利用AB-8大孔树脂为载体，戊二醛为交联剂对溶菌酶进行固定化，研究固定化酶的制备条件、酶学性质、微观结构及抑菌效果。结果表明：固定化时问4h、固定化温度25℃、戊二醛质量浓度0．3g／100mL、m酶：m载体=1：200时固定化溶菌酶的相对酶活力最高；与游离酶相比，溶菌酶经过固定化后耐热性提高、耐酸性增强，米氏方程分析表明，溶菌酶经过固定化后与底物壳聚糖的亲和力下降，固定化酶重复使用5次时，酶活力残留率为57．6％，抑菌实验结果表明，固定化溶菌酶对纯牛奶具有较好的抑菌效果。%AB-8 macroporous resin was used as a carrier to immobilize lysozyme by glutaraldehyde cross-linking. The preparation conditions, enzymatic characteristics, microstructure and antimicrobial efficacy of immobilized lysozyme were explored. Immobilized lysozyme prepared by 4 h immobilization at 25 ℃, an enzyme-to-carrier ratio of 1：200 and a glutaralde- hyde concentration of 0.3 g/100 mL presented the highest relative activity. The immobilized lysozyme showed significant improvements over free lysozyme in heat and acid tolerance. Trough a comparative analysis of their Michaelis Menten Equations, we found that immobilization resulted in a decrease in the affinity of lysozyme with chitosan, the substrate. After fifth repeated use, the immobilized lysozyme retained 57.6% of its original activity. The immobilized enzyme had good antimicrobial effect on pure milk.
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