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Enzyme Research
Volume 2011, Article ID 851272, 8 pages
http://dx.doi.org/10.4061/2011/851272
Research Article

Cross-Linked Enzyme Aggregates of Naringinase: Novel Biocatalysts for Naringin Hydrolysis

Research Institute for Medicines and Pharmaceutical Sciences (i-Med-UL), Faculty of Pharmacy, University of Lisbon, Av. Prof. Gama Pinto, 1649-003 Lisbon, Portugal

Received 15 May 2011; Accepted 4 July 2011

Academic Editor: J. Guisan

Copyright © 2011 Maria H. L. Ribeiro and Marco Rabaça. 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.

Abstract

Cross-linked enzyme aggregates (CLEAs) have emerged as interesting biocatalyst design for immobilization. These new generation enzyme biocatalysts, CLEAs, in addition to exhibiting good mechanical stability, can be highly active, since they do not include large amounts of foreign particulate nonenzymatic material and may have increased stability. Naringinase (NGase) is an enzyme complex with high potential in pharmaceutical and food industries. In fact, NGase can be used in the biotransformation of steroids, of antibiotics and mainly on glycosides hydrolysis. In this paper, the formation of CLEAs was tried using ammonium sulphate, polyethylene glycol 6000 and tert-butyl alcohol as precipitant agents and glutaraldehyde as cross-linking agent, at different pH, time, and temperature conditions. However, among the precipitant agents tested, only tert-butyl alcohol cross-linked with glutaraldehyde allowed the formation of CLEAs, at pH 4.0 and at temperature between 7 and . Different enzyme loadings were tested. The NGase-CLEAs were highly effective in naringin hydrolysis. The operational stability of the NGase-CLEAs aggregates was studied through six successive reutilizations.