Murphy_1996_Appl.Environ.Microbiol_62_456

Reference

Title : Fusarium polycaprolactone depolymerase is cutinase - Murphy_1996_Appl.Environ.Microbiol_62_456
Author(s) : Murphy CA , Cameron JA , Huang SJ , Vinopal RT
Ref : Applied Environmental Microbiology , 62 :456 , 1996
Abstract :

Polycaprolactone (PCL), a synthetic polyester, is degraded by a variety of microorganisms, including some phytopathogens. Many phytopathogens secrete cutinase, a serine hydrolase that degrades cutin, the structural polymer of the plant cuticle. We compared wild-type strains and a cutinase-negative gene replacement mutant strain of Fusarium solani f. sp. pisi (D. J. Stahl and W. Schnfer, Plant Cell 4:621-629, 1992) and a wild-type strain of Fusarium moniliforme to show that Fusarium cutinase is a PCL depolymerase. The wild-type strains, but not the mutant strain, (i) degraded PCL and used it as a source of carbon and energy, (ii) showed induction of secreted PCL depolymerase and an esterase activity of cutinase when grown in the presence of cutin, and (iii) showed induction of PCL depolymerase and an esterase activity of cutinase when grown in the presence of a hydrolysate of PCL, which contains PCL oligomers that are structurally similar to the natural inducers of cutinase. These results together with other details of regulation and conditions for optimal enzyme activity indicate that the Fusarium PCL depolymerase, required for degradation and utilization of PCL, is cutinase.

PubMedSearch : Murphy_1996_Appl.Environ.Microbiol_62_456
PubMedID: 8593048
Gene_locus related to this paper: fusso-CUT2 , fusso-CUT3

Related information

Substrate Polycaprolactone
Gene_locus fusso-CUT2    fusso-CUT3

Citations formats

Murphy CA, Cameron JA, Huang SJ, Vinopal RT (1996)
Fusarium polycaprolactone depolymerase is cutinase
Applied Environmental Microbiology 62 :456

Murphy CA, Cameron JA, Huang SJ, Vinopal RT (1996)
Applied Environmental Microbiology 62 :456