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Preparation and characterisation of gelatine hydrogels predisposed to use as matrices for effective immobilisation of biocatalystst‡

Karolina Labus, Aleksandra Drozd, and Anna Trusek-Holownia

aDivision of Bioprocess and Biomedical Engineering, Faculty of Chemistry, Wroclaw University of Technology, Norwida 4/6, 50–373 Wroclaw, Poland

 

E-mail: karolina.labus@pwr.edu.pl

Abstract: Physical, enzymatic and chemical methods were used to develop an efficient procedure for preparing gelatine hydrogels of appropriate strength and elastic properties for applications as enzyme carriers. The concentrations of the crosslinking enzyme (transglutaminase), the initial amount of gelatine, the production time and the effect of additional crosslinking with glutaraldehyde were examined. As a result, the following conditions were selected: 0.1 g cm–3 solution of gelatine, 0.01 g cm–3 of transglutaminase (mTGase), a minimum of 2 h incubation at 4°C and an additional step of crosslinking with 1.0 vol. % of glutaraldehyde. Next, the absorption properties and storage stability of hydrogels so obtained were determined. From these results, it was observed that, with the exception of the physical gel, the remaining materials presented a relatively high resistance to hydrolytic degradation and retained their original spatial structure without any visible damages.

Keywords: gelatine – hydrogel – enzymatic crosslinking – absorption properties – enzyme immobilisation

Full paper is available at www.springerlink.com.

DOI: 10.1515/chempap-2015-0235

 

Chemical Papers 70 (5) 523–530 (2016)

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