142-77-8Relevant academic research and scientific papers
Esterification activity and stability of Talaromyces thermophilus lipase immobilized onto chitosan
Romdhane, Ines Belhaj-Ben,Romdhane, Zamen Ben,Gargouri, Ali,Belghith, Hafedh
, p. 230 - 239 (2011)
The Talaromyces thermophilus lipase (TTL) was immobilized by different methods namely adsorption, ionic binding and covalent coupling, using various carriers. Chitosan, pre-treated with glutaraldehyde, was selected as the most suitable support material preserving the catalytic activity almost intact and offering maximum immobilization capacity (76% and 91%, respectively). The chitosan-immobilized lipase could be reputably used for ten cycles with more than 80% of its initial hydrolytic activity. Shift in the optimal temperature from 50 to 60 °C and in the pH from 9.5 to 10, were observed for the immobilized lipase when compared to the free enzyme. The catalytic esterification of oleic acid with 1-butanol has been carried out using hexane as organic solvent. A high performance synthesis of 1-butyl oleate was obtained (95% of conversion yield) at 60 °C with a molar ratio of 1:1 oleic acid to butanol and using 100 U (0.2 g) of immobilized lipase. The esterification product is analysed by GC/MS to confirm the conversion percentage calculated by titration.
Two-phase (bio)catalytic reactions in a table-top centrifugal contact separator
Kraai, Gerard N.,Van Zwol, Floris,Schuur, Boelo,Heeres, Hero J.,De Vries, Johannes G.
, p. 3905 - 3908 (2008)
(Figure Presented) A new spin on catalysis: A table-top centrifugal contact separator allows for fast continuous two-phase reactions to be performed by intimately mixing two immiscible phases and then separating them. Such a device has been used to produce biodiesel from sunflower oil and MeOH/NaOMe. A lipase-catalyzed esterification of oleic acid with nBuOH (see picture) also proceeds with high conversion and can be run for up to 13 h.
Self-assembled lipase nanosphere templated one-pot biogenic synthesis of silica hollow spheres in ionic liquid [Bmim][PF6]
Sarkar, Sampa,Mantri, Kshudiram,Kumar, Dinesh,Bhargava, Suresh K.,Soni, Sarvesh K.
, p. 105800 - 105809 (2015)
The spontaneous self-assembly of hydrophobic enzymatic protein triacylglycerol acylhydrolase (commonly known as lipase and a member of the serine hydrolase family) in hydrophobic 1-butyl-3-methylimidazolium hexafluorophosphate [Bmim][PF6] and in hydrophilic 1-butyl-3-methylimidazolium tetrafluoroborate [Bmim][BF4] ionic liquids resulted in the formation of lipase enzyme nanocapsules of different morphology. The lipase enzyme capsules were found to retain varying enzyme activity in both cases with both kinds of lipase capsules acting as self-catalyzing functional templates for the hydrolysis of silica precursors into silica. The presence of silica and its interaction with biomolecules was proved by X-ray Photoemission Spectroscopy (XPS). Interestingly, hollow silica spheres were obtained in the case of [Bmim][PF6] ionic liquid, while solid silica spheres were obtained in the case of [Bmim][BF4] ionic liquid for the same enzyme. The structural orientation of the enzyme within the capsules, their functional templating to obtain silica particles of varying morphology and finally their combined catalytic activity depend on the initial lipase-ionic liquid interaction. The enzyme activity of all these materials was evaluated against the esterification reaction between oleic acid (fatty acid) and butanol, i.e. biodiesel production. The relative enzyme activity was found to be 93.30% higher in the case of lipase nanocapsules synthesized in [Bmim][PF6] and its in situ templating action to make hollow silica spheres further enhanced the residual activity. Furthermore time dependent kinetics of esterification by hollow silica spheres has also been shown here. Hollow silica spheres can also be used as a reusable catalyst for up to 6 cycles. This work demonstrates that the choice of ionic liquid is critical in controlling the self-assembly of enzymes as the ionic liquid-enzyme interaction plays a major role in retaining capsule activity and enzyme function.
Esterification and interesterification reactions catalyzed by acetone powder from germinating rapeseed
Jachmanian,Mukherjee
, p. 1527 - 1532 (1996)
Acetone powder from germinating rape (Brassica napus L.) seedlings exhibits essentially similar activity in lipolysis of triacylglycerols as the corresponding seedling homogenates. Acetone powder from rape seedlings catalyzes the esterification of a fatty acid, such as oleic acid, with n-butanol or a long-chain alcohol, such as oleyl alcohol. Furthermore, the acetone powder catalyzes alcoholysis of a methyl ester, such as methyl oleate with n-butanol or oleyl alcohol, and acidolysis of methyl oleate with a fatty acid, such as erucic acid. However, triacylglycerols are not accepted as substrates for interesterification reactions. In esterification of fatty acids with n-butanol, catalyzed by the acetone powder from rape seedlings, fatty acids having an olefinic bond next to the carboxyl group as a cis-6 double bond, e.g., γ-linolenic, gorlic and petroselinic acids, or those having a cis-4 double bond, e.g., docosahexaenoic acid, are strongly discriminated against as substrates. Such substrate selectivities can be utilized for the enrichment of definite fatty acids from mixtures, derived from naturally occurring oils, via kinetic resolution.
Immobilization of Rhizopus oryzae lipase on silica aerogels by adsorption: Comparison with the free enzyme
Kharrat, Nadia,Ali, Yassine Ben,Marzouk, Sana,Gargouri, Youssef-Talel,Karra-Chaabouni, Maha
, p. 1083 - 1089 (2011)
Rhizopus oryzae lipase (ROL) was immobilized by physical adsorption onto silica aerogels. The functional properties of immobilized lipase were determined and compared to the soluble lipase ones. The optimum temperature for both free and immobilized lipase activities was 37 °C. We found that the immobilization of R. oryzae lipase onto silica aerogels increased remarkably its stability at high temperatures and within a wade pH range. Besides the immobilized enzyme exhibited a high tolerance to apolar solvent and retained its fully activity in suspension after 4 months of storage at 4 °C. This immobilized biocatalyst is applied in n-butyl oleate synthesis by esterification of oleic acid with n-butanol, using hexane as an organic solvent. The best conversion yield of the ester butyl oleate was obtained with the immobilized lipase (80% versus 35% with the free lipase). This catalytic esterification has been carried on the presence of hexane at 37 °C with oleic acid to butanol molar ratio of 1:1 and 450 IU of immobilized lipase. Furthermore, the reuse of the lipase immobilized by adsorption allowed us to observe that its can achieved 12 successive cycles, without a significant loss of its catalytic activity. Such results revealed good potential for recycling under non-aqueous system.
Chemically Modified Lipase from Thermomyces lanuginosus with Enhanced Esterification and Transesterification Activities
Noro, Jennifer,Cavaco-Paulo, Artur,Silva, Carla
, p. 4524 - 4531 (2021/09/02)
Lipase from Thermomyces lanuginosus is one of the most explored enzymes for the esterification of several added-value industrial compounds, such as biodiesel, fragrances, and flavors. Its selectivity in these reactions is mostly related with its activity towards small alcohols. In this work, the impact of the chemical modification, with 4 dodecyl chains at its surface, was evaluated regarding its transesterification and esterification activities, comparing with the native form. Linear size-differentiated alcohols (from 1 to 20 carbons in the aliphatic chain) were used to explore for the first time the effect of the chain length in both transesterification and esterification reactions, using p-nitrophenyl palmitate and oleic acid as model compounds, respectively. The chemically modified lipase showed an outstanding improvement of its catalytic performance than the native enzyme, being this increase directly proportional to the size of the alcohols chain used as substrates. The enormous potential and remarkable versatility of this novel super catalyst was here demonstrated, where diverse types of esters, differing in their potential applications (biodiesel, cosmetics, fine chemistry), were efficiently synthesized. The produced esters were fully characterized by 1H NMR, GC-MS, and FTIR.
Method for catalyzed synthesis of butyl oleate with oleic acid-based ionic liquid microemulsion
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Paragraph 0031-0050, (2019/07/04)
The invention discloses a method for catalyzed synthesis of butyl oleate with an oleic acid-based ionic liquid microemulsion. The method comprises the following steps: (1) at 25-35 DEG C, uniformly mixing a surfactant with an imidazole disulfate ionic liquid so as to obtain a surfactant mixed solution, further uniformly mixing with oleic acid and n-butyl alcohol, finally adding an imidazole fluoborate ionic liquid, and stirring so as to obtain an oleic acid-based ionic liquid microemulsion; (2) putting the oleic acid-based ionic liquid microemulsion of the step (1) into a nitrogen atmosphere,heating, stirring to carry out reactions, separating, and purifying, thereby obtaining butyl oleate. The reaction process is gentle in condition, no conventional toxic organic solvent (such as cyclohexane and methylbenzene) except reactants is used, the idea of green and environment protection can be met, the product can be easily separated, and the product is light yellow or golden yellow and ishigh in yield.
Development and Validation of a Novel Free Fatty Acid Butyl Ester Gas Chromatography Method for the Determination of Free Fatty Acids in Dairy Products
Mannion, David T.,Furey, Ambrose,Kilcawley, Kieran N.
, p. 499 - 506 (2019/01/08)
Accurate quantification of free fatty acids in dairy products is important for both product quality control and legislative purposes. In this study, a novel fatty acid butyl ester method was developed, where extracted free fatty acids are converted to butyl esters prior to gas chromatography with flame ionization detection. The method was comprehensively validated to establish linearity (20-700 mg/L; R2 > 0.9964), limits of detection (5-8 mg/L), limits of quantification (15-20 mg/L), accuracy (1.6-5.4% relative error), interday precision (4.4-5.3% relative standard deviation), and intraday precision (0.9-5.6% relative standard deviation) for each individual free fatty acid. A total of 17 dairy samples were analyzed, covering diverse sample matrices, fat content, and degrees of lipolysis. The method was compared to direct on-column injection and fatty acid methyl ester methods and overcomes limitations associated with these methods, such as either column-phase absorption or deterioration, accurate quantification of short-chain free fatty acids, and underestimation of polyunsaturated free fatty acid.
Evolving the Promiscuity of Elizabethkingia meningoseptica Oleate Hydratase for the Regio- and Stereoselective Hydration of Oleic Acid Derivatives
Engleder, Matthias,Strohmeier, Gernot A.,Weber, Hansj?rg,Steinkellner, Georg,Leitner, Erich,Müller, Monika,Mink, Daniel,Schürmann, Martin,Gruber, Karl,Pichler, Harald
, p. 7480 - 7484 (2019/04/27)
The addition of water to non-activated carbon–carbon double bonds catalyzed by fatty acid hydratases (FAHYs) allows for highly regio- and stereoselective oxyfunctionalization of renewable oil feedstock. So far, the applicability of FAHYs has been limited to free fatty acids, mainly owing to the requirement of a carboxylate function for substrate recognition and binding. Herein, we describe for the first time the hydration of oleic acid (OA) derivatives lacking this free carboxylate by the oleate hydratase from Elizabethkingia meningoseptica (OhyA). Molecular docking of OA to the OhyA 3D-structure and a sequence alignment uncovered conserved amino acid residues at the entrance of the substrate channel as target positions for enzyme engineering. Exchange of selected amino acids gave rise to OhyA variants which showed up to an 18-fold improved conversion of OA derivatives, while retaining the excellent regio- and stereoselectivity in the olefin hydration reaction.
A method of using waste acid to produce sulfonated oil
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Paragraph 0033-0034; 0040, (2017/07/05)
The invention provides a method for using waste acid to produce sulfonated oil. The method includes: after the second-step sulponation reaction during a penetrant BX production process, cooling and standing materials to normal temperature, standing for layering, and separating the waste acid from reaction products; placing the waste acid into a suction filtration barrel for suction filtration to allow a small amount of naphthalene sulfonic acid mixed into the waste acid to be reserved on filter cloth so as to obtain waste acid, namely waste sulfuric acid with sulfuric acid mass concentration of about 80%; using the waste sulfuric acid as sulfonating agent sulfonated oil DAH production to perform sulponation reaction; wherein the mole ratio of the waste sulfuric acid after being converted into sulfuric acid with the mass concentration of 100% to butyl oleate is 1.05-1.1:1. By the method, cost is lowered, resources are utilized, and environments are protected.
