Kinetics of lipase-catalyzed hydrolysis of palm oil in lecithin/izooctane reversed micellles
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1998
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Candida rugosa lipase has been used to investigate the hydrolysis of palm oil in a lecithin/isooctane reversed micellar system. The reaction obeys Michaelis-Menten kinetics for the initial conditions. Kinetic parameters such as maximum rate and Michaelis constant (K-m) were determined for lipase-catalyzed hydrolysis in n-hexane and isooctane. According to the K-m values, the enzyme affinity towards the substrate was increased in isooctane. The maximum degree of hydrolysis was generally decreased as the initial substrate concentration was increased. This may suggest that the hydrolysis in lecithin reversed micelles should be regarded as a one-substrate first-order reversible reaction. It is shown in this study that the proposed one-substrate first-order kinetic model can serve for the precise prediction of the degree of hydrolysis for a known reaction time or vice versa, when the initial substrate concentration is less than 0.325 mol/dm(3). A disagreement with this model was found when ...the initial substrate concentration was higher than approximately 0.3 mol/dm(3). This may be due to the effects of the products on lipase activity or even to the conversion of the reversed micellar system to other systems.
Izvor:
Applied Microbiology and Biotechnology, 1998, 49, 3, 267-271Izdavač:
- Springer, New York
DOI: 10.1007/s002530051167
ISSN: 0175-7598
WoS: 000073117700004
Scopus: 2-s2.0-0031893209
Institucija/grupa
Tehnološko-metalurški fakultetTY - JOUR AU - Knežević, Zorica AU - Šiler-Marinković, Slavica AU - Mojović, Ljiljana PY - 1998 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/187 AB - Candida rugosa lipase has been used to investigate the hydrolysis of palm oil in a lecithin/isooctane reversed micellar system. The reaction obeys Michaelis-Menten kinetics for the initial conditions. Kinetic parameters such as maximum rate and Michaelis constant (K-m) were determined for lipase-catalyzed hydrolysis in n-hexane and isooctane. According to the K-m values, the enzyme affinity towards the substrate was increased in isooctane. The maximum degree of hydrolysis was generally decreased as the initial substrate concentration was increased. This may suggest that the hydrolysis in lecithin reversed micelles should be regarded as a one-substrate first-order reversible reaction. It is shown in this study that the proposed one-substrate first-order kinetic model can serve for the precise prediction of the degree of hydrolysis for a known reaction time or vice versa, when the initial substrate concentration is less than 0.325 mol/dm(3). A disagreement with this model was found when the initial substrate concentration was higher than approximately 0.3 mol/dm(3). This may be due to the effects of the products on lipase activity or even to the conversion of the reversed micellar system to other systems. PB - Springer, New York T2 - Applied Microbiology and Biotechnology T1 - Kinetics of lipase-catalyzed hydrolysis of palm oil in lecithin/izooctane reversed micellles EP - 271 IS - 3 SP - 267 VL - 49 DO - 10.1007/s002530051167 ER -
@article{ author = "Knežević, Zorica and Šiler-Marinković, Slavica and Mojović, Ljiljana", year = "1998", abstract = "Candida rugosa lipase has been used to investigate the hydrolysis of palm oil in a lecithin/isooctane reversed micellar system. The reaction obeys Michaelis-Menten kinetics for the initial conditions. Kinetic parameters such as maximum rate and Michaelis constant (K-m) were determined for lipase-catalyzed hydrolysis in n-hexane and isooctane. According to the K-m values, the enzyme affinity towards the substrate was increased in isooctane. The maximum degree of hydrolysis was generally decreased as the initial substrate concentration was increased. This may suggest that the hydrolysis in lecithin reversed micelles should be regarded as a one-substrate first-order reversible reaction. It is shown in this study that the proposed one-substrate first-order kinetic model can serve for the precise prediction of the degree of hydrolysis for a known reaction time or vice versa, when the initial substrate concentration is less than 0.325 mol/dm(3). A disagreement with this model was found when the initial substrate concentration was higher than approximately 0.3 mol/dm(3). This may be due to the effects of the products on lipase activity or even to the conversion of the reversed micellar system to other systems.", publisher = "Springer, New York", journal = "Applied Microbiology and Biotechnology", title = "Kinetics of lipase-catalyzed hydrolysis of palm oil in lecithin/izooctane reversed micellles", pages = "271-267", number = "3", volume = "49", doi = "10.1007/s002530051167" }
Knežević, Z., Šiler-Marinković, S.,& Mojović, L.. (1998). Kinetics of lipase-catalyzed hydrolysis of palm oil in lecithin/izooctane reversed micellles. in Applied Microbiology and Biotechnology Springer, New York., 49(3), 267-271. https://doi.org/10.1007/s002530051167
Knežević Z, Šiler-Marinković S, Mojović L. Kinetics of lipase-catalyzed hydrolysis of palm oil in lecithin/izooctane reversed micellles. in Applied Microbiology and Biotechnology. 1998;49(3):267-271. doi:10.1007/s002530051167 .
Knežević, Zorica, Šiler-Marinković, Slavica, Mojović, Ljiljana, "Kinetics of lipase-catalyzed hydrolysis of palm oil in lecithin/izooctane reversed micellles" in Applied Microbiology and Biotechnology, 49, no. 3 (1998):267-271, https://doi.org/10.1007/s002530051167 . .