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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Konieczna-Molenda, Anna Sokolowska, Katarzyna Swider, Joanna Witek, Ewa Proniewicz, Edyta Tata, Agnieszka |
| Description | Country affiliation: Poland Author Affiliation: Tata A ( Faculty of Foundry Engineering, AGH University of Science and Technology, ul. Reymonta 23, 30-059 Krakow, Poland.); Sokolowska K ( Faculty of Chemistry, Jagiellonian University, ul. Ingardena 3, 30-060 Krakow, Poland.); Swider J ( Faculty of Chemistry, Jagiellonian University, ul. Ingardena 3, 30-060 Krakow, Poland.); Konieczna-Molenda A ( Department of Chemistry and Physics, University of Agriculture, ul. Balicka 122, 30-149 Krakow, Poland.); Proniewicz E ( Faculty of Foundry Engineering, AGH University of Science and Technology, ul. Reymonta 23, 30-059 Krakow, Poland. Electronic address: proniewi@agh.edu.pl.); Witek E ( Faculty of Chemistry, Jagiellonian University, ul. Ingardena 3, 30-060 Krakow, Poland.) |
| Abstract | This study was focused on finding of effective carriers suitable for the immobilization of cellulase. Copolymers of N-vinylformamide (NFV) and divinylbenzene (DVB) were synthesized by free radical crosslinking polymerization in inverse suspension. Methyl silicone oil was used as the continuous phase. Three polymeric carriers based on P(NVF-co-DVB) with varying degrees of crosslinking and spherical particles with different grain sizes were obtained. The formamide groups in these carriers were hydrolyzed to amino groups, yielding three P(VAm-co-DVB) polymers with vinylamine units. Enzyme, cellulase (Novozym® 476), was immobilized onto carriers with vinylamine (through glutaraldehyde) and vinylformamide groups (without glutaraldehyde). The efficiency of the enzyme immobilization was determined based on the enzymatic activity of the enzyme during the catalytic reaction relative to that of the native enzyme. All tested carriers were found to be effective carriers for the immobilization of cellulase. However, the catalytic activity of cellulase immobilized on the P(VAM-co-DVB0.27)/2000/350 carrier was higher than that for the native enzyme. In addition, two molecular spectroscopy methods, Fourier-transform absorption infrared spectroscopy (FT-IR) and Fourier-transform Raman spectroscopy (FT-Raman), were used to analyze the carriers. These studies provided complete information regarding the structure of the studied copolymers. |
| ISSN | 13861425 |
| Volume Number | 149 |
| e-ISSN | 18733557 |
| Journal | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-01-01 |
| Publisher Place | Great Britain (UK) |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Amides Chemistry Cellulase Metabolism Enzymes, Immobilized Polyvinyls Cellulose Hydrolysis Kinetics Polymerization Spectroscopy, Fourier Transform Infrared Spectrum Analysis, Raman Time Factors Journal Article Research Support, Non-u.s. Gov't Discipline Spectroscopy |
| Content Type | Text |
| Resource Type | Article |
| Subject | Spectroscopy Atomic and Molecular Physics, and Optics Analytical Chemistry Instrumentation |
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