Bommarius_2006_Curr.Opin.Biotechnol_17_606

Reference

Title : High-throughput screening for enhanced protein stability - Bommarius_2006_Curr.Opin.Biotechnol_17_606
Author(s) : Bommarius AS , Broering JM , Chaparro-Riggers JF , Polizzi KM
Ref : Curr Opin Biotechnol , 17 :606 , 2006
Abstract :

High thermostability of proteins is a prerequisite for their implementation in biocatalytic processes and in the evolution of new functions. Various protein engineering methods have been applied to the evolution of increased thermostability, including the use of combinatorial design where a diverse library of proteins is generated and screened for variants with increased stability. Current trends are toward the use of data-driven methods that reduce the library size by using available data to choose areas of the protein to target, without specifying the precise changes. For example, the half-lives of subtilisin and a Bacillus subtilis lipase were increased 1500-fold and 300-fold, respectively, using a crystal structure to guide mutagenesis choices. Sequence homology based methods have also produced libraries where 50% of the variants have improved thermostability. Moreover, advances in the high-throughput measurement of denaturation curves and the application of selection methods to thermostability evolution have enabled the screening of larger libraries. The combination of these methods will lead to the rapid improvement of protein stability for biotechnological purposes.

PubMedSearch : Bommarius_2006_Curr.Opin.Biotechnol_17_606
PubMedID: 17049838

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Citations formats

Bommarius AS, Broering JM, Chaparro-Riggers JF, Polizzi KM (2006)
High-throughput screening for enhanced protein stability
Curr Opin Biotechnol 17 :606

Bommarius AS, Broering JM, Chaparro-Riggers JF, Polizzi KM (2006)
Curr Opin Biotechnol 17 :606