Covalent immobilization of lipase onto aminopropyl-functionalized hydroxyapatite-encapsulated-γ-Fe2O3 nanoparticles: A magnetic biocatalyst for interesterification of soybean oil

Covalent immobilization of lipase onto aminopropyl-functionalized hydroxyapatite-encapsulated-γ-Fe2O3 nanoparticles: A magnetic biocatalyst for interesterification of soybean oil
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将脂肪酶共价固定在氨丙基功能化羟基磷灰石封装的 γ-Fe2O3 纳米粒子上:用于大豆油酯交换的磁性生物催化剂

DOI:
10.1016/j.foodchem.2017.01.082
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发表时间:
2017-07-15
期刊:
影响因子:
8.8
通讯作者:
Zang, Xuezhen
Zang, Xuezhen
中科院分区:
农林科学1区
文献类型:
--
作者:
Xie, Wenlei;Zang, Xuezhen

文献摘要

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制备了羟基磷灰石包裹的γ-Fe 2 O3纳米粒子,然后将来自Candida rugosa的脂肪酶通过共价键共价结合到磁性材料上。采用酶活性测定、X射线衍射(XRD)、红外光谱(FT-IR)、透射电子显微镜(TEM)、振动样品显微镜(VSM)和氮气吸附-脱附技术对磁性载体和固定化脂肪酶进行了表征。结果表明,γ-Fe 2 O3纳米粒子被羟基磷灰石包覆,脂肪酶确实被拴系到磁性载体上,而不破坏它们的结构。该固定化脂肪酶具有较强的磁响应性,对大豆油酯交换反应具有较高的催化活性。评价酯交换产物的总脂肪酸(FA)组成、滑熔点(SMP)、碘值、三酰甘油(TAG)分布和TAG中sn-2位的FA组成。酶法酯交换后,脂肪酸的位置分布和TAG种类发生了显着变化。此外,与物理共混物相比,酯交换产物的SMP明显降低。(C)2017爱思唯尔有限公司版权所有
Hydroxyapatite-encapsulated gamma-Fe2O3 nanoparticles were prepared, and lipase from Candida rugosa was then covalently bound onto the magnetic materials via covalent linkages. The magnetic carrier and immobilized lipase were characterized by enzyme activity assays, XRD, FT-IR, TEM, VSM and N-2 adsorption-desorption techniques. Results demonstrated that gamma-Fe2O3 nanoparticles were coated with the hydroxyapatite, and the lipase was indeed tethered to the magnetic carriers without damage to their structure. The immobilized lipase showed a strong magnetic responsiveness and displayed high catalytic activities towards the interesterification of soybean oil. The interesterified products were evaluated for their total fatty acid (FA) composition, slip melting point (SMP), iodine value, triacylglycerols (TAGs) profile and FA composition at sn-2 position in TAGs. The FA positional distributions and TAG species significantly changed after the enzymatic interesterification. Besides this, the interesterified products showed an obvious reduction in their SMP in comparison with the physical blends. (C) 2017 Elsevier Ltd. All rights reserved.