Biocatalytic characterization of Aspergillus oryzae -galactosidase immobilized on functionalized multi-walled carbon nanotubes

被引:10
|
作者
Rosolen, Michele Dutra [1 ]
Gennari, Adriano [1 ]
Volpato, Giandra [2 ]
Volken de Souza, Claucia Fernanda [1 ]
机构
[1] Ctr Univ UNIVATES, Lab Biotecnol Alimentos, Programa Posgrad Biotecnol, Ave Avelino Tallini 171, BR-95900000 Lajeado, RS, Brazil
[2] Inst Fed Educ Ciencia & Tecnol Rio Grande do Sul, Curso Biotecnol, Campus Porto Alegre, Porto Alegre, RS, Brazil
关键词
Aspergillus oryzae; -galactosidase; carbon nanotubes; functionalization; immobilization; BETA-GALACTOSIDASE; KLUYVEROMYCES-LACTIS; LACTOSE HYDROLYSIS; ENZYME STABILITY; THERMODYNAMICS; LIPASE;
D O I
10.1080/10242422.2017.1323886
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
The objectives of this work were to immobilize commercial Aspergillus oryzae -galactosidase on functionalized multi-walled carbon nanotubes (MWCNTs) using different treatments and to characterize the products. Treatments were performed with glutaraldehyde, ethylenediamine and a mixture of concentrated H2SO4:HNO3. The MWCNTs and their derivatives were characterized by thermogravimetric analysis. The immobilized enzymes were evaluated using inactivation kinetics, operating conditions, that is pH and temperature, kinetic parameters and lactose hydrolysis reusability. Immobilization yield and efficiency were significantly higher for -galactosidase immobilized on MWCNTs functionalized by the acid mixture (Ac-Gal-MWCNTs). These values were 97% and 82%, respectively, after 3h of immobilization. The activity of the Ac-Gal-MWCNTs was maintained at approximate to 51% of their initial activity after being stored for 90 days at 4 degrees C. The Ac-Gal-MWCNTs retained more than 90% of their initial activity up to the fourth recycle. As the acid functionalization was the most efficient method tested for immobilizing A. oryzae -galactosidase on MWCNTs, this method shows promise for industrial applications.
引用
收藏
页码:260 / 268
页数:9
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