458533-17-0Relevant 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.
Efficient tryptic proteolysis accelerated by laser radiation for peptide mapping in proteome analysis
Yao, Guoping,Deng, Chunhui,Zhang, Xiangmin,Yang, Pengyuan
supporting information; experimental part, p. 8185 - 8189 (2011/02/22)
Back to basics: Coupled with MALDI-TOF MS, laser-assisted proteolysis (see schematic illustration) enabled rapid protein digestion and peptide mapping without the need for enzyme immobilization to increase the efficiency of tryptic digestion. Protein solutions containing trypsin were digested in less than a minute upon irradiation at 808 nm with a laser.
