Self-cloning in filamentous fungi: application to the construction of endothiapepsin overproducers in Cryphonectria parasitica.
The filamentous ascomycete fungus Cryphonectria parasitica naturally secretes endothiapepsin, an aspartic proteinase. It is cultured on a commercial scale as a source of the milk-clotting enzyme for cheese making. Our objective was to increase enzyme production of an industrial C. parasitica strain by a new technique of self-cloning; it consisted in the screening for transformants producing higher levels of endothiapepsin and having integrated only the DNA fragment of interest. Such genetically improved strains that are devoid of any foreign genes should be more readily acceptable for the production of food-grade enzymes.
Jara
P
P
Sanofi Recherche, Centre de Labège, France.
Delmas
P
P
Razanamparany
V
V
Olsen
L
L
Dupin
P
P
Bayol
A
A
Bégueret
J
J
Loison
G
G
D000085:Acetates; D001203:Ascomycota / Q000201:enzymology / Q000235:genetics*; D016282:Aspartic Acid Endopeptidases / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D001483:Base Sequence; D015139:Blotting, Southern; D002364:Caseins / Q000378:metabolism; D003001:Cloning, Molecular; D003470:Culture Media; D015966:Gene Expression Regulation, Fungal / Q000235:genetics; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000235:genetics; D008969:Molecular Sequence Data; D011401:Promoter Regions, Genetic / Q000235:genetics; D014170:Transformation, Genetic; D014357:Trypsin / Q000378:metabolism
D000085:Acetates; D002364:Caseins; D003470:Culture Media; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D014357:Trypsin; D016282:Aspartic Acid Endopeptidases; C042466:Endothia aspartic proteinase