Isozymes of Alginate Lyase in the Mid-gut Gland ofTurbo cornutus

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Abstract
Alginate lyase, SP2, from Turbo cornutus was separated on an SP-Sephadex C-50 column from SP1, whose properties have already been reported, and purified according to the method employed for SP1, to obtain information on SP2. The profiles of the optimal pH, pH-stability, thermal inactivation and molecular size of SP2 were entirely the same as those of SP1. The isoelectric point of SP1 and SP2 was 7.5 and 7.7, respectively. The action of SP2 on Alginate caused a rapid decrease in solution viscosity. Analysis of digestion products of alginate with SP2 showed that the enzyme had an affinity toward the mannuronate-rich domains of the alginate molecule and released unsaturated oligomers mostly composed of mannuronic acid as final product. Alginate lyases, SP1 and SP2, were shown to be isozymes in the mid-gut gland of Turbo cornutus.

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