Wjj. Vandentweel et al., OCHROBACTRUM-ANTHROPI NCIMB-40321 - A NEW BIOCATALYST WITH BROAD-SPECTRUM L-SPECIFIC AMIDASE ACTIVITY, Applied microbiology and biotechnology, 39(3), 1993, pp. 296-300
Of 125 microorganisms that were able to use alpha-hydroxy acid amides
as sole nitrogen source, Ochrobactrum anthropi NCIMB 40321 was selecte
d for its ability to hydrolyse racemic amides L-selectively. The subst
rate specificity of whole O. anthropi cells is remarkably wide and ran
ges from alpha-H-alpha-amino-, alpha-alkyl-alpha-amino, N-hydroxy-alph
a-amino acid amides to alpha-hydroxy-acid amides. After 50% conversion
, both the L-acids formed and the remaining D-amides were present in >
99% enantiomeric excess, and ammonia accumulated in stoichiometric amo
unts. Using mandelic acid amide as a model substrate, the hydrolysis w
as optimized. Optimal rates were observed at pH 8.5 at 50-degrees-C. A
t higher temperatures the initial rate was even higher; however, fairl
y rapid inactivation occurred.