Boeris Valeria, Romanini Diana, Farruggia Beatriz, Picó Guillemo
Bioseparation Lab. Chemical-Physics Department, Faculty of Biochemical and Pharmaceutical Sciences, CONICET, FonCyT and CIUNR, National University of Rosario, Suipacha 570 (S2002RLK) Rosario, Argentina.
Int J Biol Macromol. 2009 Aug 1;45(2):103-8. doi: 10.1016/j.ijbiomac.2009.04.009. Epub 2009 May 3.
Interactions between catalase and the cationic polyelectrolytes: chitosan and Eudragit E100 have been investigated owing to their scientific and technological importance. These interactions have been characterized by turbidimetry, circular dichroism and fluorescence spectroscopy. It was found that the catalase conformation does not change significantly during the chain entanglements between the protein and the polyelectrolytes. The effects of pH, ionic strength and anions which modify the water structure were evaluated on the polymer-protein complex formation. A net coulombic interaction force between them was found since the insoluble complex formation decreased after the NaCl addition. Both polymers were found to precipitate around 80% of the protein in solution. No modification of the tertiary and secondary protein structure or the enzymatic activity was observed when the precipitate was dissolved by changing the pH of the medium. Chitosan and Eudragit E100 proved to be a useful framework to isolate catalase or proteins with a slightly acid isoelectrical pH by means of precipitation.
过氧化氢酶与阳离子聚电解质壳聚糖和聚丙烯酸树脂E100之间的相互作用因其科学和技术重要性而受到研究。这些相互作用已通过比浊法、圆二色性和荧光光谱进行了表征。结果发现，在蛋白质与聚电解质之间的链缠结过程中，过氧化氢酶的构象没有显著变化。评估了pH、离子强度和改变水结构的阴离子对聚合物-蛋白质复合物形成的影响。由于添加NaCl后不溶性复合物形成减少，因此发现它们之间存在净库仑相互作用力。两种聚合物都能沉淀溶液中约80%的蛋白质。当通过改变介质的pH值使沉淀物溶解时，未观察到蛋白质三级和二级结构或酶活性的改变。壳聚糖和聚丙烯酸树脂E100被证明是通过沉淀分离过氧化氢酶或具有微酸性等电点的蛋白质的有用框架。
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