首页 | 本学科首页   官方微博 | 高级检索  
     


Immobilization of a thermostable inorganic pyrophosphatase from the archaeon Pyrococcus furiosus onto amino‐functionalized silica beads
Authors:Qing Dong  Xufan Yan  Minhui Zheng  Ziwen Yang
Affiliation:1. Hubei Biopesticide Engineering Research Center, Wuhan, China;2. College of Life Sciences, Wuhan University, Wuhan, China
Abstract:This study focuses on the preparation and application of a recombinant thermophilic inorganic pyrophosphatase from the archaeon Pyrococcus furiosus on amino‐functionalized silica beads. The amino‐functionalized silica beads were prepared by coating with 3‐aminopropyltriethoxysilane by silanization. The thermostable inorganic pyrophosphatase was rapidly and successfully immobilized onto the amino‐functionalized silica beads with glutaraldehyde as a coupling agent (within 12 min, >95.4% protein was immobilized onto the support). The results show that the protein could be immobilized efficiently, with up to 1 mg of protein/g of support with 92.9% activity. Compared with the free enzyme, the immobilized enzyme displayed a high activity toward inorganic pyrophosphate, less sensitivity toward the pH, and increased thermal stability. The immobilized enzyme retained 56.9% of its initial activity after hydrolysis of the inorganic pyrophosphate after 12 consecutive cycles (total = 330 min) at high temperature; this indicated a high protein stability suitable for practical applications. © 2014 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2014 , 131, 40700.
Keywords:applications  bioengineering  biomaterials  proteins
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号