Chimeric gene construct coding for bi-functional enzyme endowed with endoglucanase and phytase activities

• Published in: Archives of microbiology 2009-02, Vol.191 (2), p.171-175
• Main Authors: Reddy, V. Arunodai, Venu, K, Rao, D. E. C. S, Rao, K. V, Reddy, V. D
• Format: Article
• Language: English
• Subjects: 6-Phytase - chemistry; 6-Phytase - genetics; 6-Phytase - metabolism; Bacillus - enzymology; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Bacteriology; Biochemistry; Biological and medical sciences; Biomedical and Life Sciences; Biotechnology; Cell Biology; Cellulase - chemistry; Cellulase - genetics; Cellulase - metabolism; Cloning; E coli; Ecology; Enzyme Stability; Enzymes; Escherichia coli - genetics; Escherichia coli - metabolism; Feed additives; Feeds; Fundamental and applied biological sciences. Psychology; Gene Expression; Genes; Inclusion Bodies - genetics; Inclusion Bodies - metabolism; Life Sciences; Microbial Ecology; Microbiology; Miscellaneous; Molecular Weight; Peptides; Phosphorus; Poultry; Protein Engineering; Proteins; Recombinant Fusion Proteins - chemistry; Recombinant Fusion Proteins - genetics; Recombinant Fusion Proteins - metabolism; Short Communication
• ISSN: 0302-8933; 1432-072X
• DOI: 10.1007/s00203-008-0437-8

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°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.