Loading...
CLONING, EXPRESSION AND CHARACTERIZATION OF CUTINASE, A FUNGAL LIPOLYTIC ENZYME
Lauwereys, Mark de Geus, Pieter De Meutter, J. Stanssens, P. Matthyssens, G.
Lauwereys, Mark
de Geus, Pieter
De Meutter, J.
Stanssens, P.
Matthyssens, G.
Citations
Altmetric:
Advisors
Editors
Other Contributors
Issue Date
1991
Submitted date
2024-03-20
Files
Loading...
PDF
Adobe PDF, 4.12 MB
Other Titles
Abstract
A cutinase from the fungus Fusarium solani pisi has been overproduced in E. coli
by placing a phoA-signal/cutinase hybrid gene under the control of the tac promoter.
Due to its periplasmic location the recombinant enzyme can be easily purified in
large quantities. Assays using p-nitrophenylbutyrate suggest that the overproduced
and authentic enzyme are catalytically equivalent. The specific activities on
tributyrin (4000u/mg) and triolein (800u/mg) demonstrate the lipolytic nature of the
enzyme. The cutinase, however, differs from classical lipases in that no measurable
activation around the CMC of the tributyrin substrate is observed. We also provide
evidence that the recombinant enzyme is quite thermostable.
Citation
Lipases : structure, mechanism and genetic engineering, 243 - 251
DOI
PubMed ID
PubMed Central ID
Additional Links
Embedded video
Type
Book chapter
conference paper
conference paper
Language
en
Description
Series/Report no.
GBF monographs ; Volume 16
ISSN
0930-4320
EISSN
ISBN
156081165X
3527283323
3527283323
ISMN
Gov't Doc #
Sponsors
License
Attribution-NonCommercial-ShareAlike 4.0 International