Textile Engineering Dept., University of Minho, Campus Azurém, 4800-058 Guimarães, Portugal.
Biotechnol Prog. 2010 May-Jun;26(3):636-43. doi: 10.1002/btpr.364.
In the present work, we describe for the first time the specific role of cutinase on surface modification of cellulose acetate fibers. Cutinase exhibits acetyl esterase activity on diacetate and triacetate of 0.010 U and 0.007 U, respectively. An increase on the hydroxyl groups at the fiber surface of 25% for diacetate and 317% for triacetate, after a 24 h treatment, is estimated by an indirect assay. Aiming at further improvement of cutinase affinity toward cellulose acetate, chimeric cutinases are genetically engineered by fusing the 3'-end coding sequence with a bacterial or a fungal carbohydrate-binding module and varying the linker DNA sequence. A comparative analysis of these genetic constructions is presented showing that, the superficial regeneration of cellulose hydrophilicity and reactivity on highly substituted cellulose acetates is achieved by chimeric cutinases.
在本工作中，我们首次描述了角质酶在醋酸纤维素纤维表面修饰中的特殊作用。角质酶对二醋酸酯和三醋酸酯的乙酰酯酶活性分别为 0.010 U 和 0.007 U。通过间接测定估计，经 24 小时处理后，二醋酸酯纤维表面的羟基增加了 25%，三醋酸酯纤维表面的羟基增加了 317%。为了进一步提高角质酶对醋酸纤维素的亲和力，通过融合 3'末端编码序列与细菌或真菌碳水化合物结合模块，并改变连接 DNA 序列，对嵌合角质酶进行了基因工程改造。对这些遗传构建体进行了比较分析，结果表明，通过嵌合角质酶实现了高度取代的醋酸纤维素上纤维素亲水性和反应性的表面再生。
