| Autor: |
Vassiliadi E; Institute of Chemical Biology, National Hellenic Research Foundation (NHRF), 48 Vassileos Constantinou Ave., 11635 Athens, Greece.; Department of Biological Applications and Technology, University of Ioannina, 45110 Ioannina, Greece., Tsirigotis-Maniecka M; Faculty of Chemistry, Wrocław University of Science and Technology, 50-370 Wroclaw, Poland., Symons HE; School of Chemistry, University of Bristol, Bristol BS8 1TS, UK., Gobbo P; Department of Chemical and Pharmaceutical Sciences, University of Trieste, 34127 Trieste, Italy., Nallet F; Centre de Recherche Paul-Pascal, University Bordeaux, CNRS, UMR 5031, 115 Avenue du Docteur-Schweitzer, 33600 Pessac, France., Xenakis A; Institute of Chemical Biology, National Hellenic Research Foundation (NHRF), 48 Vassileos Constantinou Ave., 11635 Athens, Greece., Zoumpanioti M; Institute of Chemical Biology, National Hellenic Research Foundation (NHRF), 48 Vassileos Constantinou Ave., 11635 Athens, Greece. |
| Abstrakt: |
The present work reports on the structural study of a film made of a hybrid blend of biopolymers used as an enzyme carrier. A cellulose derivative (HPMC) and chitosan (CS) were combined in order to formulate a film on which Mucor miehei lipase was immobilized. The film was successfully used as a biocatalyst; however, little is known about the structure of the system. Therefore, small-angle X-ray scattering, Fourier transform infrared spectroscopy (FTIR), optical microscopy, and scanning electron microscopy (SEM), as well as microindentation measurements, were used to shed light on the structure of the promising biocatalyst. Among the results, intermolecular hydrogen bonds were observed between the amide groups of the two polymers and the lipase. The presence of the enzyme does not seem to affect the mechanical properties of the matrix. The used film after 35 cycles of reaction seemed to be fatigued and had lost part of its humidity, explaining the reduction of the enzyme activity. |
