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Alpha-mannosidase from the seeds of Triticale
A Subha Mahadevi1, R Vegiraju Suryanarayana, N Siva Kumar
1Department of Biochemistry, University of Hyderabad, India.
Journal of Biochemistry, Molecular Biology, and Biophysics : JBMBB : the Official Journal of the Federation of Asian and Oceanian Biochemists and Molecular Biologists (FAOBMB)
|February 20, 2004
Summary
Researchers purified a novel alpha-mannosidase enzyme from Triticale seeds. This cereal alpha-mannosidase shares antigenic similarity with jack bean alpha-mannosidase and has specific biochemical properties.
Area of Science:
- Biochemistry
- Enzymology
- Plant Science
Background:
- Triticale seeds contain lectins and exhibit alpha-mannosidase activity.
- Previous work involved affinity purification of Triticale lectins.
Purpose of the Study:
- To isolate and characterize the alpha-mannosidase enzyme from Triticale seeds.
- To investigate the biochemical and antigenic properties of Triticale alpha-mannosidase.
Main Methods:
- Enzyme isolation using ion exchange, hydrophobic chromatography, and gel filtration.
- Molecular mass determination via Biogel P-200 and SDS-PAGE under reducing conditions.
- Antigenic similarity assessed using antibody cross-reactivity with jack bean alpha-mannosidase.
Main Results:
- Purified Triticale alpha-mannosidase is a glycoprotein (7% carbohydrate) with a native molecular mass of 195 kDa.
- The enzyme dissociates into 58 kDa and 40 kDa subunits under reducing conditions.
- The enzyme demonstrated stability at 50°C, no requirement for metal ions, and phenylalanine as the N-terminal amino acid.
Conclusions:
- Triticale alpha-mannosidase is antigenically similar to its legume counterpart.
- The enzyme possesses distinct biochemical characteristics, including subunit composition and stability.
- This study provides insights into cereal glycosidases and their potential applications.