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Lipase‐catalyzed alcoholysis of crambe oil and camelina oil for the preparation of long‐chain esters
Author(s) -
Steinke Georg,
Kirchhoff Rita,
Mukherjee Kumar D.
Publication year - 2000
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/s11746-000-0059-8
Subject(s) - camelina , chemistry , lipase , crambe , rhizomucor miehei , organic chemistry , isopropyl , oleyl alcohol , triacylglycerol lipase , alcohol , chromatography , food science , botany , biology , enzyme
Crambe oil and camelina oil were transesterified with oleyl alcohol, the alcohols derived from crambe and camelina oils, n ‐octanol or isopropanol using Novozym 435 (immobilized lipase B from Candida antarctica ), Lipozyme IM (immobilized lipase from Rhizomucor miehei ), and papaya ( Carica papaya ) latex lipase as biocatalysts. The highest conversions to alkyl esters were obtained with Novozym 435 (up to 95%) in most cases, whereas Lipozyme IM and papaya latex lipase gave lower (40 to 50%) conversions. The conversions with long‐chain alcohols (oleyl alcohol, crambe alcohols, and camelina alcohols) were higher (40 to 95%) than with medium‐chain n ‐octanol (30 to 85%). Isopropyl esters of crambe oil and camelina oil were obtained with rather low conversions using Novozym 435 (<40%) and Lipozyme IM (about 10%) as biocatalysts, whereas with papaya latex lipase no isopropyl esters were formed. The conversions of crambe oil and camelina oil to oleyl and n ‐octyl esters using Novozym 435 as biocatalyst were hardly affected by the ratio of the substrates, but with Lipozyme IM the conversions to alkyl esters distinctly increased with an excess of alcohol substrate