Imperial College London
Portrait Picture

Professor Jerry Heng

Faculty of Engineering, Department of Chemical Engineering

Professor in Particle Technology
 
 
 
//

Contact

 

+44 (0)20 7594 0784jerry.heng

 
 
//

Location

 

208ACE ExtensionSouth Kensington Campus

//

Summary

 

Publications

Citation

BibTex format

@article{Li:2021:10.1016/j.cherd.2021.06.012,
author = {Li, X and Heng, JYY},
doi = {10.1016/j.cherd.2021.06.012},
journal = {Chemical Engineering Research and Design},
pages = {81--88},
title = {The critical role of agitation in moving from preliminary screening results to reproducible batch protein crystallisation},
url = {http://dx.doi.org/10.1016/j.cherd.2021.06.012},
volume = {173},
year = {2021}
}
Download

RIS format (EndNote, RefMan)

TY  - JOUR
AB  - This study investigated the important role of agitation in obtaining consistent and reproducible results when moving from preliminary qualitative screenings for protein crystallisation to quantitative batch crystallisation experiments. Lysozyme-thaumatin binary protein mixture was used as the model protein system in this study. Poor reproducibility between batches were observed for non-agitated crystallisation conditions even if the same sampling timing and frequency applied. With agitation, from 0 to 200 rpm investigated in this study, improved reproducibility of protein crystallisation was observed with increased agitation. Additionally, agitation also had impacts on supersaturation exhaustion rate, yield and crystal size. Moreover, in agitated batch crystallisation, it was found that target protein crystallisation process was decelerated in the presence of protein impurity. In conclusion, we emphasised the essential role of agitation in protein crystallisation experiments else misleading conclusions with inconsistency might be drawn from non-agitated systems.
AU  - Li,X
AU  - Heng,JYY
DO  - 10.1016/j.cherd.2021.06.012
EP  - 88
PY  - 2021///
SN  - 0263-8762
SP  - 81
TI  - The critical role of agitation in moving from preliminary screening results to reproducible batch protein crystallisation
T2  - Chemical Engineering Research and Design
UR  - http://dx.doi.org/10.1016/j.cherd.2021.06.012
UR  - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000687279300007&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR  - https://www.sciencedirect.com/science/article/pii/S0263876221002550?via%3Dihub
UR  - http://hdl.handle.net/10044/1/91819
VL  - 173
ER  -
Download