Issue 20, 2012
From the journal:

Analyst

Immobilization of pectinase from Leucoagaricus gongylophorus on magnetic particles

Paulo Roberto Adalberto,a   Francisco José dos Santos,b   Camilla Calemi Golfeto,a   Mônica Rosas Costa Iemma,a   Dulce Helena Ferreira de Souzaa  and  Quezia Bezerra Cass*a  

* Corresponding authors

a Departamento de Química, Universidade Federal de São Carlos, Cx. Postal 676, São Carlos, São Paulo, Brazil
E-mail: quezia@pq.cnpq.br
Fax: +55-16-3351-8350

b Procell Biologics, Avenida Comendador Alfredo Maffei, 4001, São Carlos, SP, Brazil

Abstract

Polygalacturonases (EC 3.2.1.15) hydrolyze the α-1,4-glycosidic linkages in polygalacturonic acid chains. The interest on specific inhibitors of pectinase and the versatility of magnetic support for enzyme immobilization endorsed the preparation of an immobilized enzyme reactor (IMER). This work presents the synthesis of CoFe2O4 amino-derivatives, which was employed as the support for the immobilization of pectinases from Leucoagaricus gongylophorus. Amino-functionalized CoFe2O4 was obtained from glyceryl-derivatized CoFe2O4 and was characterized by infrared spectroscopy and electronic microscopy. The immobilized enzyme maintained the same thermal, chemical and kinetic behaviour of the free enzyme (Topt 60 °C; pHopt 5.0; KappM = 0.5 mg min−1; Vappmax ≈ 5.0 μmol min−1 mL−1). The straightforward synthesis of CoFe2O4 derivatives and the efficiency of immobilization offer wide perspectives for the use of the developed new IMER.

Graphical abstract: Immobilization of pectinase from Leucoagaricus gongylophorus on magnetic particles

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Article information

DOI
https://doi.org/10.1039/C2AN35682A
Article type
Paper
Submitted
23 May 2012
Accepted
17 Aug 2012
First published
17 Aug 2012

Analyst, 2012,137, 4855-4859

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Immobilization of pectinase from Leucoagaricus gongylophorus on magnetic particles

P. R. Adalberto, F. José dos Santos, C. C. Golfeto, M. R. Costa Iemma, D. H. Ferreira de Souza and Q. B. Cass, Analyst, 2012, 137, 4855 DOI: 10.1039/C2AN35682A

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