Lipolytic activities of a lipase immobilized on six selected supporting materials

Abstract

Six different types of materials including PVC, chitosan, chitin, agarose, Sepharose, and Trisacryl were evaluated for their lipase-coupling efficiencies. Among those tested, chitosan yielded the highest amount of lipase (79 mg/mL packed gel) immobilized but with lowest oil hydrolytic activity (0.03 mg eq/mL gel). The amount of lipase immobilized was affected by the length of the hydrocarbon chain attached to the PVC matrix but not by the pore size of the supports used. On the other hand, the specific activity of the immobilized lipase was affected by the pore size but not by the chain length of the hydrocarbon attached to the support. After immobilization, the optimal reaction pH was shifted from 7.5 to 8.5 and the optimal reaction temperature from 35 to 45-55 degrees C. Lipase immobilized on PVC exhibited higher thermal stability than that on agarose. The half-life of the PVC immobilized lipase operating at 30 degrees C in a packed-bed reactor was estimated to be about 400 h.

Production, purification, characterization, and applications of lipases

“…Many methods have been used to immobilize lipases, including adsorption or precipitation onto hydrophobic materials (Wisdom et al, 1984), covalent attachment to functional groups (Shaw et al, 1990), entrapment in polymer gels (Telefoncu et al, 1990), adsorption in macroporous anion exchange resins (Rizzi et al, 1992), microencapsulation in lipid vesicles (Balcão et al, 1996), and sol-gel entrapment Krishnakant and Madamwar, 2001). G. candidum lipases A and B were immobilized on Accurel EP 100 porous polypropylene supports, precoated with ovalbumin to increase stability in organic solvents and at elevated temperatures (Charton and Macrae, 1992).…”

Immobilization of lipase from Fusarium solani FS1

“…Shaw et al (9) found that the amount of lipase immobilized onto varying supports was dependent upon the length of the linker's carbon chain. The amount of protein immobilized using a linker of two carbons was considerably lower than with a linker of six to twelve carbons (9).…”

“…Shaw et al (9) found that the amount of lipase immobilized onto varying supports was dependent upon the length of the linker's carbon chain. The amount of protein immobilized using a linker of two carbons was considerably lower than with a linker of six to twelve carbons (9). When comparing the two linkers used here (glutaraldehyde and azide), the following analogy can be made: glutaraldehyde is comparable to an arm, whilst azide is comparable to a finger.…”

“…The low activity of immobilized derivatives was found to be due to the difficulty of oil droplets to penetrate the pores of the supports (9). The change in enzyme activity can be due to structural changes caused by the immobilization (2).…”

The study of the enzymatic synthesis mechanism of 4,6-disubstituted-3-cyano-2-pyridones

“…[119] Karbonilna grupa aktiviranog nosača reaguje sa amino grupom molekula enzima pri čemu nastaje Shiff-ova (Šifova) baza: Na ovaj način najčešće se aktiviraju neorganski nosači (staklo, keramika, alumosilikati, oksidi metala i dr.). [120][121][122][123][124] Ukoliko nosač ne sadrži amino grupu, potrebno ju je uvesti. 37 Uvođenje amino grupe vrši se u reakciji nosača i alkildiamina.…”