Partial purification of a thermostable dextranase using Sephacryl S-300 adsorption


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Abstract

Thermostable dextranase (1,6-α-D-glucan 6-glucanohydrolysase) from a thermophilic anaerobic bacterium strain Rt364, isolated from a New Zealand hot spring, was partially purified from the cell-free supernatant fluid by adsorption onto Sephacryl S-300, a dextran-based chromatographic resin. It was competitively eluted with 2% T10 dextran, dialysed, concentrated and examined by SDS-PAGE. The overall recovery was 47% and the increase in specific activity by this procedure was 25-fold. The Rt364 dextranase had previously been found to have an optimum temperature of 80°C and hydrolysed both α-1,6 and α-1,4 glucosidic bonds. Sephacryl S-300 adsorption is a simple, useful step with general application for concentrating and purifying bacterial enzymes that hydrolyse dextrans.

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