A review on biodiesel production using catalyzed transesterification

Biodiesel fuel production by transesterification of oils.

Biodiesel processing and production

Industrial applications of microbial lipases

https://seniordesign.engr.uidaho.edu/2007_2008/frenchfryfuel/Biodiesel%20from%20WVO%20Part%201.pdf

Biodiesel production from waste cooking oil: 1. Process design and technological assessment

Saccharomyces cerevisiae bearing a lipase cDNA from Fusarium heterosporum produced two lipases, A and B. Lipase B was significantly more stable to temperature than lipase A, but their optimum temperatures were similar. Lipase B was composed of one polypeptide (301 amino acids), and lipase A was composed of two polypeptides (275 and 26 amino acids) generated by the cleavage between Arg275 and Asp276 with a trypsin-like protease. It was suggested that the C-terminal peptide (26 amino acids) tightened the lipase structure when bound to the catalytic domain (275 amino acids) through a peptide bond. The tight structure was loosened by cleavage of the C-terminal peptide, even though the peptide interacted noncovalently with the catalytic domain, possibly through charged amino acids, in which it is rich. Deletion of the C-terminal peptide greatly decreased the lipase production by the recombinant S. cerevisiae, although its transcriptional level was the same as that of cells carrying the wild-type gene. These facts suggested that the C-terminal peptide affected the lipase production in the post-transcriptional step.

C-Terminal Peptide of Fusarium heterosporum Lipase Is Necessary for Its Increasing Thermostability

Production of Functional Lipids Containing Polyunsaturated Fatty Acids with Lipase

Penicillium abeanum lipase: Purification, characterization, and its use for docosahexaenoic acid enrichment of tuna oil

Characterization of Novel Cholesterol Esterase from Trichoderma sp. AS59 with High Ability to Synthesize Steryl Esters

We attempted to produce MAG of CLA through lipase-catalyzed esterification of a FFA mixture containing CLA (referred to as FFA-CLA) with glycerol. Screening of lipases showed that MAG-CLA was produced efficiently at 5°C with Penicillium camembertii, Rhizopus oryzae, and Candida rugosa lipases. Among them, C. rugosa lipase was selected because the lipase is widely used as a catalyst for oils and fats processing. The reaction was conducted with agitation of a 300-g mixture of FFA-CLA/glycerol (1∶5, mol/mol), a 200-U/g mixture of C. rugosa lipase, and 2% water. When the reaction was conducted at 30°C, the esterification scarcely proceeded, owing to inhibition of the reaction by glycerol. But the reaction at 5°C eliminated the inhibition and produced MAG efficiently: The degree of esterification reached 93.8% after 58 h, and MAG content in the reaction mixture was 88.4 wt%. To reduce the reaction time, the reactor was connected with a vacuum pump after 24 h, and the reaction was continued with dehydration at 5 mm Hg. The degree of esterification reached 94.7% after 24 h of dehydration (48 h in total), and MAG content increased to 93.0 wt%. Candida rugosa lipase acted a little more strongly on cis-9, trans-11 CLA than on trans-10,cis-12 CLA, but the contents of the two isomers in MAG obtained from a 48-h reaction were the same as the contents in FFA-CLA.

Akio Sugihara

Papers

C-Terminal Peptide of Fusarium heterosporum Lipase Is Necessary for Its Increasing Thermostability

Production of Functional Lipids Containing Polyunsaturated Fatty Acids with Lipase

Penicillium abeanum lipase: Purification, characterization, and its use for docosahexaenoic acid enrichment of tuna oil

Characterization of Novel Cholesterol Esterase from Trichoderma sp. AS59 with High Ability to Synthesize Steryl Esters

Production of MAG of CLA in a solvent-free system at low temperature with Candida rugosa lipase