Related Experiment Video
Updated: Jul 19, 2026
11:31
'Bioluminescent' Reporter Phage for the Detection of Category A Bacterial Pathogens
Published on: July 8, 2011
A novel phytase with preferable characteristics from Yersinia intermedia
Huoqing Huang1, Huiying Luo, Peilong Yang
1Department of Microbial Engineering, Feed Research Institute, Chinese Academy of Agricultural Sciences, PR China.
Biochemical and Biophysical Research Communications
|October 13, 2006
Summary
Researchers discovered a novel phytase enzyme from Yersinia intermedia, a bacterium found in glacier soil. This enzyme exhibits high activity and stability, suggesting its potential use in the animal feed industry.
Area of Science:
- Microbiology
- Enzymology
- Biotechnology
Background:
- Phytases are crucial enzymes for breaking down phytate, an anti-nutritional factor in plant-based animal feeds.
- Identifying novel phytases with enhanced properties is essential for improving feed efficiency and sustainability.
- Yersinia intermedia is a bacterial species, and its potential for producing valuable enzymes like phytase has not been extensively explored.
Purpose of the Study:
- To isolate and characterize a novel phytase enzyme from a Yersinia intermedia strain.
- To clone, overexpress, and purify the phytase gene (appA) and its corresponding protein (APPA).
- To evaluate the biochemical properties and potential industrial applications of the recombinant APPA.
Main Methods:
- Isolation of Yersinia intermedia strain from glacier soil.
- Cloning of the phytase gene (appA) using degenerate PCR and TAIL-PCR.
- Overexpression of the recombinant phytase (APPA) in Pichia pastoris.
- Purification and biochemical characterization of the recombinant APPA, including activity assays, pH/temperature optima, and stability tests.
Main Results:
- A Yersinia intermedia strain producing phytase activity was identified.
- The full-length phytase gene (appA) was cloned and sequenced, revealing a 441-amino acid protein (APPA) with conserved active site motifs.
- Recombinant APPA exhibited high specific activity (3960 U/mg) for sodium phytate, surpassing previously known phytases.
- The enzyme demonstrated broad pH activity (optimum 4.5), a high optimal temperature (55°C), and resistance to pepsin and trypsin.
Conclusions:
- This study reports the first detection of phytase activity and cloning of the appA gene from Yersinia intermedia.
- The characterized recombinant APPA possesses superior specific activity and favorable enzymatic properties compared to existing phytases.
- The robust characteristics of APPA suggest its significant potential for application in the animal feed industry to improve nutrient bioavailability.
Related Concept Videos
01:24Plague
Plague is a highly virulent zoonotic disease caused by Yersinia pestis, a Gram-negative, facultatively anaerobic coccobacillus. This pathogen primarily circulates among rodent populations and is transmitted to humans through the bite of infected fleas. Additional transmission routes include direct contact with infected animal tissue or inhalation of respiratory droplets from individuals with pneumonic plague. These multiple transmission pathways highlight the bacterium’s potential for rapid...
01:30Production of Pharmaceuticals
Industrial insulin production uses genetically engineered E. coli expressing a proinsulin gene controlled by a tryptophan promoter and containing a methionine linker for later cleavage. The cells also carry ampicillin resistance for selective growth. Seed cultures are stored at −80 °C and production begins by thawing a small amount to inoculate starter cultures, which are progressively scaled to a 50,000-L bioreactor. In the bioreactor, E. coli grow in nutrient-rich media under sterile, tightly...