|MENG, SHI - Mississippi State University|
|LI, JIAZU - Mississippi State University|
|CHANG, SAM - Mississippi State University|
Submitted to: Journal of Food Chemistry
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 1/9/2019
Publication Date: 1/17/2019
Citation: Meng, S., Li, J., Chang, S., Maleki, S.J. 2019. Quantitative and kinetic analyses of peanut allergens as affected by food processing. Journal of Food Chemistry. 1:100004. https://doi.org/10.1016/j.fochx.2019.100004.
Interpretive Summary: Recombinant proteins are of great interest for all types of biochemistry work. A great many recombinant proteins are made as fusions with peptides (protein fragments) or whole proteins. A His-tag (poly histidine) is the most popular fusion because it can be used for purification of the protein. In this work the impact of His-tags on several proteins has been examined.
Technical Abstract: For years, the use of polyhistidine tags (His-tags) have been a staple in the isolation of recombinant proteins in immobilized metal affinity chromatography experiments. Their usage has been widely beneficial in increasing protein purity from crude cell lysates. For some recombinant proteins, a consequence of His-tag addition is that it can affect protein function and stability. Functional proteins are essential in the elucidation of their biological, kinetic, structural, and thermodynamic properties. In this manuscript, we determine the effect of N-terminal His-tags on the thermal stability of select proteins using differential scanning fluorimetry, and identify that the removal of the His-tag can have both beneficial and deleterious effects on their stability.