Secretion of the Hormoconis resinae glucoamylase P enzyme from Trichoderma reesei directed by the natural and the cbh1 gene secretion signal.
Secretion of the Hormoconis resinae glucoamylase P (GAMP) enzyme from Trichoderma reesei using either the natural N-terminal extension of the premature glucoamylase P or the cellobiohydrolase I (CBHI) signal peptide was examined. The expression conditions for the heterologous glucoamylase P (gamP) gene in T. reesei were standardized by targeting one copy of a plasmid fragment, containing the gamP gene, to the cbh1 locus of the host. The results showed that the transient N-terminal extension of the premature GAMP acts as an efficient secretion signal in T. reesei and leads to a higher yield of extracellular glucoamylase activity than does the signal peptide of CBHI.
Joutsjoki
V V
VV
Research Laboratories, Alko Ltd., Helsinki, Finland.
Kuittinen
M
M
Torkkeli
T K
TK
Suominen
P L
PL
D000595:Amino Acid Sequence; D001483:Base Sequence; D001692:Biological Transport; D043366:Cellulose 1,4-beta-Cellobiosidase; D005087:Glucan 1,4-alpha-Glucosidase / Q000235:genetics / Q000378:metabolism*; D006026:Glycoside Hydrolases / Q000235:genetics*; D003904:Mitosporic Fungi / Q000235:genetics*; D008969:Molecular Sequence Data; D021382:Protein Sorting Signals / Q000235:genetics*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D014242:Trichoderma / Q000235:genetics
D021382:Protein Sorting Signals; D011993:Recombinant Fusion Proteins; D006026:Glycoside Hydrolases; D005087:Glucan 1,4-alpha-Glucosidase; D043366:Cellulose 1,4-beta-Cellobiosidase