Protein stabilization with retained function of monellin using a split GFP system.

ABSTRACT: Sweet proteins are an unexploited resource in the search for non-carbohydrate sweeteners mainly due to their low stability towards heating. Variants of the sweet protein monellin, with increased stability, were derived by an in vivo screening method based on the thermodynamic linkage between fragment complementation and protein stability. This approach depends on the correlation between mutational effects on the affinity between protein fragments and the stability of the intact protein. By linking the two fragments of monellin to the split GFP (green fluorescent protein) system, reconstitution of GFP was promoted and moderately fluorescent colonies were obtained. Two separate random libraries were produced for the monellin chains and the mutant clones were ranked based on fluorescence inte

SUBMITTER: Weiffert T 

PROVIDER: S-EPMC6109104 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature