Lipase-catalyzed transesterification of rendering plant fat - Short Communication
| Autor: | L. Škarková, J. Kučera, Z. Kopicová, A. Prošková |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
0301 basic medicine
030109 nutrition & dietetics Immobilized enzyme biology Chemistry Aspergillus niger Triacylglycerol lipase Transesterification biology.organism_classification Chitosan 03 medical and health sciences chemistry.chemical_compound biology.protein Organic chemistry Animal Science and Zoology Methanol Lipase Methyl acrylate Agronomy and Crop Science |
| Zdroj: | Research in Agricultural Engineering. 56:122-125 |
| ISSN: | 1805-9376 1212-9151 |
| DOI: | 10.17221/40/2009-rae |
| Popis: | Proskova A., Kopicova Z., Kucera J., Skarkova L. , 2010. Lipase-catalyzed transesterification of rendering plant fat . Res. Agr. Eng., 56: 122–125. Soluble lipase (Lipozyme CALB L) was immobilized by covalent bond to chitosan pellets prepared from Aspergillus niger mycelium. This immobilized enzyme was compared with commercial immobilized lipase of the same origin (Novozym 435). Novozym 435 is also lipase CALB L commercially immobilized by sorption on poly-(methyl acrylate). Novozym 435 shows much higher conversion of rendering plant fat in methanol under optimum conditions, having, at the same time, lower optimum temperature and lower stability at higher temperature. Lipozyme CALB L immobilized on chitosan leads to a low conversion, regardless its higher thermal stability. Novozym 435 gives conversion of about 50% of theoretical value, which is in good accordance with basically catalyzed transesterification of rendering plant fat described elsewhere. Lipozyme CALB L immobilized on chitosan gives conversion of about 10% of theoretical value only. The use of Novozym 435 in two-step system (enzyme-acid) seems to be more convenient compared with tradi tional two-step system (base-acid). |
| Databáze: | OpenAIRE |
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