Skip to the main content

Chemical and Biochemical Engineering Quarterly, Vol. 23 No. 4, 2009.

Original scientific paper

Lentikat®-based Biocatalysts: Effective Tools for Inulin Hydrolysis

S. Cattorini ; IBB-Institute for Biotechnology and Bioengineering, Centre for Biological and Chemical Engineering, Instituto Superior Técnico, Av. Rovisco Pais, 1049-001 Lisboa, Portugal
M. P. C. Marques ; IBB-Institute for Biotechnology and Bioengineering, Centre for Biological and Chemical Engineering, Instituto Superior Técnico, Av. Rovisco Pais, 1049-001 Lisboa, Portugal
F. Carvalho ; IBB-Institute for Biotechnology and Bioengineering, Centre for Biological and Chemical Engineering, Instituto Superior Técnico, Av. Rovisco Pais, 1049-001 Lisboa, Portugal
V. Chheub ; IBB-Institute for Biotechnology and Bioengineering, Centre for Biological and Chemical Engineering, Instituto Superior Técnico, Av. Rovisco Pais, 1049-001 Lisboa, Portugal
J. M. S. Cabral ; IBB-Institute for Biotechnology and Bioengineering, Centre for Biological and Chemical Engineering, Instituto Superior Técnico, Av. Rovisco Pais, 1049-001 Lisboa, Portugal
P. Fernandes orcid id orcid.org/0000-0003-0271-7796 ; IBB-Institute for Biotechnology and Bioengineering, Centre for Biological and Chemical Engineering, Instituto Superior Técnico, Av. Rovisco Pais, 1049-001 Lisboa, Portugal

Full text: english pdf 552 Kb

page 429-434

downloads: 620

cite

Abstract

A commercial inulinase preparation from Aspergillus niger was immobilized into polyvinyl alcohol hydrogel lenticular particles (Lentikats®) and into hemispheric-shaped capsules, both based on the use of LentiKat® liquid. The characterization of the resulting
biocatalysts, aiming at inulin hydrolysis to fructose, was performed, and the two methods of immobilization were compared. Temperature and pH profiles, as well as kinetic constants were determined, for both free and immobilized enzyme preparations. A broader-shaped curve was observed for the pH-activity profile when immobilized forms were compared to the free form. The apparent KM of inulinase increased roughly 2-fold upon immobilization in either form of the support particles, suggesting diffusion limitations of inulin inside the gel. Long-term operation with immobilized enzymes proved unfeasible above 55 °C, due to the lack of mechanical stability of the supports tested. When the temperature of incubation was lowered to 50 °C, the hemispheric form of the immobilized enzyme displayed considerable long-term operational stability, since it allowed 20 repeated, consecutive batch-mode runs, with a final decay in product yield of 20 %. When inulinase immobilized in Lentikats® particles was used, the final decay in product yield was roughly 70 %.

Keywords

Inulinase; inulin hydrolysis; polyvinyl alcohol; enzyme immobilization; polyethylene glycol

Hrčak ID:

45384

URI

https://hrcak.srce.hr/45384

Publication date:

23.12.2009.

Visits: 1.580 *