Prikaz osnovnih podataka o dokumentu
Alginate-immobilized lipase by electrostatic extrusion for the purpose of palm oil hydrolysis in lecithin/isooctane system
dc.creator | Knežević, Zorica | |
dc.creator | Bobić, Svetlana | |
dc.creator | Milutinović, A | |
dc.creator | Obradović, Bojana | |
dc.creator | Mojović, Ljiljana | |
dc.creator | Bugarski, Branko | |
dc.date.accessioned | 2021-03-10T10:04:24Z | |
dc.date.available | 2021-03-10T10:04:24Z | |
dc.date.issued | 2002 | |
dc.identifier.issn | 1359-5113 | |
dc.identifier.uri | http://TechnoRep.tmf.bg.ac.rs/handle/123456789/493 | |
dc.description.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. | en |
dc.publisher | Elsevier Sci Ltd, Oxford | |
dc.rights | restrictedAccess | |
dc.source | Process Biochemistry | |
dc.subject | lipase | en |
dc.subject | immobilization | en |
dc.subject | alginate | en |
dc.subject | electrostatic extrusion | en |
dc.subject | palm oil hydrolysis | en |
dc.title | Alginate-immobilized lipase by electrostatic extrusion for the purpose of palm oil hydrolysis in lecithin/isooctane system | en |
dc.type | article | |
dc.rights.license | ARR | |
dc.citation.epage | 318 | |
dc.citation.issue | 3 | |
dc.citation.other | 38(3): 313-318 | |
dc.citation.spage | 313 | |
dc.citation.volume | 38 | |
dc.identifier.doi | 10.1016/S0032-9592(02)00085-7 | |
dc.identifier.scopus | 2-s2.0-0036842712 | |
dc.identifier.wos | 000179665400003 | |
dc.type.version | publishedVersion |