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 th e premature glucoamylase P or the cellobiohydrolase I (CBHI) signal pe ptide was examined. The expression conditions for the heterologous glu coamylase P (gamP) gene in T. reesei were standardized by targeting on e copy of a plasmid fragment, containing the gamP gene, to the cbh1 lo cus of the host. The results showed that the transient N-terminal exte nsion of the premature GAMP acts as an efficient secretion signal in T . reesei and leads to a higher yield of extracellular glucoamylase act ivity than does the signal peptide of CBHI.