Basri M, Ampon K, Yunus W M, Razak C N, Salleh A B
Fakulti Sains & Pengajian Alam Sekitar, Universiti Pertanian Malaysia, Serdang.
J Chem Technol Biotechnol. 1994 Jan;59(1):37-44. doi: 10.1002/jctb.280590107.
A simple and effective method of lipase immobilization is described. Lipase from Candida rugosa was first modified with several hydrophobic modifiers before being adsorbed on to organic polymer beads. The soluble hydrophobic lipase derivatives adsorbed more strongly on to the various polymers as compared with the native lipase. The optimal adsorption temperature of the native and modified lipases on all the polymers was 40 degrees C. The optimal pH of adsorption was between 6 and 7. Lipase immobilized in this manner produced high catalytic recoveries which are affected by the type of modifiers, degree of modification and type of supports used. Monomethoxypolyethylene glycol (1900) activated with p-nitrophenyl chloroformate was found to be the best modifier of the enzyme at 95% modification, for adsorption to the polymers. Increasing the degree of modification of the enzyme increased the activity which was immobilized. Generally, both native and hydrophobic lipase derivatives showed higher specific activities when immobilized on polar polymers compared with non-polar polymers.
描述了一种简单有效的脂肪酶固定化方法。皱落假丝酵母脂肪酶在吸附到有机聚合物珠粒之前，先用几种疏水改性剂进行修饰。与天然脂肪酶相比，可溶性疏水脂肪酶衍生物在各种聚合物上的吸附更强。天然脂肪酶和改性脂肪酶在所有聚合物上的最佳吸附温度为40℃。吸附的最佳pH值在6至7之间。以这种方式固定的脂肪酶产生高催化回收率，这受到改性剂类型、改性程度和所用载体类型的影响。发现用对硝基苯基氯甲酸酯活化的单甲氧基聚乙二醇（1900）在95%改性时是该酶用于吸附到聚合物上的最佳改性剂。酶改性程度的增加提高了固定化酶的活性。一般来说，与非极性聚合物相比，天然和疏水脂肪酶衍生物固定在极性聚合物上时都表现出更高的比活性。
