Lee D D, Lee Y Y, Reilly P J, Collins E V, Tsao G T
Biotechnol Bioeng. 1976 Feb;18(2):253-67. doi: 10.1002/bit.260180210.
Glucoamylase was immobilized to porous silica and its kinetics and stability were observed with acid- and alpha-amylase-hydrolyzed dextrin as feed. The enzyme was found to be extremely stable in both laboratory and pilot plant operations. When the feed had been previously only lightly hydrolyzed, pore diffusion limitation caused appreciable decreases in glucose production rate. The severity of starch hydrolysis to dextrin markedly affected ultimate glucose yields. The diffusional gradients present in the carrier pores caused the immobilized enzyme to yield lower glucose concentrations than the free enzyme at similar feed conditions.
将糖化酶固定在多孔硅胶上，并以酸水解和α-淀粉酶水解的糊精为原料观察其动力学和稳定性。发现在实验室和中试工厂操作中该酶都极其稳定。当原料之前仅轻度水解时，孔扩散限制导致葡萄糖产率显著下降。淀粉水解为糊精的程度显著影响最终的葡萄糖产率。载体孔中存在的扩散梯度导致固定化酶在类似的进料条件下产生的葡萄糖浓度低于游离酶。
