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系统研究了由正庚烷、水、琥珀酸二辛酯磺酸钠 (AOT)所构成的油包水微乳液的百分组成、pH值、[H2 O]/[AOT]的比值 (ω0 )等对以此微乳液为基底的明胶固定化脂肪酶的活性及机械强度的影响 ,制备出了具有超高活性的微乳液凝胶固定化脂肪酶。此外 ,还对固定化酶的一些酶学特征进行了初步表征。最佳酶活对应的pH为 7 17,ω0 为 16左右。在恒定ω0 值下 ,酶活随AOT百分比的增加而提高 ,但机械强度正好相反。酶以酶粉形式直接加入微乳液中所得固定化酶的活性要比酶以酶液形式加入到AOT的正庚烷中所得的活性要高。微乳液凝胶固定化脂肪酶的活力大约是水固定化酶的 10倍 ,且在 4℃下其活性半个月内无明显变化。对中长链的脂肪醇或酸同系物 ,该固定化酶所显示出的底物选择性差异不大。
The percent composition of the water-in-oil microemulsion composed of n-heptane, water and sodium dioctylsulfosuccinate (AOT), the pH, the ratio of [H2O] / [AOT] And so on the microemulsion-based gelatin immobilized lipase activity and mechanical strength, prepared with ultra-high activity of microemulsion gel-immobilized lipase. In addition, some enzymatic characteristics of immobilized enzyme were also preliminarily characterized. The optimal pH value for the enzyme activity was 7 17 and ω 0 was about 16. At a constant ω0 value, the enzyme activity increased with increasing AOT percentage, but the mechanical strength was the opposite. The activity of the immobilized enzyme obtained by directly adding the enzyme in the form of enzyme powder to the microemulsion is higher than that obtained when the enzyme is added as an enzyme solution to the n-heptane of AOT. Microemulsion gel-immobilized lipase is approximately 10-fold more active than water-immobilized enzyme and exhibits no significant change in activity for half a month at 4 ° C. For medium and long chain fatty alcohols or acid homologues, the immobilized enzyme showed little difference in substrate selectivity.