Abstract:
A process for pressure splitting glycerides into fatty acids and glycerols involving the steps of: (a) providing a glyceride feedstock; (b) providing a hydrolytic lipase enzyme; (c) providing an alkaline earth metal selected from the group consisting of calcium, magnesium, and mixtures thereof; (d) mixing components (a)-(c) in the presence of water and with agitation, at a temperature ranging from about 50 to about 60.degree. C. to form a partially hydrolyzed glyceride feedstock; (e) introducing the partially hydrolyzed glyceride feedstock into a pressure splitter; and (f) splitting the partially hydrolyzed glyceride feedstock in the pressure splitter into carboxylic acids and glycerols.
Abstract:
A process for producing fatty acids or fatty acid derivatives from oleaginous plants. This process is characterized in that transgenic oleaginous plants are produced having on the one hand at least one gene coding for a lipase enzyme, the so-called lipase gene, and on the other hand, associated with this lipase gene, a promoter permitting an expression of the gene either in compartments different from the lipid accumulation compartments, or by exogenous induction. The seeds or fruits containing the plant lipids are collected, the seeds or fruits are crushed, if necessary after induction treatment, so as to bring the lipids and lipase into contact, the whole mixture is incubated in order to effect an enzymatic hydrolysis of the lipids, and the fatty acids or derivatives thereof are extracted.
Abstract:
A mutant fungal strain, namely G. candidum NRRL Y-552, mutant known as Henkel 9-2-3-9 produces a lipase called "UNLipase" providing a selectivity of 25:1 for oleic acid over palmitic acid by the assay procedure employed. UNLipase has a temperature range of operation of between 0 and 40 degrees Celsius (and no activity over 55 degrees Celsius). The optimum pH ranges are between 7.5 and 8.5. Magnesium cations increase activity, whereas calcium cations are inhibitory. The molecular weight of the protein appears to be 65 kDa by size exclusion chromatography. UNLipase shows a high degree of selectivity for hydrolysis, esterification and transesterification.
Abstract:
A mutant fungal strain, namely G. candidum NRRL Y-552, mutant known as Henkel 9-2-3-9 produces a lipase called "UNLipase" providing a selectivity of 25:1 for oleic acid over palmitic acid by the assay procedure employed. UNLipase has a temperature range of operation of between 0 and 40 degrees Celsius (and no activity over 55 degrees Celsius). The optimum pH ranges are between 7.5 and 8.5. Magnesium cations increase activity, whereas calcium cations are inhibitory. The molecular weight of the protein appears to be 65 kDa by size exclusion chromatography. UNLipase shows a high degree of selectivity for hydrolysis, esterification and transesterification.
Abstract:
This invention relates to a process for preparation of a novel lipase. The process is characterized by culturing a microorganism belonging to Staphylococcus capitis and capable of producing lipase in a culture medium to accumulate lipase in the cultured broth and recovering the lipase from the broth. Since the pH of this lipase is in a slightly alkali region and the lipase substantially completely converts glyceride to fatty acids and glycerin, it is useful for the economic preparation of fatty acids by the hydrolysis of fats or oils.
Abstract:
A method of increasing production of fatty acids comprising introducing into a host and expressing therein an acyl-acyl carrier protein (ACP) thioesterase (TE) from Bryantella formatexigens or a mutant thereof; a method of making a mutant B. formatexigens acyl-ACP TE; a method of making a chimeric Cuphea viscosissima acyl-ACP TE; a nucleic acid molecule comprising a nucleotide sequence encoding a mutant acyl-ACP TE or a chimeric Cuphea viscosissima acyl-ACP TE; a host comprising the nucleic acid molecule; a mutant acyl-ACP TE or chimeric Cuphea viscosissima acyl-ACP TE; a method of altering the specificity of a plant acyl-ACP TE for at least one of its substrates comprising introducing into the plant acyl-ACP TE a substrate specificity-altering mutation; and a method of altering the level of activity of a plant acyl-ACP TE.
Abstract:
Disclosed herein are methods of manufacturing renewable chemicals through the manufacture of novel triglyceride oils followed by chemical modification of the oils. Methods such as transesterification, hydrogenation, hydrocracking, deoxygenation, isomerization, interesterification, hydroxylation, hydrolysis and saponification are disclosed. Novel oils containing fatty acid chain lengths of C8, C10, C12 or C14 are also disclosed and are useful as feedstocks in the methods of the invention.
Abstract:
The present invention relates to compositions comprising polypeptides having phospholipase C activity and to the use of such compositions for hydrolysing a phospholipid or lysophospholipid, The invention also relates to processes for hydrolysing a phospholipid or lysophospholipid, comprising contacting said phospholipid or lysophospholipid with a composition or a pluralities of polypeptides having Phospholipase C activity according to the invention.
Abstract:
The invention provides hydrolases, polynucleotides encoding them, and methods of making and using these polynucleotides and polypeptides. In one aspect, the invention is directed to polypeptides, e.g., enzymes, having a hydrolase activity, e.g., an esterase, acylase, lipase, phospholipase (e.g., phospholipase A, B, C and D activity, patatin activity, lipid acyl hydrolase (LAH) activity) or protease activity, including thermostable and thermotolerant hydrolase activity, and polynucleotides encoding these enzymes, and making and using these polynucleotides and polypeptides. The hydrolase activities of the polypeptides and peptides of the invention include esterase activity, lipase activity (hydrolysis of lipids), acidolysis reactions (to replace an esterified fatty acid with a free fatty acid), transesterification reactions (exchange of fatty acids between triglycerides), ester synthesis, ester interchange reactions, phospholipase activity and protease activity (hydrolysis of peptide bonds). The polypeptides of the invention can be used in a variety of pharmaceutical, agricultural and industrial contexts, including the manufacture of cosmetics and nutraceuticals. In another aspect, the polypeptides of the invention are used to synthesize enantiomerically pure chiral products.
Abstract:
In an alcohol fermentation process, oil derived from biomass is chemically converted into an extractant available for in situ removal of a product alcohol such as butanol from a fermentation broth. The glycerides in the oil can be chemically converted into a reaction product, such as fatty acids, fatty alcohols, fatty amides, fatty acid methyl esters, fatty acid glycol esters, and hydroxylated triglycerides, and mixtures thereof, which forms a fermentation product extractant having a partition coefficient for a product alcohol greater than a partition coefficient of the oil of the biomass for the product alcohol. Oil derived from a feedstock of an alcohol fermentation process can be chemically converting into the fermentation product extractant. The oil can be separated from the feedstock prior to the feedstock being fed to a fermentation vessel, and the separated oil can be chemically converted to a fermentation product extractant, which can then contacted with a fermentation product comprising a product alcohol, whereby the product alcohol is separated from the fermentation product.