Effects of surface modification and activation of magnetic nanoparticles on the formation of amylase immobilization bonds under different ionic strength conditions

被引:20
作者
Eslamipour, Faegheh [1 ]
Hejazi, Parisa [1 ]
机构
[1] Iran Univ Sci & Technol, Biotechnol Res Lab, Sch Chem Engn, Tehran, Iran
关键词
Magnetic nanoparticles; Amylase; Immobilization mechanism; Glutaraldehyde; ALPHA-AMYLASE; SUPERPARAMAGNETIC NANOPARTICLES; ENZYME IMMOBILIZATION; SUPPORT ACTIVATION; LIPASE B; GLUTARALDEHYDE; ACID; FUNCTIONALIZATION; STABILITY; PROTEINS;
D O I
10.1016/j.molcatb.2015.05.006
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In this research, the effects of coating layers and their activation level on the mechanisms of amylase immobilization onto the surface of magnetic ferric oxide nanoparticles (MNPs) were investigated. Two MNPs with two different coating conditions were subjected to surface treatment using the amino groups, and then were activated with different concentrations of glutaraldehyde (GA). Immobilization level and activity of the immobilized enzyme were studied for low, moderate, and high ionic strengths of buffer solutions. Furthermore, the type of the bond developed between the enzyme and carrier was identified using the amount of immobilized enzyme released under different desorption conditions, and also through adsorption kinetic studies and FTIR analysis. The results indicated that for most cases, the mechanisms for amylase immobilization on MNPs activated with GA are first physical adsorption, followed by forming covalent bond between the enzyme and the coated MNPs. The maximum amount and activity of the immobilized amylase were 700 mg/gm(MNP) and 30 U/mg(immobilizedenz)., respectively, related to low GA-activated silica-coated MNPs (0.5%) and low concentration of buffer (5 mM). (C) 2015 Elsevier B.V. All rights reserved.
引用
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页码:1 / 11
页数:11
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