Immobilization of Candida antarctica lipase B on Polystyrene Nanoparticles

• Published in: Macromolecular Rapid Communications
• Main Authors: Miletic, Nemanja, Abetz, Volker, Ebert, Katrin, Loos, Katja, Miletić, Nemanja
• Format: Article in Journal/Newspaper
• Language: English
• Published: 2010
• Subjects: Candida antarctica lipase B; enzymes; nanoparticles; polystyrene; RING-OPENING POLYMERIZATION; ORGANIC MEDIA; POLYESTER SYNTHESIS; ADSORPTION; PROTEIN; CONDENSATION; BIOCATALYST; STABILITY; SUPPORTS; SILICA; Antarc*; Antarctica
• Online Access: https://hdl.handle.net/11370/23527c93-18be-45d7-9b26-db266e674e57; https://research.rug.nl/en/publications/23527c93-18be-45d7-9b26-db266e674e57; https://doi.org/10.1002/marc.200900497; https://pure.rug.nl/ws/files/6740748/2010MacromolRapidCommMiletic.pdf

Polystyrene (PS) nanoparticles were prepared via a nanoprecipitation process. The influence of the pH of the buffer solution used during the immobilization process on the loading of Candida antarctica lipase B (Cal-B) and on the hydrolytic activity (hydrolysis of p-nitrophenyl acetate) of the immobilized Cal-B was studied. The pH of the buffer solution has no influence on enzyme loading, while immobilized enzyme activity is very dependent on the pH of adsorption. Cal-B immobilized on PS nanoparticles in buffer solution pH 6.8 performed higher hydrolytic activity than crude enzyme powder and Novozyme 435.