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The method described here allows a quantitative colorimetric screening of hydrolase libraries using ester substrates. The pH indicator 4-nitrophenol is used to monitor ester hydrolysis. The enantioselectivity of an enzyme is estimated by measuring the initial rates of hydrolysis for the pure stereoisomers of the substate separately
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Multi-enzyme process for L-methionine production by inversion of enantioselectivity
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L = 20%) and its total activity increased fivefold. Whole E. coli cells expressing this evolved L-hydantoinase together with two other enzymes involved in the methionine pathway showed a fivefold increase in L-methionine productivity at > 90% conversion of the substrate D,L-5-(2-methylthioethyl)hydantoin
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L = 20%) and its total activity increased fivefold. Whole E. coli cells expressing this evolved L-hydantoinase together with two other enzymes involved in the methionine pathway showed a fivefold increase in L-methionine productivity at > 90% conversion of the substrate D,L-5-(2-methylthioethyl)hydantoin.
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Chemoenzymatic synthesis of key epothilone fragments
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Beyond binding: Using phage display to select for structure, folding and enzymatic activity in proteins
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This review describes in detail recent approaches to the use of phage display for the selection of active and substrate-specific biocatalysts
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In vivo versus in vitro screening or selection for catalytic activity in enzymes and abzymes
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