Effect of protein molecular weight on the mass transfer in protein mixing

The mixing of protein solutions with that of precipitating agents is very important in protein crystallization experiments. In this work, the interferometry images were recorded during the mixing of two proteins with different molecular weights： lysozyme of -14.6 kDa, trypsin of -23.3 kDa and pepsin...

Full description

Saved in:
Bibliographic Details
Published inScience China. Physics, mechanics & astronomy Vol. 55; no. 3; pp. 470 - 476
Main Authors Asad, Ahmed, Chai, Chuan, Wu, JiangTao
Format Journal Article
LanguageEnglish
Published Heidelberg SP Science China Press 01.03.2012
Springer Nature B.V
Subjects
Astronomy
Classical and Continuum Physics
Convection
Crystallization
Interferometry
kDa
Lysozyme
Mach-Zehnder interferometers
Mach-Zehnder干涉仪
Mass transfer
Molecular weight
Observations and Techniques
Pepsin
Physics
Physics and Astronomy
Proteins
Transport processes
传质过程
混合过程
界面动力学
蛋白质分子量
蛋白质溶液
高分子量
Mach-Zehnder interferometer
diffusion
interface
mass transfer
protein mixing
Online AccessGet full text

Cover

More Information
Summary:The mixing of protein solutions with that of precipitating agents is very important in protein crystallization experiments. In this work, the interferometry images were recorded during the mixing of two proteins with different molecular weights： lysozyme of -14.6 kDa, trypsin of -23.3 kDa and pepsin of -34.8 kDa were placed in a Mach-Zehnder interferometer. The protein mo- lecular weight dependence on the competition of the transport process and kinetics at the interface was studied. The concentra- tion profiles of protein solutions were calculated to analyze the mass transfer during the mixing process. It was observed that the mass transfer process is more efficient during the mixing of proteins with higher molecular weights. In addition, the more rapid concentration changes above the interface suggest that convection may dominate the diffusion. The phenomenon of con- vection is higher in the protein solutions with higher molecular weight.
Bibliography:11-5000/N
ASAD Ahmed, CHAI Chuan ＆ WU JiangTaoState Key Laboratory of Multiphase Flow in Power Engineering, Xi＇ an Jiaotong University, Xi＇ an 710049, China Received May 19, 2011; accepted August 19, 2011; published online February 9, 2012Corresponding author （email： jtwu@mail.xjtu.edu.cn）
The mixing of protein solutions with that of precipitating agents is very important in protein crystallization experiments. In this work, the interferometry images were recorded during the mixing of two proteins with different molecular weights： lysozyme of -14.6 kDa, trypsin of -23.3 kDa and pepsin of -34.8 kDa were placed in a Mach-Zehnder interferometer. The protein mo- lecular weight dependence on the competition of the transport process and kinetics at the interface was studied. The concentra- tion profiles of protein solutions were calculated to analyze the mass transfer during the mixing process. It was observed that the mass transfer process is more efficient during the mixing of proteins with higher molecular weights. In addition, the more rapid concentration changes above the interface suggest that convection may dominate the diffusion. The phenomenon of con- vection is higher in the protein solutions with higher molecular weight.
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1674-7348
1869-1927
DOI:10.1007/s11433-012-4640-x