Improvement of thermostable aldehyde dehydrogenase by directed evolution for application in Synthetic Cascade Biomanufacturing

Enzyme and Microbial Technology

Volumn 53, Issue 5, 2013, Pages 307-314

  Steffler, Fabian ^a,b   Guterl, Jan Karl ^a   Sieber, Volker ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b FRAUNHOFER INSTITUTE FOR INTERFACIAL ENGINEERING AND BIOTECHNOLOGY IGB   (Germany)

Author keywords

Biocatalysis; Directed evolution; Enzyme engineering; Screening; Synthetic Cascade Biomanufacturing; Thermostable dehydrogenase

Indexed keywords

BIO-MANUFACTURING; BIOCATALYSIS; DIRECTED EVOLUTION; ENZYME ENGINEERING; THERMOSTABLE DEHYDROGENASE;

ALDEHYDES; AMINO ACIDS; ESCHERICHIA COLI; RECOMBINANT PROTEINS; SCREENING; SOLUBILITY; SUBSTRATES;

ENZYMES;

ALDEHYDE DEHYDROGENASE; AMINO ACID; ENZYME VARIANT; NICOTINAMIDE ADENINE DINUCLEOTIDE;

AMINO ACID SUBSTITUTION; ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME STABILITY; ESCHERICHIA COLI; NONHUMAN; SITE DIRECTED MUTAGENESIS; SOLUBILITY; THERMOPLASMA ACIDOPHILUM; THERMOSTABILITY;

ESCHERICHIA COLI; THERMOPLASMA ACIDOPHILUM;

ALDEHYDE DEHYDROGENASE; ALDEHYDE DEHYDROGENASE FROM THERMOPLASMA ACIDOPHILUM; ALDH; BIOCATALYSIS; DIRECTED EVOLUTION; ENZYME ENGINEERING; SCREENING; SYNTHETIC CASCADE BIOMANUFACTURING; TAALDH; THERMOSTABLE DEHYDROGENASE;

ALDEHYDE DEHYDROGENASE; AMINO ACID SUBSTITUTION; BIOTECHNOLOGY; CATALYTIC DOMAIN; DIRECTED MOLECULAR EVOLUTION; ENZYME STABILITY; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NAD; PROTEIN CONFORMATION; PROTEIN ENGINEERING; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; THERMOPLASMA;

EID: 84883770256     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2013.07.002     Document Type: Article

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