Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5371503 | Biophysical Chemistry | 2011 | 4 Pages |
In studies on polyol-mediated protein stabilization, the polyols are the preferred variable and less importance is given to the intrinsic properties of the protein used. We investigated the stabilizing effects of glycerol on three in vitro evolved lipase mutants with varying stabilities and also in a broad pH range of 3.3-12.1. Significant linear negative correlation between increment in stability due to glycerol and prior stability suggests that stabilizing effects of glycerol depend on the prior stability of the protein. Polar/nonpolar surface area and charge do not have a bearing on the stabilizing effects of glycerol.
Graphical AbstractDownload full-size imageResearch Highlights⺠Stabilizing effect of glycerol on three evolved lipase mutants in pH range of 3.3-12.1. ⺠Increase in protein stability by glycerol is inversely related to the prior stability. ⺠Stability increase by glycerol is independent of surface area and charge of the mutants.