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Abstract
Guucoamylase was immobilized by amidination reaction on the granular polyacrilonitrile resin which had been preliminarily treated with dry HCl in methanol. The granular polyacrilonitrile resin was made by drop-wise addition of the dimethylf ormamide solution of polyacrilonitrile to methanol. Continuous hydrolysis of soluble starch was operated in a column which was packed with the immobilized glucoamylase (granularity : 1 mmφ). Estimated values of apparent MICHAELIS constant (Km) with the immobilized glucoamylase depended on flow rates in the column and were found to be higher than that with the native glucoamylase in the batch system. The immobilized glucoamylase column was connected in a series with a column of the immobilized a-amylase (granularity : 30-200 μmφ). And, a soluble starch solution was firstly passed through the immobilized α-amylase column and then through the immobilized glucoamylase column. The effect of the pretreatment of soluble starch in the immobilized α-amylase column on the rate of hydrolysis was recognized with regard to the balance between amount of immobilized α-amylase and the degree of the hydrolysis in terms of reducing sugar unit. A similar effect was observed in the pretreatment of soluble starch with native α-amylase in a batch system. The molecular weight distribution of the reaction product of α-amylase processing was analyzed by the gel filtration (Sephadex G-75)method for the higher molecular weight fraction and by the thin layer chromatographic method for the lower molecular weight fraction up to DP 12. On the basis of these results, the pretreatment with α-amylase was thought to be significant particularly in that the effective concentration of the substrate was increased through the fission of the glucoside chains. The endurance test of the immobilized glucoamylase column was pursued by the continuous operation for two weeks with a flow rate of 0.5 ml/min at room temperature and 40°C. Similar situations were referred to in the previous study was obtained.
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