Efficient expression of a Phanerochaete chrysosporium manganese peroxidase gene in Aspergillus oryzae

Journal Article · Fri Mar 01 00:00:00 EST 1996 · Applied and Environmental Microbiology

OSTI ID:433558

Stewart, P ^[1]; Whitwam, R E; Tien, Ming ^[2]

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1. Univ. of Wisconsin, Madison, WI (United States)
2. Pennsylvanis State Univ., University Park, PA (United States); and others

A manganese peroxidase (mnp1) from Phanerochaete chrysosporium was efficiently expressed in Aspergillus oryzae. Expression was achieved by fusing the mature cDNA of mnp1 with the A. oryzae Taka amylase promoter and secretion signal. The 3{prime} untranslated region of the glucoamylase gene of Asperigillus awamori provided the terminator. The recombinant protein (rMnP) was secreted in an active form, permitting rapid detection and purification. Physical and kinetic properties of rMnP were similar to those of the native protein. The A. oryzae expression system is well suited for both mechanistic and site-directed mutagenesis studies. 34 refs., 7 figs., 1 tab.

• OSTI ID: 433558
• Journal Information: Applied and Environmental Microbiology, Vol. 62, Issue 3; Other Information: PBD: Mar 1996
• Country of Publication: United States
• Language: English

Related Subjects

55 BIOLOGY AND MEDICINE
BASIC STUDIES
ASPERGILLUS
GENE RECOMBINATION
PHANEROCHAETE
GENES