Lipase from Candida rugosa was immobilized by adsorption onto a macroporous copolymer support. Under optimum conditions the maximum amount of protein bound was 15.4 mg/g and the immobilization efficiency was 62%. The kinetics of lipase binding to the selected polymer carrier was assessed by using a general model of topochemical reactions. The effect of temperature on adsorption was thoroughly investigated, as was the adsorption mechanism itself Analysis of the proposed kinetic model and the specific kinetic parameters measured suggest that surface kinetics control the adsorption process. According to the activation energy (E-a) and the rate constant, k, the enzyme has rather a high affinity for the support's active sites. The immobilized enzyme was used to catalyse the hydrolysis of palm oil in a lecithin/isooctane reaction system, in which the enzyme's activity was 70% that of the free enzyme. Kinetic parameters such as maximum velocity (V-max) and the Michaelis constant (K-m) were de...termined for the free and the immobilized lipase. Following repeated use, the immobilized lipase retained 56% of its initial activity after the fifth hydrolysis cycle.
Source:
Applied Microbiology and Biotechnology, 1998, 50, 6, 676-681
TY - JOUR
AU - Mojović, Ljiljana
AU - Knežević, Zorica
AU - Popadić, R
AU - Jovanović, S
PY - 1998
UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/201
AB - Lipase from Candida rugosa was immobilized by adsorption onto a macroporous copolymer support. Under optimum conditions the maximum amount of protein bound was 15.4 mg/g and the immobilization efficiency was 62%. The kinetics of lipase binding to the selected polymer carrier was assessed by using a general model of topochemical reactions. The effect of temperature on adsorption was thoroughly investigated, as was the adsorption mechanism itself Analysis of the proposed kinetic model and the specific kinetic parameters measured suggest that surface kinetics control the adsorption process. According to the activation energy (E-a) and the rate constant, k, the enzyme has rather a high affinity for the support's active sites. The immobilized enzyme was used to catalyse the hydrolysis of palm oil in a lecithin/isooctane reaction system, in which the enzyme's activity was 70% that of the free enzyme. Kinetic parameters such as maximum velocity (V-max) and the Michaelis constant (K-m) were determined for the free and the immobilized lipase. Following repeated use, the immobilized lipase retained 56% of its initial activity after the fifth hydrolysis cycle.
PB - Springer, New York
T2 - Applied Microbiology and Biotechnology
T1 - Immobilization of lipase from Candida rugosa on a polymer support
EP - 681
IS - 6
SP - 676
VL - 50
DO - 10.1007/s002530051350
ER -
@article{
author = "Mojović, Ljiljana and Knežević, Zorica and Popadić, R and Jovanović, S",
year = "1998",
abstract = "Lipase from Candida rugosa was immobilized by adsorption onto a macroporous copolymer support. Under optimum conditions the maximum amount of protein bound was 15.4 mg/g and the immobilization efficiency was 62%. The kinetics of lipase binding to the selected polymer carrier was assessed by using a general model of topochemical reactions. The effect of temperature on adsorption was thoroughly investigated, as was the adsorption mechanism itself Analysis of the proposed kinetic model and the specific kinetic parameters measured suggest that surface kinetics control the adsorption process. According to the activation energy (E-a) and the rate constant, k, the enzyme has rather a high affinity for the support's active sites. The immobilized enzyme was used to catalyse the hydrolysis of palm oil in a lecithin/isooctane reaction system, in which the enzyme's activity was 70% that of the free enzyme. Kinetic parameters such as maximum velocity (V-max) and the Michaelis constant (K-m) were determined for the free and the immobilized lipase. Following repeated use, the immobilized lipase retained 56% of its initial activity after the fifth hydrolysis cycle.",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "Immobilization of lipase from Candida rugosa on a polymer support",
pages = "681-676",
number = "6",
volume = "50",
doi = "10.1007/s002530051350"
}
Mojović, L., Knežević, Z., Popadić, R.,& Jovanović, S.. (1998). Immobilization of lipase from Candida rugosa on a polymer support. in Applied Microbiology and Biotechnology
Springer, New York., 50(6), 676-681.
https://doi.org/10.1007/s002530051350
Mojović L, Knežević Z, Popadić R, Jovanović S. Immobilization of lipase from Candida rugosa on a polymer support. in Applied Microbiology and Biotechnology. 1998;50(6):676-681.
doi:10.1007/s002530051350 .
Mojović, Ljiljana, Knežević, Zorica, Popadić, R, Jovanović, S, "Immobilization of lipase from Candida rugosa on a polymer support" in Applied Microbiology and Biotechnology, 50, no. 6 (1998):676-681,
https://doi.org/10.1007/s002530051350 . .
