دورية أكاديمية

Formation, topography and reactivity of Candida antarctica lipase B immobilized on silicon surface

التفاصيل البيبلوغرافية
العنوان: Formation, topography and reactivity of Candida antarctica lipase B immobilized on silicon surface
المؤلفون: Miletic, Nemanja, Fahriansyah, Nguyen, Le-Thu T., Loos, Katja, Miletić, Nemanja
المصدر: Miletic , N , Fahriansyah , Nguyen , L-T T , Loos , K & Miletić , N 2010 , ' Formation, topography and reactivity of Candida antarctica lipase B immobilized on silicon surface ' , Biocatalysis and Biotransformation , vol. 28 , no. 5-6 , pp. 357-369 . https://doi.org/10.3109/10242422.2010.531712Test
سنة النشر: 2010
المجموعة: University of Groningen research database
مصطلحات موضوعية: Enzyme immobilization, Candida antarctica lipase B, silanization, glutaraldehyde activation, silicon surface, SI-BASED MATERIALS, GLYCOL DIMETHACRYLATE) RESINS, ATOMIC-FORCE MICROSCOPY, ENZYME GLUCOSE-OXIDASE, GAMMA-AMINOPROPYLTRIETHOXYSILANE, COVALENT IMMOBILIZATION, BACTERIORHODOPSIN FILMS, 3-AMINOPROPYLTRIETHOXYSILANE, SPECTROSCOPY
الوصف: Candida antarctica lipase B (CaLB) was immobilized on silicon wafers previously modified with aminopropyltriethoxysilane (APTES) and activated with glutaraldehyde (GLA). The various steps of immobilization were characterized using transmission FTIR, AFM, contact angle measurements and XPS. Furthermore, the formation of APTES films during the initial immobilization step was additionally analyzed by ellipsometry and an 'island' monolayer film formation was revealed. When the concentration of APTES was increased, the amount of immobilized lipase also increased. On the other hand, while the activity of immobilized enzyme in lipase-catalyzed transesterifi cation of 6,8-difluoro-4-methylumbelliferyl octanoate initially increased, showing the highest value when 0.00050% w/v APTES solution was used for the initial immobilization step, it subsequently decreased. Comparison of enzyme activity and surface filling results indicate that there has to be multilayer formation in the enzyme layer, as revealed by AFM images and determination of enzyme loading.
نوع الوثيقة: article in journal/newspaper
اللغة: English
العلاقة: https://research.rug.nl/en/publications/4b52bb59-53df-4d66-89da-1dbbd64c5b98Test
DOI: 10.3109/10242422.2010.531712
الإتاحة: https://doi.org/10.3109/10242422.2010.531712Test
https://hdl.handle.net/11370/4b52bb59-53df-4d66-89da-1dbbd64c5b98Test
https://research.rug.nl/en/publications/4b52bb59-53df-4d66-89da-1dbbd64c5b98Test
حقوق: info:eu-repo/semantics/closedAccess
رقم الانضمام: edsbas.84A8CBF5
قاعدة البيانات: BASE