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Title

Reuse of lipase from pseudomonas fluorescens via its step-by-step coimmobilization on glyoxyl-octyl agarose beads with least stable lipases

AuthorsRios, Nathalia S.; Arana-Peña, Sara; Mendez-Sanchez, Carmen; Ortiz, Claudia; Gonçalves, Luciana R. B.; Fernández-Lafuente, Roberto
KeywordsEnzyme coimmobilization
Glyoxyl-octyl
Covalent immobilization
Interfacial activation
Reuse of coimmobilized enzymes
Issue Date27-May-2019
PublisherMultidisciplinary Digital Publishing Institute
CitationCatalysts 9(5): 487 (2019)
AbstractCoimmobilization of lipases may be interesting in many uses, but this means that the stability of the least stable enzyme determines the stability of the full combilipase. Here, we propose a strategy that permits the reuse the most stable enzyme. Lecitase Ultra (LU) (a phospholipase) and the lipases from Rhizomucor miehei (RML) and from Pseudomonas fluorescens (PFL) were immobilized on octyl agarose, and their stabilities were studied under a broad range of conditions. Immobilized PFL was found to be the most stable enzyme under all condition ranges studied. Furthermore, in many cases it maintained full activity, while the other enzymes lost more than 50% of their initial activity. To coimmobilize these enzymes without discarding fully active PFL when LU or RML had been inactivated, PFL was covalently immobilized on glyoxyl-agarose beads. After biocatalysts reduction, the other enzyme was coimmobilized just by interfacial activation. After checking that glyoxyl-octyl-PFL was stable in 4% Triton X-100, the biocatalysts of PFL coimmobilized with LU or RML were submitted to inactivation under different conditions. Then, the inactivated least stable coimmobilized enzyme was desorbed (using 4% detergent) and a new enzyme reloading (using in some instances RML and in some others employing LU) was performed. The initial activity of immobilized PFL was maintained intact for several of these cycles. This shows the great potential of this lipase coimmobilization strategy.
Publisher version (URL)https://doi.org/10.3390/catal9050487
URIhttp://hdl.handle.net/10261/182936
DOI10.3390/catal9050487
E-ISSN2073-4344
Appears in Collections:(ICP) Artículos
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