Site-Specific Covalent Immobilization of Methylobacterium extorquens Non-Blue Laccse Melac13220 on Fe3O4 Nanoparticles by Aldehyde Tag
文献类型： 外文期刊
作者： Ainiwaer, Abidan 1 ; Li, Ao 1 ; Zhao, Xingwang 1 ; Xu, Yujiao 1 ; Han, Siping 2 ; Gao, Renjun 1 ;
作者机构： 1.Jilin Univ, Sch Life Sci, Key Lab Mol Enzymol & Engn, Minist Educ, Changchun 130012, Peoples R China
2.Jilin Acad Agr Sci, Inst Agr Biotechnol, Changchun 130033, Peoples R China
关键词： laccase; immobilization; covalent binding; entrapment; thermal stability
期刊名称：CATALYSTS （ 影响因子：4.501； 五年影响因子：4.641 ）
ISSN：
年卷期： 2022 年 12 卷 11 期
页码：
收录情况： SCI
摘要： In the present study, the non-blue laccase Melac13220 from Methylobacterium extorquens was immobilized using three methods to overcome problems related to the stability and reusability of the free enzyme: entrapment of the enzyme with sodium alginate, crosslinking of the enzyme with glutaraldehyde and chitosan-, and site-specific covalent immobilization of the enzyme on Fe3O4 nanoparticles by an aldehyde tag. The site-specific covalent immobilization method showed the highest immobilization efficiency and vitality recovery. The optimum temperature of Melac13220 was increased from 65 degrees C to 80 degrees C. Immobilized Melac13220 showed significant tolerance to some organic solvents and maintained approximately 80% activity after 10 cycles of use. Differential scanning calorimetry (DSC) indicated that the melting temperature of the enzyme was increased (from 57 degrees C to 79 degrees C). Immobilization of Melac13220 also led to improvement in dye decolorization such that Congo Red was completely decolorized within 10 h. The immobilized enzyme can be easily prepared without purification, demonstrating the advantages of using the aldehyde tag strategy and providing a reference for the practical application of different immobilized laccase methods in the industrial field.
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