Optimization strategy for purification and isolation of active lectin from Colocasia esculenta L. Schott rhizome
Colocasia esculenta
Isolation
DOI:
10.7324/jabb.2024.173070
Publication Date:
2024-02-28T11:07:31Z
AUTHORS (5)
ABSTRACT
Lectins are non-enzymatic proteins that attach to carbohydrates and exhibit diverse biological activities found in Colocasia esculenta rhizomes. This study determined the optimal conditions for purifying isolating lectin from C. rhizome. The methods involved preparation of crude extracts with variations salting in, followed by out, precipitation phosphate buffer saline (PBS), then all were analyzed sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Purification isolation carried out using ion exchange chromatography pH 8.3, 7.2, 9.6. isolates evaluated bicinchoninic acid method, SDS-PAGE, hemagglutination test. results SDS-PAGE showed best extraction method use PBS as indicated presence a prominent band at ~12.5kDa. During optimization purification, isolate was obtained observed appearance single ~12.5kDa MW on 12% occurrence an agglutination reaction stage. total protein content lectins ranged 1284.83 2947.33 μg/mL. rhizome contains active compounds. condition is solvent purification
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