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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Tudorache, Madalina Gheorghe, Andreea Negoi, Alina Enache, Madalin Maria, Gabriel-Mihai Parvulescu, Vasile I. |
| Description | Country affiliation: Romania Author Affiliation: Tudorache M ( University of Bucharest, Department of Organic Chemistry, Biochemistry and Catalysis, Bd. Regina Elisabeta 4-12, Bucharest 030016, Romania.); Gheorghe A ( University of Bucharest, Department of Organic Chemistry, Biochemistry and Catalysis, Bd. Regina Elisabeta 4-12, Bucharest 030016, Romania.); Negoi A ( University of Bucharest, Department of Organic Chemistry, Biochemistry and Catalysis, Bd. Regina Elisabeta 4-12, Bucharest 030016, Romania.); Enache M ( Institute of Biology Bucharest of the Romanian Academy, Spl. Independentei 296, Sect. 6, P.O. Box 56-53, 060031, Bucharest, Romania.); Maria GM ( Institute of Biology Bucharest of the Romanian Academy, Spl. Independentei 296, Sect. 6, P.O. Box 56-53, 060031, Bucharest, Romania.); Parvulescu VI ( University of Bucharest, Department of Organic Chemistry, Biochemistry and Catalysis, Bd. Regina Elisabeta 4-12, Bucharest 030016, Romania. Electronic address: vasile.parvulescu@g.unibuc.ro.) |
| Abstract | Bifunctional catalysts designed as carbohydrate biopolymers entrapping lipase have been investigated for the biotransformation of a natural compound ( -pinene) to oxy-derivatives. Lipases assisted the epoxidation of -pinene using H2O2 as oxidation reagent and ethyl acetate as both acetate-supplier and solvent affording -pinene oxide as the main product. Further, the biopolymer promoted the isomerization of -pinene oxide to campholenic aldehyde and trans-carenol. In this case, the biopolymers played double roles of the support and also active part of the bifunctional catalyst. Screening of enzymes and their entrapping in a biopolymeric matrix (e.g. Ca-alginate and κ-carrageenan) indicated the lipase extracted from Aspergillus niger as the most efficient. In addition, the presence of biopolymers enhanced the catalytic activity of the immobilized lipase (i.e. 13.39×10(3), 19.76×10(3)and 26.46×10(3) for the free lipase, lipase-carrageenan and lipase-alginate, respectively). The catalysts stability and reusability were confirmed in eight consecutively reaction runs. |
| File Format | HTM / HTML |
| ISSN | 01448617 |
| Journal | Carbohydrate Polymers |
| Volume Number | 152 |
| e-ISSN | 18791344 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2016-11-05 |
| Publisher Place | Great Britain (UK) |
| Access Restriction | One Nation One Subscription (ONOS) |
| Content Type | Text |
| Resource Type | Article |
| Subject | Organic Chemistry Materials Chemistry Polymers and Plastics |
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