CONICET | Buscador de Institutos y Recursos Humanos

Enzyme catalysts are being increasingly applied in technological processes but it is often hampered by limitations mainly due to difficulties in enzyme recovery. Reuse as well as low operational stability renders the process expensive for technological applications. Immobilization is usually a requirement for the use of an enzyme as an industrial biocatalyst. Although there are many well-established immobilization protocols, search for new immobilization techniques are constantly pursued to obtain efficient biocatalysts. Nanostructures are very attractive for enzymatic immobilization processes since they possess ideal characteristics to enhance efficiency, from higher surface area to mass transfer resistance and effective enzyme loading. However the functionalization of the traditional nanosupports like chitosan, gold, diamond, metals, including graphene and zirconium is not a straightforward process. We have previously demonstrated the ability of several glycosaminoglicans to induce the growth of lysozyme amyloid nanofibrils to obtain an easily functionalizable nanomaterial and thus, it could be considered an efficient support for enzyme immobilization. To obtain a better recovery of the immobilized enzyme, here we propose a novel method to growth a protein amyloid nanofibrils on an activated borosilicate before the nanomaterial functionalization. The self-assembly of lactosuerum proteins triggered by silicate was detected by Raman and fluorescence techniques as well as enzymatic activity of crosslinked urease. The process efficiency depends on the nanofibrils growth condition as well as the crosslinking procedure. The protocol reported herein takes advantage of the high surface area of nanomaterials, easily functionalization of amyloid together with the packing facilities of borosilicate beds and therefore could be useful to design a new generation of insoluble biocatalyst.

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