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Cross-linkedα-amylase aggregates on Fe3O4 magnetic nanoparticles modified with polydopamine/polyethyleneimine for efficient hydrolysis of starch
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作者 Jiandong Cui Xiuming Tang +3 位作者 Qingqing Ma Yuyan Chang Qunli Zhang Shiru Jia 《Particuology》 SCIE EI CAS CSCD 2024年第7期98-105,共8页
In this workα-amylase was immobilized on magnetic Fe3O4 nanoparticles with polyethylenimine(PEI)/polydopamine(PDA)coating or 3-aminopropyl triethoxysilane(APTES)for the first time via adsorption–precipitation–cross... In this workα-amylase was immobilized on magnetic Fe3O4 nanoparticles with polyethylenimine(PEI)/polydopamine(PDA)coating or 3-aminopropyl triethoxysilane(APTES)for the first time via adsorption–precipitation–cross-linking.Compared with the freeα-amylase,the resultant magnetic cross-linkedα-amylase aggregates(PEI/PDA-M-CLEAs and N-M-CLEAs)exhibited excellent thermal and storage stability as well as pH stability.After storage at 25°C for 60 days,freeα-amylase only retained 60%of its initial activity,while PEI/PDA-M-CLEAs and N-M-CLEAs retained 80%and 78%of their initial activities,respectively.Furthermore,N-M-CLEAs and PEI/PDA-M-CLEAs showed good reusability.After 6 repeated uses,PEI/PDA-M-CLEAs and N-M-CLEAs still maintained 65%and 62%of their initial activities,respectively.Especially,PEI/PDA-M-CLEAs and N-M-CLEAs exhibited higher starch hydrolysis efficiency than freeα-amylase.The maximum dextrose equivalent(DE)values of starch hydrolysis by PEI/PDA-M-CLEAs and N-M-CLEAs reached 29.24%and 28.79%within 90 min,respectively.However,the maximum DE values of starch hydrolysis by the freeα-amylase was only 27.89%even in 150 min.The magnetic cross-linkedα-amylase aggregates could be introduced as effective biocatalyst for industrial applications in production of maltose syrups. 展开更多
关键词 Α-AMYLASE magnetic nanoparticles Functional modification magnetic cross-linked enzyme aggregates Hydrolysis of starch
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磁性交联核酸酶P1聚集体的制备及性质研究 被引量:8
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作者 邵卫祥 莫晓燕 李黎 《西安交通大学学报》 EI CAS CSCD 北大核心 2008年第8期1035-1039,共5页
采用磁性纳米颗粒与酶蛋白共沉淀后经戊二醛交联的方法,制备了磁性交联核酸酶P1聚集体,并且对比分析了游离酶和固定化酶的部分酶学性质.优化的最佳制备条件为:硫酸铵质量浓度为0.8 g/mL,沉淀时间为0.5 h,戊二醛体积分数为0.6%,交联时间... 采用磁性纳米颗粒与酶蛋白共沉淀后经戊二醛交联的方法,制备了磁性交联核酸酶P1聚集体,并且对比分析了游离酶和固定化酶的部分酶学性质.优化的最佳制备条件为:硫酸铵质量浓度为0.8 g/mL,沉淀时间为0.5 h,戊二醛体积分数为0.6%,交联时间为2 h,所制得的固定化酶活性回收率为32.4%.酶学性质研究表明,固定化酶的Km值(30.7 mmol/L)明显高于游离酶的(7.27 mmol/L),二者最适反应温度分别为90℃和75℃,最适pH值均为5.2,固定化核酸酶P1对热和酸碱的耐受性明显增强,连续反应6次后酶活力仍保留70%,良好的操作稳定性和磁响应性有利于核酸酶P1的工业化应用. 展开更多
关键词 核酸酶P1 交联酶聚集体 磁性纳米颗粒 酶学性质
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