Abstract

Studies were made on the action of alginase obtained from liver of abalone, Haliotis discus hannai Ino, on alginic acid. This enzyme splits alginic acid into products that showed a strong ultraviolet absorbancy at approximately 235mμ owing to their α, β-unsaturated carboxylic group. Alginase activity was determined by measuring the absorbancy at 235mμ. The maximum activity was obtained at the pH range of 7.0 to 7.5 and at the temperature of 30°C (Fig. 2). Sodium chloride had no effect on alginase activity, in concentrations below 0.1% but rather inhibitory effect in higher concentrations than 1% (Table 1). Parallel changes in reducing power and ultraviloet absorbancy of the solution indicate that the glycosidic linkage of alginic acid is hydrolyzed dehydratively. It was thus concluded that oligouronides containing 4, 5-unsaturated bond are formed. The pattern of alginic acid decomposition described in this study appears to be closely analogus to the eliminative decomposition of pectic acid and of polygalacturonic acid rather than to that of pectin.

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