Next Article in Journal
A New Canthinone-Type Alkaloid Isolated from Ailanthus altissima Swingle
Next Article in Special Issue
Stabilization of Candida antarctica Lipase B (CALB) Immobilized on Octyl Agarose by Treatment with Polyethyleneimine (PEI)
Previous Article in Journal
In Vitro Antioxidant, Anti-Diabetes, Anti-Dementia, and Inflammation Inhibitory Effect of Trametes pubescens Fruiting Body Extracts
Previous Article in Special Issue
Editorial: Special Issue — Enzyme Immobilization
Article Menu
Issue 5 (May) cover image

Export Article

Open AccessArticle
Molecules 2016, 21(5), 646; doi:10.3390/molecules21050646

Reversible Immobilization of Lipases on Heterofunctional Octyl-Amino Agarose Beads Prevents Enzyme Desorption

1
Departamento de Biocatalisis, Instituto de Catálisis-CSIC; C/ Marie Curie 2, Campus UAM-CSIC, Madrid 28049, Spain
2
Escuela de Química, Grupo de investigación en Bioquímica y Microbiología (GIBIM), Edificio Camilo Torres 210, Universidad Industrial de Santander, Bucaramanga 680002, Colombia
3
Departamento de Engenharia Química, Universidade Federal Do Ceará, Campus Do Pici, CEP 60455-760 Fortaleza, Brazil
4
Escuela de Microbiología, Universidad Industrial de Santander, Bucaramanga 680002, Colombia
5
Departamento de Química, Facultad de Ciencias, Universidad del Tolima, Ibagué 546, Colombia
These authors contributed equally to this work.
Current address: Laboratorio de Biotecnología, Instituto Colombiano del Petróleo-Ecopetrol, Piedecuesta, Bucaramanga 680012, Colombia
*
Author to whom correspondence should be addressed.
Academic Editor: Derek J. McPhee
Received: 16 March 2016 / Revised: 28 April 2016 / Accepted: 9 May 2016 / Published: 16 May 2016
(This article belongs to the Special Issue Enzyme Immobilization 2016)
View Full-Text   |   Download PDF [4510 KB, uploaded 16 May 2016]   |  

Abstract

Two different heterofunctional octyl-amino supports have been prepared using ethylenediamine and hexylendiamine (OCEDA and OCHDA) and utilized to immobilize five lipases (lipases A (CALA) and B (CALB) from Candida antarctica, lipases from Thermomyces lanuginosus (TLL), from Rhizomucor miehei (RML) and from Candida rugosa (CRL) and the phospholipase Lecitase Ultra (LU). Using pH 5 and 50 mM sodium acetate, the immobilizations proceeded via interfacial activation on the octyl layer, after some ionic bridges were established. These supports did not release enzyme when incubated at Triton X-100 concentrations that released all enzyme molecules from the octyl support. The octyl support produced significant enzyme hyperactivation, except for CALB. However, the activities of the immobilized enzymes were usually slightly higher using the new supports than the octyl ones. Thermal and solvent stabilities of LU and TLL were significantly improved compared to the OC counterparts, while in the other enzymes the stability decreased in most cases (depending on the pH value). As a general rule, OCEDA had lower negative effects on the stability of the immobilized enzymes than OCHDA and while in solvent inactivation the enzyme molecules remained attached to the support using the new supports and were released using monofunctional octyl supports, in thermal inactivations this only occurred in certain cases. View Full-Text
Keywords: heterofunctional supports; octyl supports; interfacial activation of lipases; ion exchange; enzyme hyperactivation; reversible immobilization heterofunctional supports; octyl supports; interfacial activation of lipases; ion exchange; enzyme hyperactivation; reversible immobilization
Figures

Figure 1

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).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Rueda, N.; Albuquerque, T.L.; Bartolome-Cabrero, R.; Fernandez-Lopez, L.; Torres, R.; Ortiz, C.; dos Santos, J.C.S.; Barbosa, O.; Fernandez-Lafuente, R. Reversible Immobilization of Lipases on Heterofunctional Octyl-Amino Agarose Beads Prevents Enzyme Desorption. Molecules 2016, 21, 646.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]

Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top