Present work describes the purification of an acidic β-galactosidase from Lens culinaris (Lsbgal) to homogeneity via 857 fold with specific activity of 87 U/mg. The molecular mass of purified Lsbgal was estimated ~ 76 kDa by Size Exclusion Chromatography on Superdex-200 (ÄKTA purifier) and on SDS-PAGE, showed hetero-dimeric subunits i.e.
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