机构地区: 广西大学化学化工学院
出 处: 《高校化学工程学报》 2013年第5期836-841,共6页
摘 要: 为了探索定向制备蓝圆鲹蛋白活性多肽的工艺条件,进行了酶解体系的动力学研究。蓝圆鲹蛋白经碱性蛋白酶在一定条件下作用可得到活性多肽。采用pH-stat法建立了蓝圆鲹蛋白-碱性蛋白酶酶解体系的酶解反应动力学模型。利用高效体积排阻色谱分析了不同水解度下酶解产物中多肽片段族分子量的分布,并采用3-D图形表达了酶解过程中水解度-多肽片段族分子量-质量百分数之间的变化关系,经Matlab数学拟合得到了酶解过程中多肽片段族组分百分数与水解度和分子量的关系。验证实验表明,建立的3-D动力学模型与实际水解过程基本吻合,该模型揭示了酶解过程中多肽分子量组成的变化规律,可对酶解体系进行实时定量分析和动态表征,此酶解过程动力学研究也有利于定量获得定向目标产物。 In order to find out the process condition for preparing the bioactive peptides obtained from Decapterus maruadsi protein, the dynamic model for the Decapterus maruadsi enzymatic system was studied. Alkaline protease was used to hydrolyze Decapterus maruadsi protein which forms complicated active peptides consequently. The dynamic model for enzymolysis of Decapterus maruadsi protein---alkaline protease system was obtained via the pH-stat method. The molecular weight distribution of the polypeptide fragments under the different degrees of hydrolysis (DH) in the hydrolysate of Decapterus maruadsi protein was analyzed by high performance size exclusion chromatography (HPSEC). In terms of chromatograms obtained at different DH values, a 3-D continuous surface and corresponding contour were plotted to characterize the relation of DH - polypeptide fragment molecular weight - mass percent in the enzymatic process. Mass percentages of polypeptide fragments at the different molecular weights and DH values were established with Matlab simulation. Results show that the 3-D dynamic model is basically consistent with the real hydrolysis. This model has revealed the composition variation with polypeptide molecular weights in the enzymolysis and may be used to conduct the real-time quantitative analysis and the dynamic attribute of the enzymolysis system. It is also beneficial to the directional and quantitative preparation of target active peptides.
领 域: [化学工程]