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Synthesis and characterization of PMMA composites activated with starch for immobilization of L-asparaginase

机译：固定化L-天冬酰胺酶的淀粉活化PMMA复合材料的合成与表征

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Poly (methyl methacrylate) (PMMA)-starch composites were prepared by emulsion polymerization technique for L-asparaginase (L-ASNase) immobilization as highly activated support. The hydroxide groups on the prepared composites offer a very simple, mild and firm combination for enzyme immobilization. The pure PMMA and PMMA-starch composites were characterized as structural, thermal and morphological. PMMA-starch composites were found to have better thermal stability and more hydrophilic character than pure PMMA. L-ASNase was immobilized onto PMMA-starch composites contained the different ratio of starch (1, 3, 5, and 10 wt %). Immobilized L-ASNase showed better performance as compared to the native enzyme in terms of thermal stability and pH. K-m value of immobilized enzyme decreased approximately eightfold compared with the native enzyme. In addition to, immobilized L-ASNase was found to retain 60% of activity after 1-month storage period at 4 degrees C. Therefore, PMMA-starch composites can be provided more advantageous in terms of enzymatic affinity, thermal, pH and storage stability as L-ASNase immobilization matrix. (c) 2016 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2016, 133, 43421.
机译：通过乳液聚合技术制备了聚甲基丙烯酸甲酯（PMMA）-淀粉复合物，用于固定L-天冬酰胺酶（L-ASNase）作为高度活化的载体。制备的复合材料上的氢氧基团为酶固定提供了非常简单，温和且牢固的组合。纯PMMA和PMMA淀粉复合材料的结构，热学和形态学特征均得到了表征。发现PMMA-淀粉复合材料比纯PMMA具有更好的热稳定性和更亲水的特性。将L-ASNase固定在含有不同比例淀粉（1、3、5和10 wt％）的PMMA-淀粉复合材料上。与天然酶相比，固定化的L-ASNase在热稳定性和pH方面表现出更好的性能。与天然酶相比，固定化酶的K-m值降低了大约八倍。此外，发现固定化的L-ASNase在4摄氏度下保存1个月后仍保留60％的活性。因此，就酶亲和力，热，pH和储存稳定性而言，PMMA-淀粉复合材料可以提供更多优势。作为L-ASNase固定基质。 （c）2016 Wiley Periodicals，Inc. J. Appl。 Polym。科学2016，133，43421。

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