Purification and Characterization of Glucose Dehydrogenase from a Heterotrophically Grown Blue-Green Alga

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Abstract
NADP- and NAD-dependent glucose dehydrogenase was partially purified from a dark-grown blue-green alga (endophytic Nostoc strain MAC). Polacrylamide gel electrophoresis established that a single protein possessed dual activity for either NADP or NAD. No other electron acceptor substituted for pyridine nucleotides, and no evidence for a flavine prosthetic group was found. Although the Km for NADP was 8.8 .mu.M and for NAD 328 .mu.M, the enzyme was equally active with NAD or NADP at saturating levels of substrates. The enzyme was similar to previously described glucose dehydrogenase in that it had a high Km for glucose (18-20 mM at 35.degree. C) and an alkaline pH optimum of 7.6-9.4.

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