TechnoRep - Faculty of Technology and Metallurgy Repository
University of Belgrade - Faculty of Technology and Metallurgy
    • English
    • Српски
    • Српски (Serbia)
  • English 
    • English
    • Serbian (Cyrillic)
    • Serbian (Latin)
  • Login
View Item 
  •   TechnoRep
  • Tehnološko-metalurški fakultet
  • Radovi istraživača / Researchers’ publications (TMF)
  • View Item
  •   TechnoRep
  • Tehnološko-metalurški fakultet
  • Radovi istraživača / Researchers’ publications (TMF)
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

Alginate-immobilized lipase by electrostatic extrusion for the purpose of palm oil hydrolysis in lecithin/isooctane system

Authorized Users Only
2002
Authors
Knežević, Zorica
Bobić, Svetlana
Milutinović, A
Obradović, Bojana
Mojović, Ljiljana
Bugarski, Branko
Article (Published version)
Metadata
Show full item record
Abstract
Lipase from Candida rugosa was immobilized in alginate beads for possible application in non-aqueous or microaqueous reaction systems. An electrostatic droplet generation technique was used for production of small diameter ( lt 1 mm) lipase-alginate beads. This technique provided negligible loss of the lipase (immobilization efficiencies were 98.2-99.2%). Under optimal immobilization conditions (applied potential 4.9 kV, needle gauge 21, 2% sodium alginate solution) the lipase-alginate beads, 0.65 mm in diameter, retained enzyme activity equivalent to 75% that of free lipase. The activity of the immobilized lipase was verified in the reaction of palm oil hydrolysis in a lecithin/isooctane system. The reaction rate with alginate-immobilized lipase was lower than with the free enzyme but the final conversions were approximately the same (similar to 74%). Immobilized lipase could be used for up to three reaction cycles with little loss of activity.
Keywords:
lipase / immobilization / alginate / electrostatic extrusion / palm oil hydrolysis
Source:
Process Biochemistry, 2002, 38, 3, 313-318
Publisher:
  • Elsevier Sci Ltd, Oxford

DOI: 10.1016/S0032-9592(02)00085-7

ISSN: 1359-5113

WoS: 000179665400003

Scopus: 2-s2.0-0036842712
[ Google Scholar ]
76
71
URI
http://TechnoRep.tmf.bg.ac.rs/handle/123456789/493
Collections
  • Radovi istraživača / Researchers’ publications (TMF)
Institution/Community
Tehnološko-metalurški fakultet
TY  - JOUR
AU  - Knežević, Zorica
AU  - Bobić, Svetlana
AU  - Milutinović, A
AU  - Obradović, Bojana
AU  - Mojović, Ljiljana
AU  - Bugarski, Branko
PY  - 2002
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/493
AB  - Lipase from Candida rugosa was immobilized in alginate beads for possible application in non-aqueous or microaqueous reaction systems. An electrostatic droplet generation technique was used for production of small diameter ( lt  1 mm) lipase-alginate beads. This technique provided negligible loss of the lipase (immobilization efficiencies were 98.2-99.2%). Under optimal immobilization conditions (applied potential 4.9 kV, needle gauge 21, 2% sodium alginate solution) the lipase-alginate beads, 0.65 mm in diameter, retained enzyme activity equivalent to 75% that of free lipase. The activity of the immobilized lipase was verified in the reaction of palm oil hydrolysis in a lecithin/isooctane system. The reaction rate with alginate-immobilized lipase was lower than with the free enzyme but the final conversions were approximately the same (similar to 74%). Immobilized lipase could be used for up to three reaction cycles with little loss of activity.
PB  - Elsevier Sci Ltd, Oxford
T2  - Process Biochemistry
T1  - Alginate-immobilized lipase by electrostatic extrusion for the purpose of palm oil hydrolysis in lecithin/isooctane system
EP  - 318
IS  - 3
SP  - 313
VL  - 38
DO  - 10.1016/S0032-9592(02)00085-7
ER  - 
@article{
author = "Knežević, Zorica and Bobić, Svetlana and Milutinović, A and Obradović, Bojana and Mojović, Ljiljana and Bugarski, Branko",
year = "2002",
abstract = "Lipase from Candida rugosa was immobilized in alginate beads for possible application in non-aqueous or microaqueous reaction systems. An electrostatic droplet generation technique was used for production of small diameter ( lt  1 mm) lipase-alginate beads. This technique provided negligible loss of the lipase (immobilization efficiencies were 98.2-99.2%). Under optimal immobilization conditions (applied potential 4.9 kV, needle gauge 21, 2% sodium alginate solution) the lipase-alginate beads, 0.65 mm in diameter, retained enzyme activity equivalent to 75% that of free lipase. The activity of the immobilized lipase was verified in the reaction of palm oil hydrolysis in a lecithin/isooctane system. The reaction rate with alginate-immobilized lipase was lower than with the free enzyme but the final conversions were approximately the same (similar to 74%). Immobilized lipase could be used for up to three reaction cycles with little loss of activity.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Process Biochemistry",
title = "Alginate-immobilized lipase by electrostatic extrusion for the purpose of palm oil hydrolysis in lecithin/isooctane system",
pages = "318-313",
number = "3",
volume = "38",
doi = "10.1016/S0032-9592(02)00085-7"
}
Knežević, Z., Bobić, S., Milutinović, A., Obradović, B., Mojović, L.,& Bugarski, B.. (2002). Alginate-immobilized lipase by electrostatic extrusion for the purpose of palm oil hydrolysis in lecithin/isooctane system. in Process Biochemistry
Elsevier Sci Ltd, Oxford., 38(3), 313-318.
https://doi.org/10.1016/S0032-9592(02)00085-7
Knežević Z, Bobić S, Milutinović A, Obradović B, Mojović L, Bugarski B. Alginate-immobilized lipase by electrostatic extrusion for the purpose of palm oil hydrolysis in lecithin/isooctane system. in Process Biochemistry. 2002;38(3):313-318.
doi:10.1016/S0032-9592(02)00085-7 .
Knežević, Zorica, Bobić, Svetlana, Milutinović, A, Obradović, Bojana, Mojović, Ljiljana, Bugarski, Branko, "Alginate-immobilized lipase by electrostatic extrusion for the purpose of palm oil hydrolysis in lecithin/isooctane system" in Process Biochemistry, 38, no. 3 (2002):313-318,
https://doi.org/10.1016/S0032-9592(02)00085-7 . .

DSpace software copyright © 2002-2015  DuraSpace
About TechnoRep | Send Feedback

OpenAIRERCUB
 

 

All of DSpaceInstitutions/communitiesAuthorsTitlesSubjectsThis institutionAuthorsTitlesSubjects

Statistics

View Usage Statistics

DSpace software copyright © 2002-2015  DuraSpace
About TechnoRep | Send Feedback

OpenAIRERCUB