Effects of Regioselectivity and Lipid Class Specificity of Lipases on Transesterification, Exemplified by Biodiesel Production

Abstract

Lipase-catalyzed ethanolysis of triolein was studied as a model for biodiesel production. Four lipases were immobilized on porous polypropylene, and ethanolysis reactions were carried out in methyl t-butyl ether. The reaction products were analyzed using gas chromatography. Three of the four lipases studied were efficient in the conversion of triolein to 2-monoolein, but slow in the final step of producing glycerol. However, Candida antarctica lipase B was slow in the conversion of triolein, but more efficient in the subsequent two steps than the other lipases. The 1,3-selectivity of the lipases was less pronounced for the monooleins than for triolein. Silica gel was investigated as a catalyst for acyl migration, showing an increase in biodiesel yield with three of the lipases, but a reduction in yield when C. antarctica lipase B was used. The highest biodiesel yield (96 %) was obtained with a combination of Rhizopus arrhizus lipase and C. antarctica lipase B.Electronic supplementary materialThe online version of this article (doi:10.1007/s11746-014-2465-7) contains supplementary material, which is available to authorized users.

Lipases in liquid formulation for biodiesel production: Current status and challenges

“…For a satisfactory production, lipases should be able to convert all three forms of glyceridesmonoacylglycerols (MAG), diacylglycerols (DAG), and TAG-to biodiesel. Lipases with a limited specificity become inapplicable for biodiesel production, whereas lipases with sn-1,3-specific efficiently catalyze the process [72] and their yields exceed maximum theoretical yields under appropriate operating conditions [73]. Figure 4 shows how a sn-1,3-specific lipasecatalyzed alcoholysis with acyl migration develops.…”

“…Remonatto et al [33] reports that the use of liquid lipases on biodiesel production can make the whole process more sustainable, cost effective, and competitive, once these commercial enzymes can be produced and sold to prices up to 50 times lower than the immobilized biocatalysts. Furthermore, it is important to cite that lipases are spontaneously soluble in aqueous solutions as a result of their globular protein nature [72]. Pedersen et al [107] describe that the use of lipases in liquid formulation modifies the reaction system in diverse forms.…”

Novel Combi-lipase Systems for Fatty Acid Ethyl Esters Production

“…In this work, it is shown that the immobilization support alone plays also a key role in the CL properties assessed: The CF values obtained for the biocatalysts obtained by the combination of derivatives of the same lipase on LW and PU supports (semiCL) differ from a merely additive effect (Figure 3). In general, it is expected a synergistic effect in CL (CF s > 1) when the component biocatalysts complement each other in their respective rate-limiting steps, e.g., one is faster acting on triglycerides, but slower than the other on partial glycerides [33]. Negative effects (CF s < 1), when inhibitors and/or inactivators (e.g., glycerol or ethanol [34]) for each biocatalyst are accumulated along the reaction time in a higher degree for the presence of the other component with regard to the situation when each biocatalyst was alone.…”

Optimisation of enzymatic transesterification of linseed oil and pork lard mixture with ethanol using response surface methodology

“…One reason may be the enzyme's intolerance for water, which is present in non-refined LO or other constituents of reaction. 19 Lipolase 100 L (EX) was selected for further reaction condition optimisation by RSM.…”