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Enzymatic fatty ester synthesis
Simona Pečnik, Željko Knez, 1992, izvirni znanstveni članek

Opis: Fatty ester synthesis with immobilized 1,3-specific lipase from Mucor Miehei is described. 1,2-Isopropylidene glycerol was peoduced by condensation of glycerol with acetone was esterified with oleic acid in the presence of a Mucor Miehei lipaze (Lipozyme TM) to obtain 1,2 isopropylidene- 3-oleoyl glycerol. The effects of various process parameters (temperature and pressure)and various ratios (enzyme/substrate) have been investigated to determine optimal conditions for the esterification process. The highest conversion of oleic acid (80% w/w) was obtained at 55 oC and 57.057 bar, while the optimal addition of lipase to substrate was determined to be 0,096 g per gram of reaction mixture. The esterification can be modelled successfully as a reverse second order reaction. Thermodynamic properties of the reaction system at 55 oC and 0.057 bar were also determined. Activation energy was 20.82 kJ/mole, entropy of activation -0,26 kJ/(Kmole) and free energy of activation was 103.32 kJ/mole.
Ključne besede: chemical engineering, biotechnology, esterification, syntheses, esters, enzymes, lipase, Mucor miehei, reaction kinetics, reaction thermodynamics, 1, 2-isopropylidene-3-oleoyl glycerol
Objavljeno: 06.06.2012; Ogledov: 1623; Prenosov: 76
URL Povezava na celotno besedilo

Silica aerogels as support for lipase catalyzed esterifications at sub- and supercritical conditions
Zoran Novak, Maja Leitgeb, Vlasta Krmelj, Željko Knez, 2003, izvirni znanstveni članek

Opis: The enzymes (lipases from Candida rugosa and porcine pancreas) were immobilized on silica aerogels by sol-gel procedure followed by supercritical drying with CO2. Such immobilized enzymes were used as biocatalysts for esterification in supercritical CO2 and near critical propane at 40 °C and 100 bar. It was found out that the initial reaction rates in propane rose two to three times in comparison with the same reaction, catalyzed by free lipase. SC CO2 deactivated the non-immobilized lipase in reaction mixture while with the immobilized enzyme the conversion was 35%. The initial reaction rates in propane were 20 times higher than in water medium due to the properties of propane as a medium for esterification of fatty acids.
Ključne besede: chemical processing, biotechnology, esterification, immobilization of enzymes, supercritial CO2, propane, lipases, supercritical CO2 drying
Objavljeno: 01.06.2012; Ogledov: 1330; Prenosov: 20
URL Povezava na celotno besedilo

Decolorization of textile dyes by whole cultures of Ischnoderma Resinosum and by purified laccase and Mn-peroxidase
Vanja Kokol, Aleš Doliška, Ivana Eichlerová, Petr Baldrian, František Nerud, 2007, izvirni znanstveni članek

Opis: Ischnoderma resinosum produced extracellular ligninolytic enzymes laccase and MnP. The activity of laccase achieved the maximum on day 10 (29.4 U L-1), the MnP on day 14 (34.5 U L-1). Laccase and Mn-peroxidase were purified from the culture liquid using gel permeation and ion-exchange chromatographies. Purified Mn-peroxidase performed decolorization of all textile dyes tested (Reactive Black 5, Reactive Blue 19, Reactive Red 22 and Reactive Yellow 15). Laccase was inactive with Reactive Black 5 and Reactive Red 22, while all dyes were decolorized after addition of the redox mediators violuric acid (VA) and hydroxybenzotriazole (HBT). The culture liquid from I. resinosum cultures was also able to decolorize all dyes as well as the synthetic dyebaths in the presence of VA and HBT. The highest decolorization rates were detected in acidic pH (3-4).
Ključne besede: Ischnoderma resinosum, Basidiomycetes, Laccase, Mn-peroxidase, Textile dyes, ligninolytic enzymes
Objavljeno: 01.06.2012; Ogledov: 1223; Prenosov: 69
URL Povezava na celotno besedilo

The influence of enzymatic treatment on wool fibre properties using PEG-modified proteases
Suzana Jus, Marc Schroeder, Georg M. Gübitz, Elisabeth Heine, Vanja Kokol, 2007, izvirni znanstveni članek

Opis: The main contribution of the presented work was to introduce the use of proteases modified with the soluble polymer polyethylene glycol (PEG) in the bio-finishing process of wool fibres, to target enzyme action to the outerparts of wool fibres, i.e. to avoid the diffusion and consequent destroying of the inner parts of the wool fibre structure, in the case of native proteases using. Different proteolytic enzymes from Bacillus lentus and Bacillus subtilis in native and PEG-modified forms were investigated and their influence on the modification of wool fibres morphology surface, chemical structure, as well as the hydrolysis of wool proteins, the physico-mechanical properties, and the sorption properties of 1:2 metal complex dye during dyeing were studied. SEM images of wool fibres confirmed smoother and cleaner fibre surfaces without fibre damages using PEG-modified proteases. Modified enzyme products have a benefit effect on the wool fibres felting behaviours (14%) in the case when PEG-modified B. lentus is used, without markedly fibre damage expressed by tensile strength and weight loss ofthe fibre. Meanwhile the dye exhaustion showed slower but comparable level of dye uptake at the end of the dyeing.
Ključne besede: volnena vlakna, proteolitski encimi, encimske modifikacije, sorpcija barve, morfologija vlaken, wool fibres, proteolytic enzymes, enzyme modification, felting, dye sorption, protein hydrolysis, XPS-analysis, fibre morphology
Objavljeno: 01.06.2012; Ogledov: 2065; Prenosov: 91
URL Povezava na celotno besedilo

A novel metalloprotease from Bacillus cereus for protein fibre processing
Fernanda de Sousa, Suzana Jus, Anita Erbel, Vanja Kokol, Artur Cavaco-Paulo, Georg M. Gübitz, 2007, izvirni znanstveni članek

Opis: A novel protease produced by Bacillus cereus grown on wool as carbon and nitrogen source was purified. B. cereus protease is a neutral metalloprotease with a molecular mass of 45.6 kDa. The optimum activity was at 45 °C and pH 7.0. The substrate specificity was assessed using oxidized insulin B-chain and synthetic peptide substrates. The cleavage of the insulin B-chain was determined to be Asn3, Leu6, His10-Leu11, Ala14, Glu21, after 12 h incubation. Among the peptide substrates, the enzyme did not exhibit activity towards ester substrates; with p-nitroanilide, the kinetic data indicate that aliphatic and aromatic amino acids were the preferred residues at the P1 position. For furylacryloyl peptides substrates, which are typical substrates for thermolysin, the enzyme exhibited high hydrolytic activity with a Km values of 0.858 and 2.363 mM for N-(3-[2-Furyl]acryloyl)-Ala-Phe amide and N-(3-[2-Furyl]acryloyl)-Gly-Leu amide, respectively. The purified protease hydrolysed proteins substrates such as azocasein, azocoll, keratin azure and wool.
Ključne besede: textile finishing, enzymatic modification, wool fibre, enzymes, Bacilus cereus, specificity, kinetics, metalloprotease
Objavljeno: 01.06.2012; Ogledov: 1422; Prenosov: 83
URL Povezava na celotno besedilo

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