SOLVENT EFFECT ON KINETICS OF HYDROLYSIS OF RAFFINOSE CATALYZED BY INVERTASE

Invertase shows an increased activity in aquo-polyhydric media than in the aqueous media. Invertase activity increases by 44% in 0.2M sorbit ol solution than that in aqueous media. The effect of various concentr ations of structurally similar polyols viz, ethylene glycol, glycerol, erythritol and sorbitol on the kinetics of invertase catalysed hydrol ysis of raffinose have been investigated. Activity of invertase increa ses with increase in length of carbon chain of polyols upto 0.2M conce ntration of polyols and decreases with further increase in polyols con centration. Thermal stability of the enzyme increases with the concent ration increase as well as with increase in number of hydroxyl groups per polyol molecule. Substrate specificity of invertase in aquo-polyol ic media has not been altered.