Alginate-immobilized lipase by electrostatic extrusion for the purpose of palm oil hydrolysis in lecithin/isooctane system
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2002
Authors
Knežević, Zorica
Bobić, Svetlana
Milutinović, A
Obradović, Bojana

Mojović, Ljiljana

Bugarski, Branko

Article (Published version)

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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 hydrolysisSource:
Process Biochemistry, 2002, 38, 3, 313-318Publisher:
- Elsevier Sci Ltd, Oxford
DOI: 10.1016/S0032-9592(02)00085-7
ISSN: 1359-5113
WoS: 000179665400003
Scopus: 2-s2.0-0036842712
Institution/Community
Tehnološko-metalurški fakultetTY - 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 . .