Rhizopus arrhizus lipase-catalyzed interesterification of the midfraction of palm oil to a cocoa butter equivalent fat
Abstract
Celite-immobilized lipase from Rhizopus arrhizus was used to interesterify triacylglycerols of the palm oil midfraction with stearic acid in n-hexane. Under optimum conditions, acyl exchange occurred mainly between the palmitoyl group from the palm oil midfraction and the stearoyl group from the reaction mixture, giving an interesterified product whose fatty acyl composition was similar to that of cocoa butter. Addition of defatted soya lecithin significantly increased the substrate conversion. This was attributed to the formation of reverse micelles around the Celite-immobilized and hydrated enzyme that protected the enzyme from the nonpolar solvent and enhanced substrate and product diffusion in the enzyme microenvironment. The reverse micelle system exhibited higher productivity and operational stability when compared to the Celite-immobilized lipase.
Keywords:
Celite-immobilized lipase / Interesterification reaction / palm oil midfraction / reverse micelleSource:
Enzyme and Microbial Technology, 1993, 15, 5, 438-443Publisher:
- Elsevier Science Inc, New York
DOI: 10.1016/0141-0229(93)90132-L
ISSN: 0141-0229
PubMed:
Scopus: 2-s2.0-0027593821
Institution/Community
Tehnološko-metalurški fakultetTY - JOUR AU - Mojović, Ljiljana AU - Šiler-Marinković, Slavica AU - Kukić, G. AU - Vunjak-Novaković, Gordana PY - 1993 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/45 AB - Celite-immobilized lipase from Rhizopus arrhizus was used to interesterify triacylglycerols of the palm oil midfraction with stearic acid in n-hexane. Under optimum conditions, acyl exchange occurred mainly between the palmitoyl group from the palm oil midfraction and the stearoyl group from the reaction mixture, giving an interesterified product whose fatty acyl composition was similar to that of cocoa butter. Addition of defatted soya lecithin significantly increased the substrate conversion. This was attributed to the formation of reverse micelles around the Celite-immobilized and hydrated enzyme that protected the enzyme from the nonpolar solvent and enhanced substrate and product diffusion in the enzyme microenvironment. The reverse micelle system exhibited higher productivity and operational stability when compared to the Celite-immobilized lipase. PB - Elsevier Science Inc, New York T2 - Enzyme and Microbial Technology T1 - Rhizopus arrhizus lipase-catalyzed interesterification of the midfraction of palm oil to a cocoa butter equivalent fat EP - 443 IS - 5 SP - 438 VL - 15 DO - 10.1016/0141-0229(93)90132-L ER -
@article{ author = "Mojović, Ljiljana and Šiler-Marinković, Slavica and Kukić, G. and Vunjak-Novaković, Gordana", year = "1993", abstract = "Celite-immobilized lipase from Rhizopus arrhizus was used to interesterify triacylglycerols of the palm oil midfraction with stearic acid in n-hexane. Under optimum conditions, acyl exchange occurred mainly between the palmitoyl group from the palm oil midfraction and the stearoyl group from the reaction mixture, giving an interesterified product whose fatty acyl composition was similar to that of cocoa butter. Addition of defatted soya lecithin significantly increased the substrate conversion. This was attributed to the formation of reverse micelles around the Celite-immobilized and hydrated enzyme that protected the enzyme from the nonpolar solvent and enhanced substrate and product diffusion in the enzyme microenvironment. The reverse micelle system exhibited higher productivity and operational stability when compared to the Celite-immobilized lipase.", publisher = "Elsevier Science Inc, New York", journal = "Enzyme and Microbial Technology", title = "Rhizopus arrhizus lipase-catalyzed interesterification of the midfraction of palm oil to a cocoa butter equivalent fat", pages = "443-438", number = "5", volume = "15", doi = "10.1016/0141-0229(93)90132-L" }
Mojović, L., Šiler-Marinković, S., Kukić, G.,& Vunjak-Novaković, G.. (1993). Rhizopus arrhizus lipase-catalyzed interesterification of the midfraction of palm oil to a cocoa butter equivalent fat. in Enzyme and Microbial Technology Elsevier Science Inc, New York., 15(5), 438-443. https://doi.org/10.1016/0141-0229(93)90132-L
Mojović L, Šiler-Marinković S, Kukić G, Vunjak-Novaković G. Rhizopus arrhizus lipase-catalyzed interesterification of the midfraction of palm oil to a cocoa butter equivalent fat. in Enzyme and Microbial Technology. 1993;15(5):438-443. doi:10.1016/0141-0229(93)90132-L .
Mojović, Ljiljana, Šiler-Marinković, Slavica, Kukić, G., Vunjak-Novaković, Gordana, "Rhizopus arrhizus lipase-catalyzed interesterification of the midfraction of palm oil to a cocoa butter equivalent fat" in Enzyme and Microbial Technology, 15, no. 5 (1993):438-443, https://doi.org/10.1016/0141-0229(93)90132-L . .