Formation of enzyme polymer engineered structure for laccase and cross-linked laccase aggregates stabilization. 2013

Thanina Hassani, and Sidy Ba, and Hubert Cabana
Environmental Engineering Laboratory, Department of Civil Engineering, University of Sherbrooke, 2500 Boulevard de l'Université, Sherbrooke, Quebec, Canada J1K 2R1.

Laccase and laccase-based cross-linked enzyme aggregates (CLEAs) were stabilized through the formation of a surrounding polymeric network made of chitosan and 3-aminopropyltriethoxysilane. The thermoresistance of the resulting enzyme polymer engineered structures of laccase (EPES-lac) and CLEAs (EPES-CLEA) were more than 30 times higher than that of free laccase and CLEAs at pH 3 and 40 °C. The EPES showed higher residual activity than the unmodified biocatalysts against chaotropic salts (up to 10 times), EDTA (up to 5 times), methanol (up to 15 times) and acetone (up to 20 times). The Michaelis-Menten kinetic parameters revealed that the affinity for 2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulphonic acid) has doubled for the EPES-lac and EPES CLEA compared to their unmodified forms. The EPES-lac structures acted optimally at pH 4 and their activity was nearly temperature-independent, while the laccase activity of EPES-CLEA was optimal at pH 4 and 60 °C. Globally, the EPES have shown significantly improved properties which make them attractive candidate for the development of laccase-based applications.

UI MeSH Term Description Entries
D011437 Propylamines Derivatives of propylamine (the structural formula NH2CH2CH2CH3).
D003432 Cross-Linking Reagents Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other. Bifunctional Reagent,Bifunctional Reagents,Cross Linking Reagent,Crosslinking Reagent,Cross Linking Reagents,Crosslinking Reagents,Linking Reagent, Cross,Linking Reagents, Cross,Reagent, Bifunctional,Reagent, Cross Linking,Reagent, Crosslinking,Reagents, Bifunctional,Reagents, Cross Linking,Reagents, Cross-Linking,Reagents, Crosslinking
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D004795 Enzyme Stability The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat. Enzyme Stabilities,Stabilities, Enzyme,Stability, Enzyme
D004800 Enzymes, Immobilized Enzymes which are immobilized on or in a variety of water-soluble or water-insoluble matrices with little or no loss of their catalytic activity. Since they can be reused continuously, immobilized enzymes have found wide application in the industrial, medical and research fields. Immobilized Enzymes,Enzyme, Immobilized,Immobilized Enzyme
D012821 Silanes Compounds similar to hydrocarbons in which a tetravalent silicon atom replaces the carbon atom. They are very reactive, ignite in air, and form useful derivatives. Silane
D013696 Temperature The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms. Temperatures
D015202 Protein Engineering Procedures by which protein structure and function are changed or created in vitro by altering existing or synthesizing new structural genes that direct the synthesis of proteins with sought-after properties. Such procedures may include the design of MOLECULAR MODELS of proteins using COMPUTER GRAPHICS or other molecular modeling techniques; site-specific mutagenesis (MUTAGENESIS, SITE-SPECIFIC) of existing genes; and DIRECTED MOLECULAR EVOLUTION techniques to create new genes. Genetic Engineering of Proteins,Genetic Engineering, Protein,Proteins, Genetic Engineering,Engineering, Protein,Engineering, Protein Genetic,Protein Genetic Engineering
D042845 Laccase A copper-containing oxidoreductase enzyme that catalyzes the oxidation of 4-benzenediol to 4-benzosemiquinone. It also has activity towards a variety of O-quinols and P-quinols. It primarily found in FUNGI and is involved in LIGNIN degradation, pigment biosynthesis and detoxification of lignin-derived products. Laccase B,Laccase I,Laccase II,Laccase III,Urishiol Oxidase,p-Diphenol Oxidase,Oxidase, Urishiol,Oxidase, p-Diphenol,p Diphenol Oxidase
D048271 Chitosan Deacetylated CHITIN, a linear polysaccharide of deacetylated beta-1,4-D-glucosamine. It is used in HYDROGEL and to treat WOUNDS. Poliglusam

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