动态高压微射流诱导的去折叠胰蛋白酶结构预测  

Prediction and simulating of the conformation of unfolded trypsin induced by dynamic high-pressure microfluidization

作　　者：张兆琴[1,1] 刘伟[1] 刘军平[1] 邹立强[1] 刘成梅[1] 

机构地区：[1]南昌大学食品科学与技术国家重点实验室,江西南昌330047

出　　处：《食品工业科技》2013年第7期102-105,共4页Science and Technology of Food Industry

基　　金：国家自然科学基金(31060209);国家重点实验室重点青年基金(SKLF-QN-201101);江西省青年科学家培养对象计划(20112BCB23003)

摘　　要：采用差示扫描量热法和圆二色谱分析了动态高压微射流处理前后胰蛋白酶结构的变化,结合前期研究中动态高压微射流诱导的去折叠胰蛋白酶构象的表征,通过PyMOL、3DSMax等软件分别对天然胰蛋白酶和动态高压微射流诱导的去折叠胰蛋白酶的三维空间构象进行模拟和预测,结果表明:与天然胰蛋白酶相比,动态高压微射流处理后胰蛋白酶热焓降低,二级结构构象单元百分含量发生变化,去折叠胰蛋白酶结构更加松散。模拟的胰蛋白酶分子构象示意图更直观地显示了胰蛋白酶的活性中心、二硫键以及二级结构信息,对动态高压微射流诱导的去折叠胰蛋白酶三维结构模型变化做一初探。Differential scanning calorimetry and circular dichroism were used to analyze the conformational change of trypsin induced by dynamic high-pressure microfluidization（DHPM）. Based on the reflection in conformational change of the unfolding trypsin induced by DHPM in our previous study,the conformation of native and unfolding trypsin was predicted and modeled by PyMOL and 3DS Max.The results indicated that compared with native trypsin,the decrease in thermal enthalpy and the change of percentages of secondary structural elements, the loose structure of unfolding trypsin was found. The active center, disulfide bond and the secondary structural information of trypsin was visually viewed by the modeled conformation figure.In addition, preliminary study on the structural modeling change of DHPM-induced unfolding trypsin was completed.

关 键 词：胰蛋白酶 动态高压微射流 去折叠 结构预测 

分 类 号：TS201.2[轻工技术与工程—食品科学]