Immobilization of Candida rugosa lipase by adsorption onto biosafe meso/macroporous silica and zirconia
Samo za registrovane korisnike
2015
Autori
Zivković, Lidija T. IzraelŽivković, Ljiljana
Babić, Biljana M.
Kokunešoski, Maja
Jokić, Bojan M.
Karadzic, Ivanka M.
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
Lipase from Candida rugosa was immobilized by adsorption onto laboratory prepared supports, silica SBA-15 and zirconia. The adsorption process was studied as a function of pH in terms of percent of adsorbed lipase, enzyme activity and zeta potential of support and enzyme. Several analytical approaches such as laser Doppler electrophoresis, Fourier transform infrared spectroscopy (FTIR) and field emission scanning electron microscopy (FESEM) showed that the lipase was successfully immobilized onto both supports. The zeta-potential data suggest that the adsorption efficiency does not depends on the sign but on the magnitude of the surface charge of adsorption partners, and therefore underline the importance of their dispersion stability. Adsorption to material surface altered enzyme characteristics. nu(max), for the lipase immobilized onto silica and zirconia were 4.8-fold and 3.6-fold lower than that of the free lipase, respectively. The Km showed no alteration of enzyme-substrate affin...ity on zirconia support, whereas the enzyme immobilized on silica had 3.6 times lower affinity. Thermostability at 60 degrees C of the lipase was improved 12-fold on zirconia and 4-fold on silica. Finally, in examining reusability, the immobilized lipase retained more than 90% of initial activity after eight reuses on both supports. (C) 2014 Elsevier B.V. All rights reserved.
Ključne reči:
Immobilization / Adsorption / Lipase / SBA-15 / Zirconia / Kinetic parametersIzvor:
Biochemical Engineering Journal, 2015, 93, 73-83Izdavač:
- Elsevier B.V.
Finansiranje / projekti:
- Sinteza, procesiranje i karakterizacija nanostrukturnih materijala za primenu u oblasti energije, mehaničkog inženjerstva, zaštite životne stredine i biomedicine (RS-45012)
- Simultana bioremedijacija i soilifikacija degradiranih prostora, za očuvanje prirodnih resursa biološki aktivnih supstanci i razvoj i proizvodnju biomaterijala i dijetetskih proizvoda (RS-43004)
DOI: 10.1016/j.bej.2014.09.012
ISSN: 1369-703X; 1873-295X
WoS: 000347362100010
Scopus: 2-s2.0-84908582649
Institucija/grupa
Tehnološko-metalurški fakultetTY - JOUR AU - Zivković, Lidija T. Izrael AU - Živković, Ljiljana AU - Babić, Biljana M. AU - Kokunešoski, Maja AU - Jokić, Bojan M. AU - Karadzic, Ivanka M. PY - 2015 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/5758 AB - Lipase from Candida rugosa was immobilized by adsorption onto laboratory prepared supports, silica SBA-15 and zirconia. The adsorption process was studied as a function of pH in terms of percent of adsorbed lipase, enzyme activity and zeta potential of support and enzyme. Several analytical approaches such as laser Doppler electrophoresis, Fourier transform infrared spectroscopy (FTIR) and field emission scanning electron microscopy (FESEM) showed that the lipase was successfully immobilized onto both supports. The zeta-potential data suggest that the adsorption efficiency does not depends on the sign but on the magnitude of the surface charge of adsorption partners, and therefore underline the importance of their dispersion stability. Adsorption to material surface altered enzyme characteristics. nu(max), for the lipase immobilized onto silica and zirconia were 4.8-fold and 3.6-fold lower than that of the free lipase, respectively. The Km showed no alteration of enzyme-substrate affinity on zirconia support, whereas the enzyme immobilized on silica had 3.6 times lower affinity. Thermostability at 60 degrees C of the lipase was improved 12-fold on zirconia and 4-fold on silica. Finally, in examining reusability, the immobilized lipase retained more than 90% of initial activity after eight reuses on both supports. (C) 2014 Elsevier B.V. All rights reserved. PB - Elsevier B.V. T2 - Biochemical Engineering Journal T1 - Immobilization of Candida rugosa lipase by adsorption onto biosafe meso/macroporous silica and zirconia EP - 83 SP - 73 VL - 93 DO - 10.1016/j.bej.2014.09.012 ER -
@article{ author = "Zivković, Lidija T. Izrael and Živković, Ljiljana and Babić, Biljana M. and Kokunešoski, Maja and Jokić, Bojan M. and Karadzic, Ivanka M.", year = "2015", abstract = "Lipase from Candida rugosa was immobilized by adsorption onto laboratory prepared supports, silica SBA-15 and zirconia. The adsorption process was studied as a function of pH in terms of percent of adsorbed lipase, enzyme activity and zeta potential of support and enzyme. Several analytical approaches such as laser Doppler electrophoresis, Fourier transform infrared spectroscopy (FTIR) and field emission scanning electron microscopy (FESEM) showed that the lipase was successfully immobilized onto both supports. The zeta-potential data suggest that the adsorption efficiency does not depends on the sign but on the magnitude of the surface charge of adsorption partners, and therefore underline the importance of their dispersion stability. Adsorption to material surface altered enzyme characteristics. nu(max), for the lipase immobilized onto silica and zirconia were 4.8-fold and 3.6-fold lower than that of the free lipase, respectively. The Km showed no alteration of enzyme-substrate affinity on zirconia support, whereas the enzyme immobilized on silica had 3.6 times lower affinity. Thermostability at 60 degrees C of the lipase was improved 12-fold on zirconia and 4-fold on silica. Finally, in examining reusability, the immobilized lipase retained more than 90% of initial activity after eight reuses on both supports. (C) 2014 Elsevier B.V. All rights reserved.", publisher = "Elsevier B.V.", journal = "Biochemical Engineering Journal", title = "Immobilization of Candida rugosa lipase by adsorption onto biosafe meso/macroporous silica and zirconia", pages = "83-73", volume = "93", doi = "10.1016/j.bej.2014.09.012" }
Zivković, L. T. I., Živković, L., Babić, B. M., Kokunešoski, M., Jokić, B. M.,& Karadzic, I. M.. (2015). Immobilization of Candida rugosa lipase by adsorption onto biosafe meso/macroporous silica and zirconia. in Biochemical Engineering Journal Elsevier B.V.., 93, 73-83. https://doi.org/10.1016/j.bej.2014.09.012
Zivković LTI, Živković L, Babić BM, Kokunešoski M, Jokić BM, Karadzic IM. Immobilization of Candida rugosa lipase by adsorption onto biosafe meso/macroporous silica and zirconia. in Biochemical Engineering Journal. 2015;93:73-83. doi:10.1016/j.bej.2014.09.012 .
Zivković, Lidija T. Izrael, Živković, Ljiljana, Babić, Biljana M., Kokunešoski, Maja, Jokić, Bojan M., Karadzic, Ivanka M., "Immobilization of Candida rugosa lipase by adsorption onto biosafe meso/macroporous silica and zirconia" in Biochemical Engineering Journal, 93 (2015):73-83, https://doi.org/10.1016/j.bej.2014.09.012 . .