دورية أكاديمية
Formation, topography and reactivity of Candida antarctica lipase B immobilized on silicon surface
العنوان: | Formation, topography and reactivity of Candida antarctica lipase B immobilized on silicon surface |
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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 |
DOI: | 10.3109/10242422.2010.531712 |
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