Muzzarelli R A, Barontini G, Rocchetti R
Biotechnol Bioeng. 1976 Oct;18(10):1445-54. doi: 10.1002/bit.260181011.
alpha-Chymotrypsin and acid phosphatase have been immobilized on chitosan, a polyaminosaccharide, without using any intermediate reagent; the immobilized enzymes are active and their activity is much higher than for chitin-immobilized enzymes. The best pH conditions for operating chitosan columns have been determined and columns have been used to transform substrates in large amounts, with no decrease of activity or enzyme losses. Due to the nonconvalent interaction between chitosan and enzymes, the pure and active enzymes can be eventually recovered from the columns. The effects of metal ions, aldehydes, and salts are reported and discussed. Applications are foreseen in the food and biomedical sciences and industries.
α-胰凝乳蛋白酶和酸性磷酸酶已被固定在壳聚糖（一种聚氨基糖）上，无需使用任何中间试剂；固定化酶具有活性，其活性远高于固定在几丁质上的酶。已确定了操作壳聚糖柱的最佳pH条件，并且这些柱已被用于大量转化底物，而酶活性没有降低，也没有酶损失。由于壳聚糖与酶之间的非共价相互作用，最终可以从柱中回收纯的活性酶。报告并讨论了金属离子、醛类和盐类的影响。预计在食品和生物医学科学及行业中会有应用。
