Increased activity of enzymatic transacylation of acrylates through rational design of lipases

Journal of Molecular Catalysis B: Enzymatic

Volumn 65, Issue 1-4, 2010, Pages 3-10

  Syrén, Per Olof ^a   Lindgren, Ebba ^a   Hoeffken, Hans Wolfgang ^b   Branneby, Cecilia ^b   Maurer, Steffen ^b   Hauer, Bernhard ^b   Hult, Karl ^a  

^a ROYAL INSTITUTE OF TECHNOLOGY   (Sweden)

^b BASF SE   (Germany)

Author keywords

CALB; Kinetics; Lipase; Point mutations; Proficiency

Indexed keywords

ACYL ACCEPTOR; ANTARCTICA; CALB; CANDIDA ANTARCTICA LIPASE B; CONCENTRATION OF; CUTINASE; DOUBLE BONDS; ELECTRONIC EFFECTS; ENERGETIC COSTS; HYDROLASES; METHYL METHACRYLATES; METHYL PROPIONATES; POINT MUTATIONS; RATIONAL DESIGN; WILD-TYPE ENZYMES;

CATALYSIS; ENZYMES; ESTERIFICATION; ESTERS; LIPASES; SALTS;

REACTION RATES;

ACRYLIC ACID DERIVATIVE; ESTER; HYDROLASE; LIPASE B; METHACRYLIC ACID METHYL ESTER; PROPIONIC ACID DERIVATIVE; SULFURIC ACID; TRIACYLGLYCEROL LIPASE;

ACYLATION; ARTICLE; CANDIDA ANTARCTICA; CATALYSIS; CHEMICAL BOND; CHEMICAL REACTION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME KINETICS; RHIZOMUCOR;

CANDIDA ANTARCTICA; HUMICOLA INSOLENS; PSEUDOZYMA ANTARCTICA; RHIZOMUCOR;

EID: 77952673518     PISSN: 13811177     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcatb.2009.11.016     Document Type: Article

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