| Autor: |
Ivan Kurtovic, Tim D. Nalder, Helen Cleaver, Susan N. Marshall |
| Jazyk: |
angličtina |
| Rok vydání: |
2020 |
| Předmět: |
|
| Zdroj: |
Biotechnology Reports, Vol 28, Iss , Pp e00535- (2020) |
| Druh dokumentu: |
article |
| ISSN: |
2215-017X |
| DOI: |
10.1016/j.btre.2020.e00535 |
| Popis: |
Lipase from Candida rugosa (CrL) was immobilised on highly hydrophobic, octadecyl methacrylate resin (Lifetech™ ECR8806M) via interfacial adsorption. The aim was to produce a stable biocatalyst suitable for use in a range of lipid-modifying reactions. Immobilisation was carried out in 10 mM phosphate buffer (pH 6.0) over 24 h at 21 °C. High protein binding of 58.7 ± 4.9 mg/g dry support accounted for ∼53 % of the applied protein. The activity recovery against tributyrin was 74.0 ± 1.1 %. The specific activity of immobilised CrL against tributyrin was considerably higher than that of Novozym® 435, at 1.79 ± 0.05 and 1.08 ± 0.04 U/mg bound protein, respectively. Incubation with high concentrations (10 % w/v) of both Triton X-100 and SDS resulted in only a small reduction in immobilised lipase activity. Solvent-free synthesis of glycerides by the FFA-saturated immobilised CrL was successful over 6 reaction cycles, with no apparent loss of activity. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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