…Aminoacylases genes (ACY1 and ASPA) are nearly ubiquitously present in organs and tissues, with sequences moderately to highly conserved across animal species (Yates et al., 2020). Acylase I and acylase II enzymes catalyse the stereospecific hydrolysis of N‐acetylated amino acids, including NAA, and are identified in multiple tissues from various species including intestine, liver and kidneys, presumably mediating the catabolism of ingested N‐acetylated amino acids under normal dietary conditions (Birnbaum et al., 1952; Birnbaum, 1955; Nadler and Cooper, 1972; D'Adamo et al., 1973; Endo, 1978; Endo, 1980; Daabees et al., 1984; Giardina et al., 1997; Giardina et al., 1999; Lindner et al., 2000; Arnaud et al., 2004; Hershfield et al., 2006; Surendran et al., 2006; Mersmann et al., 2011; Luna et al., 2013).…”