Immobilization of Alkaline Protease on Amino-Functionalized Magnetic Nanoparticles and Its Efficient Use for Preparation of Oat Polypeptides
Immobilization of Alkaline Protease on Amino-Functionalized Magnetic Nanoparticles and Its Efficient Use for Preparation of Oat Polypeptides
复制标题
氨基功能化磁性纳米粒子上碱性蛋白酶的固定化及其在燕麦多肽制备中的高效应用
DOI：
10.1021/ie504691j
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发表时间：
2015
影响因子：
4.2
通讯作者：
Zong Minhua
中科院分区：
文献类型：
--
作者：
Hu Tenggen;Cheng Jianhua;Zhang Bobo;Lou Wenyong;Zong Minhua
碱性蛋白酶被成功地固定到氨基功能化的Fe 3 O 4纳米粒子。酶的载量为388.2mg蛋白/g载体，酶活力回收率大于54.2%。固定化后碱性蛋白酶对底物的亲和力和稳定性显著提高。固定化酶重复使用10次后仍保持其初始活力的50.1%，具有良好的操作稳定性。该固定化酶能够高效催化水解燕麦麸制备燕麦多肽。在优化条件下，燕麦多肽（8.4mg/mL）对DPPH自由基的最大清除率（抗氧化活性）为82.3%，远高于文献报道的结果。此外，固定化酶制备的燕麦多肽比游离酶制备的燕麦多肽具有更高的抗氧化活性，这是由于燕麦多肽中相对疏水性组分的增加。此外，该固定化酶还具有良好的应用前景。
Alkaline protease was successfully immobilized onto amino-functionalized Fe3O4 nanoparticles. The enzyme loading was 388.2 mg of protein/g of support and the activity recovery was more than 54.2%. After immobilization, the affinity of alkaline protease toward substrate and its stability were significantly enhanced. The immobilized enzyme still retained 50.1% of its initial activity after 10 cycles of successive reuse, exhibiting excellent operational stability. The immobilized enzyme was capable of efficiently catalyzing hydrolysis of oat bran into oat polypeptides. Under the optimized conditions, the maximum DPPH radical scavenging rate (antioxidant activity) of oat polypeptides (8.4 mg/mL) was 82.3%, which was much higher than the reported result. Moreover, the prepared oat polypeptides by immobilized enzyme showed higher antioxidant activity than those prepared by free enzyme, owing to an increase of relatively hydrophobic components of oat polypeptides. Furthermore, the immobilized enzyme was demonstr...