Enzyme loading in the support and medium composition during immobilization alter activity, specificity and stability of octyl agarose-immobilized Eversa Transform

International Journal of Biological Macromolecules, Год журнала: 2025, Номер 295, С. 139667 - 139667

Опубликована: Янв. 9, 2025

Язык: Английский

Insights on the role of blocking agent on the properties of the lipase from Thermomyces lanuginosus immobilized on heterofunctional support for hydroesterification reactions

International Journal of Biological Macromolecules, Год журнала: 2024, Номер 275, С. 133555 - 133555

Опубликована: Июль 1, 2024

Here, we report a study of the effect blocking agent on properties lipase from Thermomyces lanuginosus (TLL) immobilized heterofunctional support (Purolite C18-ethylnediamina (EDA)- vinyl sulfone (VS)-TLL-blocking agent) in different reactions. The performance biocatalysts was compared to those standard hydrophobic C18-TLL) and commercial one (TLL-IM). nature (Cys, Gly Asp) altered enzyme features. TLL-IM always gave comparatively worse performance, with its specificity for oil being very Purolite biocatalysts. Under optimized conditions, C18-TLL yielded 97 % hydrolysis conversion after 4 h using water/waste cooking soybean (WCSO) mass ratio 4.3, biocatalyst load 6.5 wt% temperature 44.2 °C (without buffer or emulsification agent). In esterification reactions purified free fatty acids (FFAs) obtained WCSO, best TLL depended utilized alcohol: linear amyl alcohol preferred by C18-EDA-VS-TLL-Gly, while higher activity achieved utilizing isoamyl as nucleophile C18-EDA-VS-TLL-Cys, C18-EDA-VS-TLL-Asp IM-TLL catalysts. All results indicate influence step final

Язык: Английский

Ethanolysis of degummed soybean oil using magnetic CLEAs from Eversa® Transform

Journal of Biotechnology, Год журнала: 2025, Номер unknown

Опубликована: Март 1, 2025

Язык: Английский