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. 1991 Apr;57(4):1259-60.
doi: 10.1128/aem.57.4.1259-1260.1991.

Purification and Characterization of d-Aminoacylase from Alcaligenes faecalis DA1

Y B Yang  1 , C S Lin, C P Tseng, Y J Wang, Y C Tsai
Affiliations

Purification and Characterization of d-Aminoacylase from Alcaligenes faecalis DA1

Y B Yang et al. Appl Environ Microbiol. 1991 Apr.

Abstract

A d-aminoacylase from Alcaligenes faecalis DA1 has been purified to homogeneity by a simple purification procedure with two columns, Fractogel DEAE-650 and HW-50. The specific activity of the purified enzyme was found to be 580 U/mg of protein with N-acetyl-dl-methionine as the reaction substrate. The apparent molecular weight and isoelectric point of this enzyme were determined to be 55,000 and 5.4, respectively.

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