Results 201 to 210 of about 24,463 (245)
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Lipase immobilization on biodegradable film with sericin
Biotechnology and Applied Biochemistry, 2021AbstractAn ecofriendly and low‐cost film composed by cassava starch, polyvinyl alcohol, and sericin blend (CS–PVA–SS) was synthesized, characterized, and applied as a novel support for Botryosphaeria ribis EC‐01 lipase immobilization by enzyme–film–enzyme adsorption. Film revealed thickness between 230 and 309 μm and higher flexibility and malleability
Michael da Conceição de Castro +6 more
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Polymeric membranes for lipase immobilization
Journal of the American Oil Chemists' Society, 1990Lipase triacylglycerol acylhydrolase, (E.C. 3.1.1.3) is an enzyme that is fully active on aggregated substrates and practically inactive on monodisperse systems. A lipase immobilized on polymeric membranes has been applied for sunflower oil hydrolysis. The influence of membrane properties on enzyme activity is studied.
Magdalena Rucka +2 more
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Macroporous Beads for Lipase Immobilization
Journal of Bioactive and Compatible Polymers, 2007Lipase isolated from Arthrobacter sp. (RRLJ-1, MTCC No. 5125, named ABL), is effective in resolving a wide range of racemic drug intermediates. In this study, ABL was immobilized on a series of synthetic macroporous epoxy copolymers beads with varying pore sizes, surface area and hydrophobicity.
Indu Bhushan +7 more
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Silanized palygorskite for lipase immobilization
Journal of Molecular Catalysis B: Enzymatic, 2009Abstract Lipase from Candida lipolytica has been immobilized on 3-aminopropyltriethoxysilane-modified palygorskite support. Scanning electron micrographs proved the covalently immobilization of C. lipolytica lipase on the palygorskite support through glutaraldehyde.
Jianhua Huang, Yuanfa Liu, Xingguo Wang
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Covalent immobilization of lipase in organic solvents
Biotechnology and Bioengineering, 1989AbstractLipase from Rhizopus sp. has been immobilized covalently on tresyl activated silica. Three different coupling media were evaluated: aqueous buffer, n‐hexane, and a microemulsion based on n‐hexane, aqueous buffer, and the nonionic surfactant triethylene glycol monododecyl ether.
M B, Stark, K, Holmberg
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Ultrafiltration membranes as carriers for lipase immobilization
Enzyme and Microbial Technology, 1990The feasibility of directly incorporating lipase from Rhizopus in the interior of poly(vinyl chloride) ultrafiltration membranes during the phase inversion process for their manufacturing has been demonstrated. The obtained membranes used for plant oil hydrolysis have shown better time stability as compared with those of lipase immobilized by ...
M, Rucka, B, Turkiewicz
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Biodiesel production by transesterification using immobilized lipase
Biotechnology Letters, 2012Biodiesel can be produced by transesterification of vegetable or waste oil catalysed by lipases. Biodiesel is an alternative energy source to conventional fuel. It combines environmental friendliness with biodegradability, low toxicity and renewability.
Sunil Kumar, Narwal, Reena, Gupta
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Lipase-immobilized biocatalytic membranes for biodiesel production
Bioresource Technology, 2013Microbial lipase from Candida rugosa (Amano AY-30) has good transesterification activity and can be used for biodiesel production. In this study, polyvinylidene fluoride (PVDF) membrane was grafted with 1,4-diaminobutane and activated by glutaraldehyde for C. rugosa lipase immobilization.
Chia-Hung, Kuo +4 more
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Lipases: sources, immobilization methods, and industrial applications
Applied Microbiology and Biotechnology, 2019Enzymes are natural catalysts highly specific to the substrate type and operate under mild conditions of temperature, pressure, and pH with high conversion rates, which makes them more efficient than conventional chemical catalysts. The enzymes can be obtained from various sources, animal, vegetable, and microbiological.
Danielle Gonçalves, Filho +2 more
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Stereospecific hydrolysis by soluble and immobilized lipases
Biotechnology and Bioengineering, 1982AbstractStereospecific hydrolysis of insoluble monoesters by lipases are reported. Among the lipases tested, porcine pancreatic lipase was the most stereospecific when acting on 3‐chloro–2‐methyl propanol propionate. When the chain length of the acid was enhanced, the stereospecificity decreased.
J, Lavayre, J, Verrier, J, Baratti
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