タンニンをリガンドとするたんぱく質吸着体による清酒のたんぱく混濁母物質の除去 ; 基礎的検討

概要

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Fresh sake is pasteurized at 55-65℃ for 15 min. This process usually produces turbidity in the stored sake. The soluble proteins in the sake derived from rice-koji during fermentaiton (protein turbid precursors) form insoluble materials (protein turbid matters) when denatured by heat and gradually grow to large particles, giving the sake a slight turbidity. These particles are too small to be removed by ordinary filtration.In this paper, adsorption of the protein turbid precursors from sake onto an immobilized tannin packed in a column was examined. An adsorbent prepared by coupling the BrCN-activated gallotannin to aminohexylcellulose was found to be most effective. Analysis of sake components and sensory evaluation revealed no quality change in the treated sake. The elution pattern of the adsorbed substances from the adsorbent with 0.01 N HCl showed 3 peaks, of which the 2nd contained α-amylase, glucoamylase, and acid protease. Glucoamylase in sake was adsorbed onto the adsorbent at 850 units/ml adsorbent (wet), which was comparable to 50-100 ml sake/ml. A sake was continuously treated with the adsorbent and fractionated into a fixed volume. Residual glucoamylase in the fraction and the turbidity appearing after pasteurization of the sake correlated well.
公益社団法人日本生物工学会の論文
1977-11-25