Electrochemically synthesized polyaniline as support for lipase immobilization

被引:17
作者
Bezbradica, Dejan [1 ]
Jugovic, Branimir [2 ]
Gvozdenovic, Milica [1 ]
Jakovetic, Sonja [1 ]
Knezevic-Jugovic, Zorica [1 ]
机构
[1] Univ Belgrade, Fac Technol & Met, Belgrade 11000, Serbia
[2] Serbian Acad Arts & Sci, Inst Tech Sci, Belgrade 11000, Serbia
关键词
Lipase; Amination; Polyaniline; Electrochemical synthesis; Galvanostatic technique; CHEMICAL AMINATION; PROTEIN IMMOBILIZATION; ENZYME IMMOBILIZATION; GLUCOSE-OXIDASE; BIOSENSOR; GLUTARALDEHYDE; STABILIZATION; ACTIVATION; ELECTRODE; FILM;
D O I
10.1016/j.molcatb.2011.02.004
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要
Electrochemical synthesis of polyaniline support for enzyme immobilization provides easier control over the properties of obtained polymer and reduced risk of biocatalyst inactivation with residues of toxic compounds. In the present study, immobilization of lipase from Candida rugosa on electrochemically synthesized PANI (activated with glutaraldehyde) resulted with high lipase loadings up to 93.7 mg of proteins per gram of dry support. The activation of support and immobilization were optimized, with respect to activity yield. The optimum concentration of glutaraldehyde was 2% (w/v) and optimum concentration of enzyme was 4 mg ml(-1). Modification of enzyme surface with carbodiimide and ethylenediamine was performed in order to increase concentration of amino groups. Aminated lipase exhibited higher specific activity (52%) and thermal stability (3 times) after immobilization, compared with non-modified lipase. Also, reusability of immobilized enzyme was significantly increased with amination, especially if immobilization was performed at pH 10, so in such a way obtained derivative retained 91% of activity after 15 reaction cycles. (C) 2011 Elsevier B.V. All rights reserved.
引用
收藏
页码:55 / 60
页数:6
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