PARTIAL PURIFICATION AND CHARACTERIZATION OF A NEWLY IDENTIFIED LECTIN-LIKE PROTEIN FROM ELEUSINE CORACANA (FINGER MILLET) SEEDS
DOI:
https://doi.org/10.55766/sujst11850Keywords:
Eleusine coracana seed, Lectin, Hemagglutination activity, Partial purification, CharacterizationAbstract
Lectins are carbohydrate-binding proteins with significant biological activities, including antimicrobial, anticancer, and antioxidant properties. Eleusine coracana (finger millet), a nutritionally rich cereal traditionally valued in India, has not been extensively explored for lectin properties. This study aimed to partially purify and characterize a lectin-like protein from Eleusine coracana seeds, with a focus on its hemagglutination activity, pH - temperature stability, sugar specificity, effects of metal ions and EDTA. Lectin partial purification was performed using ammonium sulphate precipitation followed by dialysis, yielding a protein concentration of 1 mg/mL. Hemagglutination assays revealed highest activity toward human blood group A+. The lectin was active within a pH range of 5-9, with maximum stability at pH 6-7, and retained high activity between 20-50 °C, with thermal stability up to 70°C. Sugar specificity assays showed mild hemagglutination inhibition by galactose. EDTA completely abolished hemagglutination activity, while Ca²⁺, Zn²⁺, and Mg²⁺ enhanced its activity, suggesting lectin’s metal dependence. These results demonstrate presence of lectin with distinct stability and characteristics in Eleusine coracana seeds, providing a foundation for further purification, characterization and exploration of its potential biomedical and nutraceutical applications.
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