Book ChapterDOI
Characterization and utilization of Candida rugosa lipase immobilized on controlled pore silica.
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TLDR
Candida rugosa lipase was immobilized by covalent binding on controlled poresilica (CPS) using glutaraldehyde ascross-linking agent under aqueous and nonaqueous conditions and revealed good potential for recycling under ahydrous (olive-oil hydrolysis) andNonaqueous (butyl butyrate synthesis) conditions.Abstract:
Candida rugosa lipase was immobilized by covalent binding on controlled pore silica (CPS) using glutaraldehyde as cross-linking agent under aqueous and nonaqueous conditions. The immobilized C. rugosa was more active when the coupling procedure was performed in the presence of a nonpolar solvent, hexane. Similar optima pH (7.5–8.0) was found for both free and immobilized lipase. The optimum temperature for the immobilized lipase was about 10°C higher than that for the free lipase. The thermal stability of the CPS lipase was also greater than the original lipase preparation. Studies on the operational stability of CPS lipase revealed good potential for recycling under aqueous (olive-oil hydrolysis) and nonaqueous (butyl butyrate synthesis) conditions.read more
Citations
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Journal ArticleDOI
Hydrogen peroxide generation with immobilized glucose oxidase for textile bleaching.
TL;DR: The immobilization technique provided repeated application of the enzyme even in low concentration, and the hydrogen peroxide generated in the enzymatic reaction was successively used for textile bleaching.
Journal ArticleDOI
Preparation of a biocatalyst via physical adsorption of lipase from Thermomyces lanuginosus on hydrophobic support to catalyze biolubricant synthesis by esterification reaction in a solvent-free system
Flávia Arantes Pires Lage,Jaquelinne de Jorge Bassi,Maria Carolina Cucatti Corradini,Larissa Midiane Todero,Jaine H.H. Luiz,Adriano A. Mendes +5 more
TL;DR: Under optimal experimental conditions, reusability tests of the biocatalyst (TLL-PMA) after thirty successive cycles of reaction were performed and the nature of the product (isoamyl oleate) was confirmed by attenuated total reflection Fourier transform infrared (ATR-FTIR), proton ((1)H NMR) and carbon ((13)C N MR) nuclear magnetic resonance spectroscopy analyses.
Journal ArticleDOI
Immobilization and stabilization of microbial lipases by multipoint covalent attachment on aldehyde-resin affinity: Application of the biocatalysts in biodiesel synthesis
Adriano A. Mendes,Adriano A. Mendes,Roberto C. Giordano,Raquel L. C. Giordano,Heizir F. de Castro +4 more
TL;DR: Microbial lipase preparations from Thermomyces lanuginosus and Pseudomonas fluorescens were immobilized by multipoint covalent attachment on Toyopearl AF-amino-650M resin and the most active and thermal stable derivatives used to catalyze the transesterification reaction of babassu and palm oils with ethanol in solvent-free media found to be less active and thermally stable.
Journal ArticleDOI
Evaluation of the catalytic properties of Burkholderia cepacia lipase immobilized on non-commercial matrices to be used in biodiesel synthesis from different feedstocks.
Patrícia Caroline Molgero Da Rós,Guilherme Martins Silva,Adriano A. Mendes,Júlio César dos Santos,Heizir F. de Castro +4 more
TL;DR: The objective of this work was to produce an immobilized form of lipase from Burkholderia cepacia with advantageous catalytic properties and stability to be used in the ethanolysis of different feedstocks, mainly babassu oil and tallow beef.
Journal ArticleDOI
Immobilisation studies and catalytic properties of microbial lipase onto styrene–divinylbenzene copolymer
TL;DR: In this paper, a bacterial lipase from Candida rugosa was immobilised by physical adsorption onto styrene-divinylbenzene (STYDVB) copolymer.
References
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Journal ArticleDOI
Enzymatic catalysis in nonaqueous solvents.
TL;DR: The rate enhancements afforded by chymotrypsin and subtilisin in the transesterification reaction in octane are of the order of 100 billion-fold; covalent modification of the active center of the enzymes by a site-specific reagent renders them catalytically inactive in organic solvents.
Journal ArticleDOI
Bioreactors with immobilized lipases: state of the art.
TL;DR: This review attempts to provide an updated compilation of studies reported in the literature pertaining to reactors containing lipases in immobilized forms, in a way that helps the reader direct a bibliographic search and develop an integrated perspective of the subject.
Journal ArticleDOI
Efficient immobilization of lipases by entrapment in hydrophobic sol-gel materials.
TL;DR: A novel method to achieve lipase immobilization by entrapment in chemically inert hydrophobic silica gels which are prepared by hydrolysis of alkyl‐substituted silanes in the presence of the enzyme is presented.
Journal ArticleDOI
Immobilized lipase reactors for modification of fats and oils—A review
TL;DR: In this paper, the authors focus on the use of immobilized lipase technology to effect ester synthesis and interesterification reactions, and various immobilization procedures, reactor configurations, and process considerations are all reviewed and discussed.
Book
Biocatalysis in Organic Media
TL;DR: The epoxidation of alkenes in water/solvent two-phase systems is discussed to give an example of the scope of biotechnological processes that is obtained by using organic media.