• A galactomannan-hydrolysing α-galactosidase from jack fruit (Artocarpus integrifolia) seed: Affinity chromatographic purification and properties

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    • Keywords


      α-Galactosidase; galactomannan; jack fruit seed; Artocarpus integrifolia

    • Abstract


      An acid α-galactosidase from the seeds of the jack fruit seed (Artocarpus integrifolia) has been purified to homogeneity by affinity chromatography on a matrix formed by cross-linking the soluble α-galactose-bearing guar seed galactomannan. The 35kDa enzyme was a homotetramer of 9.5kDa subunits. Its carbohydrate part (5.5%) was composed of galactose and arabinose. TheKm withp-nitrophenyl α-D-galactoside as substrate was 0.35 mM. TheKi values indicated inhibition by galactose, 1-O-methyl α-galactose and melibiose in the decreasing order. Among α-galactosides, the enzyme liberated galactose from melibiose, but not from raffinose or stachyose at its pH optimum (5.2). The guar seed galactomannan was however efficiently degalactosidated; limited enzyme treatment abolished the precipitability of the polysaccharide by the α-galactose-specific jack fruit seed lectin, and complete hydrolysis yielded insoluble polysaccharide. Though similar in sugar specificity and subunit assembly, α-galactosidase and the lectin coexisting in the jack fruit seed gave no indication of immunological identity.

    • Author Affiliations


      P S Appukuttan1 Debkumar Basu1

      1. Neurochemistry Division, Sree Chitra Tirunal Institute for Medical Sciences and Technology, Trivandrum - 695 011, India
    • Dates

  • Journal of Biosciences | News

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      Posted on July 25, 2019

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