Abstract

The extracellular enzyme β-glucosidase, present in a culture filtrate and produced by Aspergillus niger, was concentrated up to 700 times by two-phase partitioning. The two-phase systems were achieved by dissolving dextran and poly(ethylene glycol) in the culture filtrate in such proportions that the lower phase, containing the enzyme, consisted of a very small volume compared with the upper phase. The enzyme had high affinity for the lower phase when the system contained 100 m M KSCN at pH 8.0, and the recoveries of β-glucosidase were in the range of 85–95% with a concentrating factor of 60–720 times. At the same time, the enzyme was purified 2–3 times.

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