کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1743259 | 1522009 | 2013 | 9 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Catalytic behavior of carbonic anhydrase enzyme immobilized onto nonporous silica nanoparticles for enhancing CO2 absorption into a carbonate solution Catalytic behavior of carbonic anhydrase enzyme immobilized onto nonporous silica nanoparticles for enhancing CO2 absorption into a carbonate solution](/preview/png/1743259.png)
Nonporous, nano-sized support materials can offer a large external surface area for enzyme immobilization and improve the activity of the immobilized enzyme by eliminating internal diffusion of a substrate. In this study, nonporous silica nanoparticles with different sizes were synthesized by a flame spray pyrolysis (FSP) method and used as support materials for immobilization of the carbonic anhydrase (CA) enzyme for a CO2 capture application. The immobilization conditions, such as reaction time, pH, and initial enzyme concentration, were investigated to obtain both high enzyme loading and activity. The effects of temperature and pH on the immobilized enzyme's catalytic activity were investigated. Through immobilization, the CA enzymes remained active at the elevated temperature and pH conditions expected during CO2 absorption from the flue gases. At 50 °C and pH 10.5, the activities of the immobilized enzymes were about three times that of the free enzyme. Classic Danckwerts theory for absorption with reaction was applied to calculate the enzymatic kinetics for CO2 absorption. The enzyme's thermal stability also was significantly improved by the immobilization. Compared to its free enzyme counterpart, the half-life time of the immobilized enzyme was increased by up to 4.4 times over a 30-day test period at 50 °C.
► Silica nanoparticles were synthesized as a new support material for CA immobilization.
► Immobilized enzymes exhibited high CA loading and catalytic activity.
► Activity of the immobilized CA was three times the free CA at 50 °C and pH 10.5.
► Half-life time of the CA enzyme at 50 °C increased by 4.4 times by immobilization.
► Enzymatic kinetics was obtained for the immobilized CA enzymes.
Journal: International Journal of Greenhouse Gas Control - Volume 13, March 2013, Pages 17–25