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Volume 70, Issue 5

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

Karolina Labus
  • Corresponding author
  • Division of Bioprocess and Biomedical Engineering, Faculty of Chemistry, Wroclaw University of Technology, Norwida 4/6, 50–373 Wroclaw, Poland
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  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Aleksandra Drozd
  • Division of Bioprocess and Biomedical Engineering, Faculty of Chemistry, Wroclaw University of Technology, Norwida 4/6, 50–373 Wroclaw, Poland
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Anna Trusek-Holownia
  • Division of Bioprocess and Biomedical Engineering, Faculty of Chemistry, Wroclaw University of Technology, Norwida 4/6, 50–373 Wroclaw, Poland
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2016-02-11 | DOI: https://doi.org/10.1515/chempap-2015-0235

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.

The immobilisation experiments indicated gelatine-based hydrogels crosslinked with transglutaminase as suitable for use as matrices for the entrapment of enzymes, which catalyse the conversion of low-molecular mass compounds. In addition to the potential for effective re-use in subsequent batch processes, the essential advantage of the immobilised β-galactosidase obtained in the current study is a marked reduction in its volume under storage conditions of long duration, without any significant decline in catalytic activity.

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

Presented at the 42nd International Conference of the Slovak Society of Chemical Engineering, Tatranské Matliare, Slovakia, 25–29 May 2015.

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About the article

Received: 2015-06-16

Revised: 2015-10-02

Accepted: 2015-10-05

Published Online: 2016-02-11

Published in Print: 2016-05-01


Citation Information: Chemical Papers, Volume 70, Issue 5, Pages 523–530, ISSN (Online) 1336-9075, ISSN (Print) 0366-6352, DOI: https://doi.org/10.1515/chempap-2015-0235.

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