Characterization of D-Aminoacylase from Alcaligenes denitrificans DA181

概要

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The D-aminoacylase produced by Alcaligenes denitrificans DA181 was a new type of aminoacylase which had both high stereospecificity and specific activity. The molecular weight and isoelectric point of this enzyme were 58,000 and 4.4,respectively. The apparent K_m and κ_cat values of this enzyme for N-acetyl-D-methionine were estimated to be 0.48 mM and 6.24×10^4 min^<-1>, respectively. The optimum temperature was 45℃. The enzyme was stable up to 55℃ for 1 hr in the presence of 0.2 mg/ml bovine serum albumin. The enzyme was stable in the pH range of 6.0 to 11.0 with an optimum pH of 7.5. This enzyme contained about 2.1 g atom of zinc per mole of enzyme. Enzyme activity was inhibited by incubation with EDTA. The inhibition by EDTA was fully reversed by Co^<2+> and partially by Zn^<2+>.
社団法人日本農芸化学会の論文
1992-09-23