Sandstrom_2009_Protein.Eng.Des.Sel_22_413

Reference

Title : Directed evolution of Candida antarctica lipase A using an episomaly replicating yeast plasmid - Sandstrom_2009_Protein.Eng.Des.Sel_22_413
Author(s) : Sandstrom AG , Engstrom K , Nyhlen J , Kasrayan A , Backvall JE
Ref : Protein Engineering Des Sel , 22 :413 , 2009
Abstract :

We herein report the first directed evolution of Candida antarctica lipase A (CalA), employing a combinatorial active-site saturation test (CAST). Wild-type CalA has a modest E-value of 5.1 in kinetic resolution of 4-nitrophenyl 2-methylheptanoate. Enzyme variants were expressed in Pichia pastoris by using the episomal vector pBGP1 which allowed efficient secretory expression of the lipase. Iterative rounds of CASTing yielded variants with good selectivity toward both the (S)- and the (R)-enantiomer. The best obtained enzyme variants had E-values of 52 (S) and 27 (R).

PubMedSearch : Sandstrom_2009_Protein.Eng.Des.Sel_22_413
PubMedID: 19509064

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Citations formats

Sandstrom AG, Engstrom K, Nyhlen J, Kasrayan A, Backvall JE (2009)
Directed evolution of Candida antarctica lipase A using an episomaly replicating yeast plasmid
Protein Engineering Des Sel 22 :413

Sandstrom AG, Engstrom K, Nyhlen J, Kasrayan A, Backvall JE (2009)
Protein Engineering Des Sel 22 :413