Overexpression of the Aspergillus niger pH 2.5 acid phosphatase gene in a heterologous host Trichoderma reesei.
An Aspergillus gene coding for a pH 2.5 acid phosphatase enzyme was successfully overexpressed in Trichoderma reesei under the strong main cellobiohydrolase I (cbh 1) promoter. The best transformants produced up to 240 times more of the acid phosphatase than the Aspergillus strain from which the phosphatase gene was originally isolated. The recombinant enzyme was effectively secreted into the culture medium both by its own and the cbh 1 secretion signal. The heterologous pH 2.5 acid phosphatase enzyme produced by the Trichoderma transformants was seen as four protein bands of about 55-66 kD resulting from variable glycosylation in Trichoderma. The activity of the recombinant enzyme was not affected. Enzyme preparations rich in both cellulose and phytate hydrolysing enzymes are of interest in the animal feed industry.
Miettinen-Oinonen
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A
Primalco Ltd Biotec, Rajamäki, Finland.
Torkkeli
T
T
Paloheimo
M
M
Nevalainen
H
H
D000135:Acid Phosphatase / Q000096:biosynthesis / Q000235:genetics*; D001234:Aspergillus niger / Q000201:enzymology / Q000235:genetics*; D015971:Gene Expression Regulation, Enzymologic; D006863:Hydrogen-Ion Concentration; D011994:Recombinant Proteins / Q000096:biosynthesis; D014242:Trichoderma / Q000235:genetics*
D011994:Recombinant Proteins; D000135:Acid Phosphatase