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. 1991 Apr;57(4):1259–1260. doi: 10.1128/aem.57.4.1259-1260.1991

Purification and Characterization of d-Aminoacylase from Alcaligenes faecalis DA1

Yunn-Bor Yang 1, Chyuan-Sheng Lin 1, Ching-Ping Tseng 1, Yng-Jiin Wang 1, Ying-Chieh Tsai 1,*
PMCID: PMC182879  PMID: 16348465

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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