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磁性生物活性玻璃共固定葡萄糖氧化酶-过氧化氢酶的研究 被引量:4

Co-immobilization of Glucose Oxidase and Catalase on Magnetic Mesoporous Bioactive Glasses
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摘要 生物活性玻璃具有良好的生物相容性和生物活性,利用其进行酶的固定化是一种新的实验理念。本文对生物活性玻璃进行改性,加入一定量乙二醇利用溶胶-凝胶的方法制备了表面具一定磁性的磁性生物活性玻璃微球,并利用该微球对葡萄糖氧化酶和过氧化氢酶进行固定。实验表明,同时固定两种酶比单独固定效果更为显著。之后将GOD-CAT以一定的比例分别在传统水相和有机相二恶烷中进行共固定化,比较水相共固定化酶和有机相共固定化酶的酶比活力和酶学性质,找到了最佳的固定介质。实验表明,戊二醛浓度为0.4%,加酶活力比GOD:CAT为1:2,二恶烷含水量1.5%时,GOD的表观酶活回收率达到90.25%;而传统水相中,GOD的表观酶活回收率最大仅为72.18%。连续使用10次后,有机相固定化酶活为初始值的67.30%,而传统水相中酶活仅为初始值的44.33%。 Due to the biocompatibility and bioactivity, bioactive glasses is consider as a new type of carrier for enzymes immobilization. In this paper, the bioactive glasses was modified to be magnetic using the sol-gel approach and polyethylene glycol (PEG) and was used to immobilize glucose oxidase and catalase. Co-immobilization was much more better than individual immobilization of the two enzymes. The special activities and enzyme characterization were determined and the best medium was selected. Under the conditions of 0.4% glutaraldehyde, 1.5% moisture, and glucose oxidase:catalase of 1:2, the enzyme recovery of glucose oxidase reached 92.25%. In aqueous phase, the maximum enzyme recovery was only 72.18%. After 10 repeated use, the residue activities of the immobilized enzyme in organic solvent and aqueous phase were 67.30% and 44.33%, respectively.
出处 《现代食品科技》 EI CAS 北大核心 2013年第9期2180-2185,2130,共7页 Modern Food Science and Technology
基金 国家高技术研究发展计划(863计划)(SQ2010AA0222655001)
关键词 葡萄糖氧化酶 过氧化氢酶 共固定 相对酶活 glucose oxidase catalase co-immobilization relative enzyme
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参考文献9

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共引文献19

同被引文献44

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