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Study of enzymatic esterification in a solvent system with and without adsorptive control of water with molecular sieves (CROSBI ID 481416)

Prilog sa skupa u zborniku | sažetak izlaganja sa skupa | međunarodna recenzija

Giacometti, Jasminka ; Milin, Čedomila ; Vasić-Rački, Đurđa ; Giacometti, Fabio Study of enzymatic esterification in a solvent system with and without adsorptive control of water with molecular sieves // 10th European Congress on Biotechnology "Biotechnological Challenges in the new Millennium" : abstracts / Perez Mellado, Rafael (ur.). Madrid: Sebiot, 2001. str. 213-213

Podaci o odgovornosti

Giacometti, Jasminka ; Milin, Čedomila ; Vasić-Rački, Đurđa ; Giacometti, Fabio

engleski

Study of enzymatic esterification in a solvent system with and without adsorptive control of water with molecular sieves

Enzymatic esterification of glycerol with oleic acid was carried out in equimolar ratio and catalyzed by immobilized Mucor miehei lipase in a solvent system. The effects of organic solvents, versus log P value, molecular sieves and temperatures were investigated. Lipase catalyzed esterification of glycerol with oleic acid in a solvent system was carried out with 6.67 mg/ml immobilized Mucor miehei lipase at 25, 37 and 50oC, using n-hexane, cyclohexane and isooctane, without and by adding 40 mg/ml of 5Ĺ molecular sieves at the start of esterification, at 100 rpm, in a batch stirrer-tank reactor (BSTR). The reactions were followed by the determination of reaction conversions during 45 hrs. The assay of enzyme reaction was performed by measurement with the pH-stat method and simultaneously monitored by the determination of free oleic acid, monoolein and diolein by gas chromatography method . The highest reaction rates were obtained in nonpolar tested solvents. Changing the system hydrophobicity, by using tested organic solvents, influenced the initial rate conversion but had no affect on the final equilibrium conversion. Changing the tested reaction temperature in the system with molecular sieves, major changes on the initial rate conversion were found at 25oC, but had no affect on the final equilibrium conversion. After 28 h no reaction products were observed with lipase from Pseudomonas cepacia (PS-C and PS-D). The comparison of the used reaction conditions showed the optimal lipase activity in the presence of n-hexane and molecular sieves at 37oC.

enzyme-catalyzed esterification; adsorptive control of water; molecular sieves; solvent system; Lipozym

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Podaci o prilogu

213-213.

2001.

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objavljeno

Podaci o matičnoj publikaciji

10th European Congress on Biotechnology "Biotechnological Challenges in the new Millennium" : abstracts

Perez Mellado, Rafael

Madrid: Sebiot

Podaci o skupu

European Congress on Biotechnology "Biotechnological Challenges in the new Millennium" (10 ; 2001)

poster

08.07.2001-11.07.2001

Madrid, Španjolska

Povezanost rada

Kemijsko inženjerstvo, Farmacija, Prehrambena tehnologija