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Alkaline phytase from Lilium longiflorum: purification and structural characterization
Barry G Garchow1, Sonali P Jog, Bakul Dhagat Mehta
1Department of Chemistry, Michigan Technological University, Houghton, MI 49931, USA.
Protein Expression and Purification
|October 4, 2005
Summary
This study reports the first purification of alkaline phytase from plant sources, specifically Lilium longiflorum pollen. This enzyme shows potential for use as a feed and food supplement due to its unique properties.
Area of Science:
- Biochemistry
- Enzymology
- Plant Science
Background:
- Phytases are crucial enzymes that hydrolyze phytic acid, important in food and animal feed industries.
- While acid phytases are well-studied, alkaline phytases from plants remain largely uncharacterized.
- Limited information exists on the purification and structural properties of plant-derived alkaline phytases.
Purpose of the Study:
- To describe the purification of alkaline phytase from plant tissue.
- To characterize the structural properties of this novel alkaline phytase.
- To assess its potential as a commercial supplement.
Main Methods:
- Purification involved selective precipitation (heat, ammonium sulfate), anion exchange, chromatofocusing, and gel electrophoresis.
- Molecular mass was determined using Ferguson plot analysis and SDS-PAGE.
- Isoform analysis was performed using 2-D gel electrophoresis and MALDI-TOF mass spectrometry.
Main Results:
- Alkaline phytase was purified approximately 3000-fold from Lilium longiflorum pollen with 4.2% recovery.
- The enzyme is a homodimer with a native molecular mass of ~118 kDa and subunit mass of 52-55 kDa.
- Multiple isoforms with pI values ranging from 7.3 to 8.3 were identified.
Conclusions:
- This is the first report of purified alkaline phytase from a plant source.
- The enzyme exhibits unique properties suggesting its utility in feed and food applications.
- Further research into its catalytic and structural characteristics is warranted.
