β-Galactosidase of Aspergillus oryzae immobilized in an ion exchange resin combining the ionic-binding and crosslinking methods: Kinetics and stability during the hydrolysis of lactose

Journal of Molecular Catalysis B: Enzymatic

Volumn 71, Issue 3-4, 2011, Pages 139-145

  Guidini, Carla Zanella ^a   Fischer, Janaína ^a   Resende, Miriam Maria De ^a   Cardoso, Vicelma Luiz ^a   Ribeiro, Eloízio Júlio ^a  

^a FEDERAL UNIVERSITY OF UBERLÂNDIA   (Brazil)

Author keywords

Galactosidase; Glutaraldehyde; Kinetics; Lactose hydrolysis; Resin Duolite A568

Indexed keywords

ACETATE BUFFERS; ASPERGILLUS ORYZAE; COMPETITIVE INHIBITION; CROSSLINKED; DUOLITE; ENZYMATIC ACTIVITIES; FIRST-ORDER MODELS; GALACTOSIDASES; GLUTARALDEHYDE; GLUTARALDEHYDES; HYDROLYSIS KINETICS; HYDROLYSIS REACTION; IMMOBILIZED BIOCATALYSTS; IMMOBILIZED ENZYME; INITIAL CONCENTRATION; IONIC EXCHANGE; LACTOSE HYDROLYSIS; MICHAELIS-MENTEN MODEL; SODIUM-ACETATE BUFFER; THERMAL DEACTIVATION; THERMAL STABILITY;

ACTIVATION ENERGY; ALDEHYDES; ASPERGILLUS; CONCENTRATION (PROCESS); ENZYME ACTIVITY; HYDROLYSIS; ION EXCHANGE; KINETICS; RESINS; THERMODYNAMIC STABILITY; VOLATILE FATTY ACIDS;

SUGARS;

ACETIC ACID; BETA GALACTOSIDASE; GALACTOSE; GLUCOSE; GLUTARALDEHYDE; ION EXCHANGE RESIN; LACTOSE;

ARTICLE; ASPERGILLUS ORYZAE; BIOCATALYST; CROSS LINKING; ENZYME ACTIVITY; ENZYME IMMOBILIZATION; ENZYME STABILITY; HYDROLYSIS KINETICS; NONHUMAN; TEMPERATURE; THERMOSTABILITY;

ASPERGILLUS ORYZAE;

EID: 79958017523     PISSN: 13811177     EISSN: 18733158     Source Type: Journal    
DOI: 10.1016/j.molcatb.2011.04.010     Document Type: Article

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