TY - JOUR
T1 - Overexpression of the Aspergillus niger pH 2.5 acid phosphatase gene in a heterologous host Trichoderma reesei
AU - Miettinen-Oinonen, Arja
AU - Torkkeli, Tuula
AU - Paloheimo, Marja
AU - Helena Nevalainen, Nevalainen
PY - 1997/10/2
Y1 - 1997/10/2
N2 - 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.
AB - 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.
KW - Feed
KW - Optimum acid phosphatase
KW - Overexpression
KW - pH 2.5
KW - Trichoderma
UR - http://www.scopus.com/inward/record.url?scp=0031549642&partnerID=8YFLogxK
U2 - 10.1016/S0168-1656(97)00121-1
DO - 10.1016/S0168-1656(97)00121-1
M3 - Article
C2 - 9335175
AN - SCOPUS:0031549642
SN - 0168-1656
VL - 58
SP - 13
EP - 20
JO - Journal of Biotechnology
JF - Journal of Biotechnology
IS - 1
ER -