alexa A Highly Stable Biocatalyst Obtained from Covalent Immo
ISSN: 2155-9821

Journal of Bioprocessing & Biotechniques
Open Access

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Research Article

A Highly Stable Biocatalyst Obtained from Covalent Immobilization of a Non-Commercial Cysteine Phytoprotease

Walter David Obregón1, José Sebastián Cisneros1, Florencia Ceccacci1 and Evelina Quiroga2*
1Research Laboratory Vegetable Proteins (LIPROVE), Faculty of Sciences, National University of La Plata (UNLP), 47 and 115 s / N, La Plata (B1900AVW), Argentina
2Membranes and Biomaterials Laboratory, Institute of Applied Physics (INFAP) -CONICET, National University of San Luis (UNSL), Almirante Brown 907, San Luis (D5700HHW), Argentina
Corresponding Author : Evelina Quiroga
Membranes and Biomaterials Laboratory
Institute of Applied Physics (INFAP) -CONICET
National University of San Luis (UNSL)
Almirante Brown 907, San Luis (D5700HHW), Argentina
Tel: 542-652-423-789
E-mail: [email protected]
Received January 26, 2015; Accepted February 24, 2015; Published February 27, 2015
Citation: Obregón WD, Cisneros JS, Ceccacci F Quiroga E (2015) A Highly Stable Biocatalyst Obtained from Covalent Immobilization of a Non-Commercial Cysteine Phytoprotease. J Bioprocess Biotech 5:211. doi: 10.4172/2155-9821.1000211
Copyright: © 2015 Obregón WD, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
 

Abstract

In this work, araujiain (enzymatic preparation obtained from the latex of Araujia hortorum fruits) was successfully immobilized on glyoxyl-agarose via multipoint covalent attachment. Thus, good efficiency of immobilization and high operational stability of immobilized enzyme were obtained. The activity of araujiain at alkaline pH was significantly improved after immobilization. In addition, immobilized araujiain also showed high activity and good stability, without significant loss in its activity, at temperatures between 37 and 60°C and in the presence of immiscible organic solvents. Immobilized araujiain also showed good performance in a mixture of 50% ethyl acetate in buffer, used for peptide synthesis, with better results than when the free enzyme was used as catalyst. These results indicate that immobilized araujiain via multipoint covalent attachment can be highly stabilized and this method might be used for practical applications of araujiain in hydrolytic and synthetic processes.

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