The Candida rugosa lipase catalyzed synthesis of amyl isobutyrate in organic solvent and solvent-free system: A kinetic study
Само за регистроване кориснике
2006
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
The Candida rugosa lipase catalyzed esterification of butyric acid with amyl alcohol in isooctane and in solvent-free system was studied. Nearly complete conversion ( gt 95%) of substrates was achieved using low enzyme amount of 0.5% (w/v) at 45 degrees C. The initial rates of esterification were attempted to correlate with concentrations of substrates by various bisubstrate kinetic models. The reaction rate of esterification in isooctane could be described with a ping-pong bi-bi mechanism and inhibition by amyl alcohol. Obtained specificity constants indicate that lipase from C. rugosa has higher affinity towards acid substrate. The rate of esterification in solvent-free system could not be described with applied bisubstrate models probably due to denaturation of lipase in absence of solvent at high concentrations of both substrates. Nevertheless, the maximum initial rate in solvent-free system was higher than corresponding values in isooctane which indicates that solvent-free system... has good perspectives for industrial utilization at lower S/E ratios.
Кључне речи:
Candida rugosa lipase / ping-pong bi-bi kinetics / alcohol inhibition / amyl isobutyrate / esterificationИзвор:
Journal of Molecular Catalysis B-Enzymatic, 2006, 38, 1, 11-16Издавач:
- Elsevier, Amsterdam
DOI: 10.1016/j.molcatb.2005.10.004
ISSN: 1381-1177
WoS: 000235006200002
Scopus: 2-s2.0-29744436242
Институција/група
Tehnološko-metalurški fakultetTY - JOUR AU - Bezbradica, Dejan AU - Mijin, Dušan AU - Šiler-Marinković, Slavica AU - Knežević, Zorica PY - 2006 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/914 AB - The Candida rugosa lipase catalyzed esterification of butyric acid with amyl alcohol in isooctane and in solvent-free system was studied. Nearly complete conversion ( gt 95%) of substrates was achieved using low enzyme amount of 0.5% (w/v) at 45 degrees C. The initial rates of esterification were attempted to correlate with concentrations of substrates by various bisubstrate kinetic models. The reaction rate of esterification in isooctane could be described with a ping-pong bi-bi mechanism and inhibition by amyl alcohol. Obtained specificity constants indicate that lipase from C. rugosa has higher affinity towards acid substrate. The rate of esterification in solvent-free system could not be described with applied bisubstrate models probably due to denaturation of lipase in absence of solvent at high concentrations of both substrates. Nevertheless, the maximum initial rate in solvent-free system was higher than corresponding values in isooctane which indicates that solvent-free system has good perspectives for industrial utilization at lower S/E ratios. PB - Elsevier, Amsterdam T2 - Journal of Molecular Catalysis B-Enzymatic T1 - The Candida rugosa lipase catalyzed synthesis of amyl isobutyrate in organic solvent and solvent-free system: A kinetic study EP - 16 IS - 1 SP - 11 VL - 38 DO - 10.1016/j.molcatb.2005.10.004 ER -
@article{ author = "Bezbradica, Dejan and Mijin, Dušan and Šiler-Marinković, Slavica and Knežević, Zorica", year = "2006", abstract = "The Candida rugosa lipase catalyzed esterification of butyric acid with amyl alcohol in isooctane and in solvent-free system was studied. Nearly complete conversion ( gt 95%) of substrates was achieved using low enzyme amount of 0.5% (w/v) at 45 degrees C. The initial rates of esterification were attempted to correlate with concentrations of substrates by various bisubstrate kinetic models. The reaction rate of esterification in isooctane could be described with a ping-pong bi-bi mechanism and inhibition by amyl alcohol. Obtained specificity constants indicate that lipase from C. rugosa has higher affinity towards acid substrate. The rate of esterification in solvent-free system could not be described with applied bisubstrate models probably due to denaturation of lipase in absence of solvent at high concentrations of both substrates. Nevertheless, the maximum initial rate in solvent-free system was higher than corresponding values in isooctane which indicates that solvent-free system has good perspectives for industrial utilization at lower S/E ratios.", publisher = "Elsevier, Amsterdam", journal = "Journal of Molecular Catalysis B-Enzymatic", title = "The Candida rugosa lipase catalyzed synthesis of amyl isobutyrate in organic solvent and solvent-free system: A kinetic study", pages = "16-11", number = "1", volume = "38", doi = "10.1016/j.molcatb.2005.10.004" }
Bezbradica, D., Mijin, D., Šiler-Marinković, S.,& Knežević, Z.. (2006). The Candida rugosa lipase catalyzed synthesis of amyl isobutyrate in organic solvent and solvent-free system: A kinetic study. in Journal of Molecular Catalysis B-Enzymatic Elsevier, Amsterdam., 38(1), 11-16. https://doi.org/10.1016/j.molcatb.2005.10.004
Bezbradica D, Mijin D, Šiler-Marinković S, Knežević Z. The Candida rugosa lipase catalyzed synthesis of amyl isobutyrate in organic solvent and solvent-free system: A kinetic study. in Journal of Molecular Catalysis B-Enzymatic. 2006;38(1):11-16. doi:10.1016/j.molcatb.2005.10.004 .
Bezbradica, Dejan, Mijin, Dušan, Šiler-Marinković, Slavica, Knežević, Zorica, "The Candida rugosa lipase catalyzed synthesis of amyl isobutyrate in organic solvent and solvent-free system: A kinetic study" in Journal of Molecular Catalysis B-Enzymatic, 38, no. 1 (2006):11-16, https://doi.org/10.1016/j.molcatb.2005.10.004 . .