A freshwater green microalgal strain was isolated and the lectin was identified in it by a strong hemagglutination activity (HA) assay. Characterization of the algal strain was found to be (MW769776). A single step affinity chromatographic technique was developed to purify lectin (CSL) using guar gum as the affinity matrix. The precipitate showed a single active peak with a titer value of 1024 HU, with a concentration of 1111 U, and a purification fold of 9. The purified protein exhibited a single band in SDS-PAGE with a molecular weight of 16 kDa. Analysis by liquid chromatography-electrospray ionization-quadrupole-time of flight mass spectrometry (LC-ESI-Q-TOF-MS) of tryptic-digested purified lectin showed that it was a monomeric protein. A multiple sequence alignment analysis revealed that the peptide sequences of CSL exhibited similarity with the H-type lectin domain of . The structure of CSL was studied by FTIR and homology modeling methods, indicating the presence of -helix as well as -sheet in its secondary structure. Whereas the 3D structure exhibited the similarity with the core protein of light-harvesting reaction center complex of photosystem I. The significance of this study suggests that the characteristics of CSL are consistent with its identification as a hemagglutinin, a type of novel lectin, which suggests its candidature for various biological purposes.Communicated by Ramaswamy H. Sarma.
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