高等学校化学学报 ›› 2019, Vol. 40 ›› Issue (12): 2512-2520.doi: 10.7503/cjcu20190444

• 物理化学 • 上一篇    下一篇

铁氨基黏土纳米结构脂肪酶的构筑及催化特性

范小雨,王可,孙仕勇(),马彪彪,吕瑞   

  1. 西南科技大学环境与资源学院, 绵阳 621010
  • 收稿日期:2019-08-07 出版日期:2019-12-04 发布日期:2019-12-04
  • 通讯作者: 孙仕勇 E-mail:shysun@swust.edu.cn
  • 基金资助:
    国家自然科学基金(41672039);四川省杰出青年科技基金人才培育项目(2019JDJQ0056)

Construction and Catalytic Performances of Fe-aminoclay Nanostructured Lipase

Xiaoyu FAN,Ke WANG,Shiyong SUN(),Biaobiao MA,Rui LÜ   

  1. School of Environment and Resource, Southwest University of Science and Technology, Mianyang 621010, China
  • Received:2019-08-07 Online:2019-12-04 Published:2019-12-04
  • Contact: Shiyong SUN E-mail:shysun@swust.edu.cn
  • Supported by:
    ? Supported by the National Natural Science Foundation of China(41672039);the Youth Science and Technology Foundation of Sichuan Province, China(2019JDJQ0056)

摘要:

以铁氨基黏土(Fe-aminoclay)为载体, 1-(3-二甲氨基丙基)-3-乙基碳二亚胺盐酸盐(EDC)为共价交联剂, 构筑了铁氨基黏土纳米结构脂肪酶催化剂(Feclay-lipase). 利用X射线衍射(XRD)、 透射电子显微镜(TEM)和傅里叶变换红外光谱(FTIR)等技术对Feclay-lipase进行了表征, 并通过酶动力学对比研究了游离脂肪酶和Feclay-lipase的酶学特性. 结果表明, Fe-aminoclay的载酶量为414.4 mg/g, 固定化效率可达82.88%, Feclay-lipase的酶活较游离酶提高了3倍, 最适反应温度提高了10 ℃, 最适反应 pH向碱性偏移, 储存稳定性更好, 在4 ℃下贮存30 d后其酶活无明显减弱.

关键词: 铁氨基黏土, 脂肪酶, 纳米结构载体, 固定化酶, 纳米生物催化剂

Abstract:

Lipase from Aspergillus oryzae was immobilized on Fe-aminoclay support via 1-(3-dimethylami-nopropyl)-3-ethylcarbodiimide hydrochloride(EDC) as covalent crosslinking agent. The nanocomposite structure of immobilized lipase(Feclay-lipase) was characterized by means of X-ray diffraction(XRD), transmission electron microscope(TEM) and Fourier transform infrared spectroscopy(FTIR). The enzymatic properties of free lipase and Feclay-lipase were studied by enzymatic kinetics. The results showed that the optimal immobilization efficiency of Feclay-lipase was 82.88%, immobilization capacity was 414.4 mg/g support, and the enzyme activity was 28.24 U/mg, which was three times higher than that of free lipase(8.21 U/mg). The optimum reaction temperature of Feclay-lipase increased from 45 ℃ to 55 ℃, the optimum pH shifted to alkalinity, and the catalytic activity of Feclay-lipase did not decrease significantly after storage at 4 ℃ for one month.

Key words: Fe-aminoclay, Lipase, Nanostructured support, Enzyme immobilization, Nanobiocatalyst

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