Chimeric gene construct coding for bi-functional enzyme endowed with endoglucanase and phytase activities.
Phytase and endoglucanase enzymes are being widely used as feed additives in poultry industry. In our earlier studies, the Bacillus phytase, when expressed in Escherichia coli, was found in inclusion bodies, whereas endoglucanase was found in active soluble form. Herein, we report the development of a chimeric gene construct coding for ~73 kDa fusion protein and its over-expression in E. coli in soluble form. The novel enzyme exhibited both endoglucanase and phytase activities across broad pH (4.0-8.0) and temperature (25-75 degrees C) ranges. As such, the bi-functional enzyme seems promising and might serve as a potential feed additive for enhanced nutrition uptake in monogastric animals.
Reddy
V Arunodai
VA
Centre for Plant Molecular Biology, Osmania University, Hyderabad, 500 007, India. vdreddycpmb@yahoo.com
Venu
K
K
Rao
D E C S
DE
Rao
K V
KV
Reddy
V D
VD
D010832:6-Phytase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001407:Bacillus / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002480:Cellulase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004795:Enzyme Stability; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D015870:Gene Expression; D002479:Inclusion Bodies / Q000235:genetics / Q000378:metabolism; D008970:Molecular Weight; D015202:Protein Engineering; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D001426:Bacterial Proteins; D011993:Recombinant Fusion Proteins; D010832:6-Phytase; D002480:Cellulase