Facile one‐pot synthesis of silica‐based lipase nanocatalysts for improving stability. (1st April 2018)

• Record Type: Journal Article
• Authors: Zhou, Yan; Sun, Shanshan; Jiang, Shuhui; Liang, Hao
• Is Part Of: Micro & nano letters. Volume 13:Number 4(2018)
• Page Start: 572
• Page End: 575
• Publication Date: 2018-04-01
• Subjects: silicon compounds -- nanoparticles -- nanocomposites -- enzymes -- molecular biophysics -- biochemistry -- nanofabrication -- catalysis -- catalysts -- pH -- recycling -- nanobiotechnology; facile one‐pot synthesis -- silica‐based lipase nanocatalysts -- lipases inactivation -- high temperature organic solvents -- extremely acidic organic solvents -- alkaline organic solvents -- silica nanoparticles -- (3‐ammonia propyl) triethoxysilane -- APTES -- immobilised Candida rugosa lipase -- free enzyme -- immobilised CRL -- stability test -- pH values -- recyclable usability -- protein -- rigid carrier -- SiO2; Nanotechnology -- Periodicals; Nanostructures -- Periodicals; Microtechnology -- Periodicals; 620.5
• DOI: 10.1049/mnl.2017.0402
• Languages: English
• ISSNs: 1750-0443

Abstract

Abstract : The inactivation of lipases caused by organic solvents, high temperature, extremely acidic and alkaline requires a high stability. In this work, a novel one‐pot synthesis for the lipase immobilisation on silica nanoparticles was reported. The optimal amounts of (3‐ammonia propyl) triethoxysilane (APTES) and ammonia were studied. The apparent K m value of the immobilised Candida rugosa lipase (CRL) was lower than that of free enzyme, showing affinity of the immobilised CRL to its substrate had increased. The results of stability test showed that the immobilised lipase was more stable than free enzyme at different temperatures and pH values. In particular, the immobilised CRL kept 96% activity at 90°C, while the free enzyme only remained 75% activity. Immobilised lipase had high catalytic efficiency, enhanced stability and recyclable usability compared to free enzymes, because of the cross‐linking between the protein and the rigid carrier. Therefore, the immobilised method would be beneficial to improving the activity and stability of enzyme universally.