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J Biotechnol. 2003 Feb 27;101(1):89-96.

Degradation of N-acylhomoserine lactones, the bacterial quorum-sensing molecules, by acylase.

Author information

1
Novozymes Biotech, Inc., 1445 Drew Avenue, Davis, CA 95616, USA. fxu@novozymes.com

Erratum in

  • J Biotechnol. 2003 Apr 10;102(1):99. Dussen Heinz-Josef [corrected to Deussen Heinz-Josef].

Abstract

Porcine kidney acylase I was shown to be able to deacylate N-acylhomoserine lactones, a family of chemicals employed by Gram-negative bacteria as quorum-sensing molecules for cell population density-dependent growth (such as biofilm formation). The enzyme transformed both N-butyryl-and N-octanoyl-L-homoserine lactones into L-homoserine. An optimal pH of 10 at 23 degrees C and an optimal temperature of 76 degrees C at pH 9 were found for the enzyme in hydrolyzing N-butyryl-homoserine lactone. At pH 9 and 23 degrees C, the enzymatic catalysis had a K(m) of 81+/-3 mM and a k(cat) of 127+/-2 nmol min(-1) per mg. The enzyme was also shown to be able to reduce the biofilm growth in an aquarium water sample. Potential physiological significance and medicinal/industrial applications of the N-acylhomoserine lactone-degrading activity of acylase are discussed.

PMID:
12523973
DOI:
10.1016/s0168-1656(02)00305-x
[Indexed for MEDLINE]

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