Immobilisation of α-L-rhamnosidase of <i>Aspergillus terreus </i>on bagasse particles based matrix

Abstract

α-L-rhamnosidase from <i>Aspergillus terreus </i>has been immobilised on bagasse particles based matrix. <i>K</i>_m, <i>p</i>H<i> </i>and temperature optima of the immobilized enzyme using narigin as the substrate have been found to be 0.24 mM, 4.0 and 55°C respectively. The corresponding values for the same enzyme in the solution phase are 0.16 mM, 4.0 and 55°C respectively.

The immobilized preparation of α-L-rhamnosidase hydrolyses naringin present in Citrus sinansis juice indicating its applicability in the debittering of citrus fruit juices.