357944-43-5Relevant academic research and scientific papers
An easily regenerable enzyme reactor prepared from polymerized high internal phase emulsions
Ruan, Guihua,Wu, Zhenwei,Huang, Yipeng,Wei, Meiping,Su, Rihui,Du, Fuyou
, p. 54 - 60 (2016/04/20)
A large-scale high-efficient enzyme reactor based on polymerized high internal phase emulsion monolith (polyHIPE) was prepared. First, a porous cross-linked polyHIPE monolith was prepared by in-situ thermal polymerization of a high internal phase emulsion containing styrene, divinylbenzene and polyglutaraldehyde. The enzyme of TPCK-Trypsin was then immobilized on the monolithic polyHIPE. The performance of the resultant enzyme reactor was assessed according to the conversion ability of Nα-benzoyl-l-arginine ethyl ester to Nα-benzoyl-l-arginine, and the protein digestibility of bovine serum albumin (BSA) and cytochrome (Cyt-C). The results showed that the prepared enzyme reactor exhibited high enzyme immobilization efficiency and fast and easy-control protein digestibility. BSA and Cyt-C could be digested in 10 min with sequence coverage of 59% and 78%, respectively. The peptides and residual protein could be easily rinsed out from reactor and the reactor could be regenerated easily with 4 M HCl without any structure destruction. Properties of multiple interconnected chambers with good permeability, fast digestion facility and easily reproducibility indicated that the polyHIPE enzyme reactor was a good selector potentially applied in proteomics and catalysis areas.
A graphene-based multifunctional affinity probe for selective capture and sequential identification of different biomarkers from biosamples
Cheng, Gong,Wang, Zhi-Gang,Liu, Yan-Lin,Zhang, Ji-Lin,Sun, De-Hui,Ni, Jia-Zuan
supporting information, p. 10240 - 10242 (2012/11/13)
A novel multifunctional graphene-based affinity probe has been explored for selective capture of two different types of peptides from the biosamples for sequential detection. The Royal Society of Chemistry 2012.
