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Molecules 2017, 22(7), 1088; doi:10.3390/molecules22071088

New Heterofunctional Supports Based on Glutaraldehyde-Activation: A Tool for Enzyme Immobilization at Neutral pH

1
Departamento de Biocatálisis, Instituto de Catálisis y Petroleoquímica (CSIC), Marie Curie 2. Cantoblanco, Campus UAM, 28049 Madrid, Spain
2
Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE), Centro Nacional de Pesquisa em Energia e Materiais (CNPEM), Cx. P. 6192, 13083-970 Campinas, São Paulo, Brazil
3
Departamento de Ciência de Alimentos, Faculdade de Engenharia de Alimentos (FEA), Universidade Estadual de Campinas (UNICAMP), 13083-862 Campinas, São Paulo, Brazil
4
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Paraná, Cx. P. 19081 Centro Politécnico, 81531-980 Curitiba, Paraná, Brazil
5
Departamento de Química, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, 14040-901 Ribeirão Preto, São Paulo, Brazil
6
Departamento de Química, Universidade Federal do Paraná, Cx. P. 19081 Centro Politécnico, 81531-980 Curitiba, Paraná, Brazil
Author contributions: These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Received: 3 May 2017 / Revised: 26 June 2017 / Accepted: 27 June 2017 / Published: 29 June 2017
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Abstract

Immobilization is an exciting alternative to improve the stability of enzymatic processes. However, part of the applied covalent strategies for immobilization uses specific conditions, generally alkaline pH, where some enzymes are not stable. Here, a new generation of heterofunctional supports with application at neutral pH conditions was proposed. New supports were developed with different bifunctional groups (i.e., hydrophobic or carboxylic/metal) capable of adsorbing biocatalysts at different regions (hydrophobic or histidine richest place), together with a glutaraldehyde group that promotes an irreversible immobilization at neutral conditions. To verify these supports, a multi-protein model system (E. coli extract) and four enzymes (Candida rugosa lipase, metagenomic lipase, β-galactosidase and β-glucosidase) were used. The immobilization mechanism was tested and indicated that moderate ionic strength should be applied to avoid possible unspecific adsorption. The use of different supports allowed the immobilization of most of the proteins contained in a crude protein extract. In addition, different supports yielded catalysts of the tested enzymes with different catalytic properties. At neutral pH, the new supports were able to adsorb and covalently immobilize the four enzymes tested with different recovered activity values. Notably, the use of these supports proved to be an efficient alternative tool for enzyme immobilization at neutral pH. View Full-Text
Keywords: enzyme immobilization; heterofunctional supports; glutaraldehyde; thermal stability; Candida rugosa lipase; metagenomic lipase; β-glucosidase; β-galactosidase enzyme immobilization; heterofunctional supports; glutaraldehyde; thermal stability; Candida rugosa lipase; metagenomic lipase; β-glucosidase; β-galactosidase
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Melo, R.R.; Alnoch, R.C.; Vilela, A.F.L.; Souza, E.M.; Krieger, N.; Ruller, R.; Sato, H.H.; Mateo, C. New Heterofunctional Supports Based on Glutaraldehyde-Activation: A Tool for Enzyme Immobilization at Neutral pH. Molecules 2017, 22, 1088.

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