Lipase-catalyzed Knoevenagel condensation in water-ethanol solvent system. Does the enzyme possess the substrate promiscuity?

Biochemical Engineering Journal

Volumn 101, Issue , 2015, Pages 99-107

  Li, Weina ^a,b,c   Li, Rong ^b,d   Yu, Xiaochun ^a   Xu, Xuebing ^b   Guo, Zheng ^b   Tan, Tianwei ^a   Fedosov, Sergey N ^b  

^a BEIJING UNIVERSITY OF CHEMICAL TECHNOLOGY   (China)

^b AARHUS UNIVERSITY   (Denmark)

^c NORTHWEST UNIVERSITY   (China)

^d JILIN UNIVERSITY   (China)

Author keywords

Enzyme biocatalysis; Ethanol; Kinetic parameters; Knoevenagel condensation; Lipase; Promiscuity

Indexed keywords

CATALYSIS; CONDENSATION; CONDENSATION REACTIONS; ENZYMATIC HYDROLYSIS; ENZYMES; ETHANOL; HYDROGEN; HYDROLYSIS; KETONES; KINETIC PARAMETERS; LIPASES; SOLVENTS; SUBSTRATES;

COMPETITIVE INHIBITION; COVALENT MODIFICATIONS; ENZYMATIC ACTIVITIES; ENZYME BIOCATALYSIS; KNOEVENAGEL CONDENSATION; PROMISCUITY; SPONTANEOUS CONDENSATION; SUBSTRATE SATURATION;

ORGANIC SOLVENTS;

ALBUMIN; ALCOHOL; ALDEHYDE; CAFFEIC ACID; HYDROGEN; KETONE; PROTON; SOLVENT; TRIACYLGLYCEROL LIPASE; WATER;

ARTICLE; CATALYSIS; COMPETITIVE INHIBITION; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; HYDROLYSIS; KNOEVENAGEL CONDENSATION; MUCOR; MUCOR JAVANICUS; NONHUMAN; PIG; PRIORITY JOURNAL; STEADY STATE; YARROWIA LIPOLYTICA;

MUCOR JAVANICUS; SUS; YARROWIA LIPOLYTICA;

EID: 84929315259     PISSN: 1369703X     EISSN: 1873295X     Source Type: Journal    
DOI: 10.1016/j.bej.2015.04.021     Document Type: Article

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