Tuning the catalytic properties of lipases immobilized on divinylsulfone activated agarose by altering its nanoenvironment

Enzyme and Microbial Technology

Volumn 77, Issue , 2015, Pages 1-7

  dos Santos, Jose C S ^a,b   Rueda, Nazzoly ^a,c   Gonçalves, Luciana R B ^b   Fernandez Lafuente, Roberto ^a  

^a INSTITUTO DE CATÁLISIS Y PETROLEOQUÍMICA   (Spain)

^b FEDERAL UNIVERSITY OF CEARÁ   (Brazil)

^c UNIVERSIDAD INDUSTRIAL DE SANTANDER   (Colombia)

Author keywords

Divinylsulfone support; Enzyme nano environment; Enzyme stability; Lipase; Lipase activity; Tuning lipase properties

Indexed keywords

CHEMICAL REACTIONS; ENZYMES; LIPASES;

CATALYTIC PROPERTIES; ENZYME SPECIFICITY; ENZYME STABILITY; ETHYL HEXANOATE; EXPERIMENTAL CONDITIONS; LIPASE ACTIVITY; LIPASE B FROM CANDIDA ANTARCTICA; THERMOMYCES LANUGINOSUS;

ENZYME ACTIVITY;

AGAROSE; ASPARTIC ACID; BUTYRIC ACID; BUTYRIC ACID DERIVATIVE; CYSTEINE; DIVINYLSULFONE; ETHANOLAMINE; ETHYLENEDIAMINE; FUNGAL ENZYME; GLYCINE; HEXANOIC ACID; IMIDAZOLE; IMMOBILIZED ENZYME; MANDELIC ACID; METHYL PHENYLACETATE; ORGANIC SOLVENT; P NITROPHENYL BUTYRATE; PHENYLACETIC ACID; PHENYLACETIC ACID DERIVATIVE; SULFONE DERIVATIVE; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG; DIVINYL SULFONE; FUNGAL PROTEIN; LIPASE B, CANDIDA ANTARCTICA; SEPHAROSE; SULFONE;

ARTICLE; BIOCATALYST; CANDIDA ANTARCTICA; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME IMMOBILIZATION; ENZYME INACTIVATION; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYME SUBSTRATE; HYDROLYSIS; NONHUMAN; PH; SURFACE PROPERTY; THERMOMYCES LANUGINOSUS; THERMOSTABILITY; ASCOMYCETES; CANDIDA; CATALYSIS; ENZYMOLOGY; KINETICS; METABOLISM; NANOTECHNOLOGY;

CANDIDA ANTARCTICA; DAPHNE VIRUS S; THERMOMYCES LANUGINOSUS;

ASCOMYCOTA; CANDIDA; CATALYSIS; ENZYME STABILITY; ENZYMES, IMMOBILIZED; FUNGAL PROTEINS; HYDROGEN-ION CONCENTRATION; KINETICS; LIPASE; NANOTECHNOLOGY; SEPHAROSE; SUBSTRATE SPECIFICITY; SULFONES;

EID: 84930194250     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2015.05.001     Document Type: Article

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