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Updated: Jun 28, 2026
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Identification of Functional Protein Regions Through Chimeric Protein Construction
Published on: January 8, 2019
Chimeric gene construct coding for bi-functional enzyme endowed with endoglucanase and phytase activities
V Arunodai Reddy1, K Venu, D E C S Rao
1Centre for Plant Molecular Biology, Osmania University, Hyderabad, 500 007, India. vdreddycpmb@yahoo.com
Archives of Microbiology
|November 7, 2008
Summary
Researchers developed a novel bifunctional enzyme with both phytase and endoglucanase activities. This fusion protein, expressed in E. coli, shows promise as a feed additive for improved nutrition in monogastric animals.
Area of Science:
- Biotechnology
- Enzyme Engineering
- Animal Nutrition
Background:
- Phytase and endoglucanase are crucial feed additives in poultry.
- Previous expression of Bacillus phytase in E. coli resulted in inclusion bodies, while endoglucanase remained soluble.
Purpose of the Study:
- To develop a chimeric gene construct for a fusion protein with both phytase and endoglucanase activities.
- To achieve soluble and active over-expression of this bifunctional enzyme in E. coli.
Main Methods:
- Construction of a chimeric gene encoding a ~73 kDa fusion protein.
- Over-expression of the fusion protein in Escherichia coli.
- Characterization of enzyme activity across various pH and temperature conditions.
Main Results:
- The chimeric fusion protein was successfully over-expressed in a soluble form in E. coli.
- The novel enzyme demonstrated both phytase and endoglucanase activities.
- The bifunctional enzyme maintained activity over a broad pH range (4.0-8.0) and temperature range (25-75°C).
Conclusions:
- The developed bifunctional enzyme is a promising candidate for feed additive applications.
- This enzyme could enhance nutrient uptake in monogastric animals.
- Soluble expression of fusion proteins offers advantages over separate enzyme production.
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