α-Rhamnosidase and β-glucosidase expressed by naringinase immobilized on new ionic liquid sol-gel matrices: Activity and stability studies

Journal of Biotechnology

Volumn 152, Issue 4, 2011, Pages 147-158

  Vila Real, Helder ^a   Alfaia, António J ^a   Rosa, João N ^a   Gois, Pedro M P ^a   Rosa, M Emilia ^b   Calado, António R T ^a   Ribeiro, Maria H ^a  

^a RESEARCH INSTITUTE FOR MEDICINES IMED ULISBOA   (Portugal)

^b ICEMS   (Portugal)

Author keywords

Activity; Ionic liquids; Naringinase; SEM; Sol gel; Stability; TMOS Glycerol

Indexed keywords

CONVERGENCE OF NUMERICAL METHODS; EFFICIENCY; ENZYME ACTIVITY; FLAVONOIDS; HYDROPHOBICITY; IONIC LIQUIDS; NEGATIVE IONS; POSITIVE IONS; SCANNING ELECTRON MICROSCOPY; SOL-GEL PROCESS; SOL-GELS; STABILITY; THERMODYNAMIC PROPERTIES;

DIFFERENT STRUCTURE; ENVIRONMENTAL-FRIENDLY; GLUCOSIDASE ACTIVITY; HYDROPHOBIC ANIONS; HYDROPHOBIC NATURE; KINETICS PARAMETER; NARINGINASE; TMOS/GLYCEROL;

ENZYME IMMOBILIZATION;

3 AMINOPROPYLTRIMETHOXYSILANE; ALPHA RHAMNOSIDASE; AURANTIIN; BETA GLUCOSIDASE; DIGLYCERYLSILANE; FLAVONE DERIVATIVE; GLYCEROL; HYDROLASE; IMIDAZOLE DERIVATIVE; IONIC LIQUID; METHYLTRIMETHOXYSILANE; NARINGINASE; PRUNIN; SILANE DERIVATIVE; TETRAMETHOXYSILANE; UNCLASSIFIED DRUG;

ARTICLE; ENZYME ACTIVITY; ENZYME IMMOBILIZATION; ENZYME KINETICS; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; HYDROLYSIS; HYDROPHOBICITY; NONHUMAN; PARTITION COEFFICIENT; PENICILLIUM; PENICILLIUM DECUMBENS; PRIORITY JOURNAL; PROTEIN EXPRESSION; SCANNING ELECTRON MICROSCOPY;

EID: 79955155741     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2010.08.005     Document Type: Article

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