Improvement of the stability of alcohol dehydrogenase by covalent immobilization on glyoxyl-agarose

Bolívar, Juan M.; Wilson, Lorena; Ferrarotti, Susana Alicia; Guisán, José M.; Fernández‐Lafuente, Roberto; Mateo, César

doi:10.1016/j.jbiotec.2006.01.028

Cited by 87 publications

(51 citation statements)

References 36 publications

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“…Among those 29 lysine residues, at least 9 lysine residues per subunit are fairly exposed on the same surface plane to readily react to the carrier surface. Therefore, the higher number of potential reactive groups on the enzyme surface, together the features of glyoxyl chemistry, favor the multipoint covalent attachment that intensively rigidifies GlyDH-Gs tertiary structure as it has been reported for many other enzymes (Bolivar et al, 2006;Rocha-Martín et al, 2012b). In the light of these results, we selected GlyDH-Gs immobilized on Ag-G under the optimal immobilization conditions for further experiments.…”

Section: Study Of the Thermal Stability Of Several Glydhs Immobilizedmentioning

confidence: 94%

Selective oxidation of glycerol to 1,3-dihydroxyacetone by covalently immobilized glycerol dehydrogenases with higher stability and lower product inhibition

Rocha-Martín

Acosta

Berenguer

et al. 2014

Bioresource Technology

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Section: Study Of the Thermal Stability Of Several Glydhs Immobilizedmentioning

confidence: 94%

Selective oxidation of glycerol to 1,3-dihydroxyacetone by covalently immobilized glycerol dehydrogenases with higher stability and lower product inhibition

Rocha-Martín

Acosta

Berenguer

et al. 2014

Bioresource Technology

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“…Multipoint attachment of polysaccharides increases the rigidity, as well as hydration of these molecules [10][11][12]. Dextrans are a kind of polysaccharides containing mainly α-1,6 and variable numbers of α-1,2, α-1,3, and α-1,4 linkages between glucose units [13,14].…”

mentioning

confidence: 99%

Glucose Oxidase-dextran Conjugates with Enhanced Stabilities Against Temperature and pH

Altıkatoğlu

Basaran

Ariöz

et al. 2010

Appl Biochem Biotechnol

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Multipoint covalent bonding of glucose oxidase (EC 1.1.3.4) to hydrophilic natural polymer dextran and optimization of procedures to obtain, with enhanced temperature and pH stabilities, were studied. Purified enzyme was conjugated with various molecular weight dextrans (17.5, 75, and 188 kD) in a ratio of 20:1, 10:1, 1:1, 1:5, 1:10, 1:15, and 1:20. After 1 h of incubation at pH 7, the activities of purified enzyme and conjugates were determined at different temperatures (25 degrees C, 30 degrees C, 35 degrees C, 40 degrees C, 50 degrees C, 60 degrees C, 70 degrees C, and 80 degrees C), and the results were evaluated for thermal resistance. Increases in temperature from 25 degrees C to 50 degrees C did not change the activities of the conjugates. The conjugate, which was prepared with 75 kDa dextran in a molar ratio of 1:5, showed the highest thermal resistance and even the activity still remains at 80 degrees C at pH 7.0. This conjugate also displayed activity in a wide pH range (pH 4.0-7.0) at high temperatures. Conjugate, which was synthesized with 75 kDa dextran in a molar ratio of 1:5, appears to be feasible and useful for biotechnological applications.

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“…Only a few examples using covalent binding are described [9,10]. The support (carrier) used included a synthetic organic polymer, a biopolymer, or an inorganic solid [11][12][13][14].…”

mentioning

confidence: 99%

Characterization of Alcohol Dehydrogenase from Permeabilized Brewer's Yeast Cells Immobilized on the Derived Attapulgite Nanofibers

Zhao

Hou

Gong

et al. 2009

Appl Biochem Biotechnol

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Alcohol dehydrogenase (ADH) from permeabilized brewer's yeast was immobilized on derived attapulgite nanofibers via glutaraldehyde covalent binding. The effect of immobilization on ADH activity, optimum temperature and pH, thermal, pH and operational stability, reusability of immobilized ADH, and bioreduction of ethyl 3-oxobutyrate (EOB) to ethyl(S)-3-hydroxybutyrate ((S)-EHB) by the immobilized ADH were investigated. The results show the immobilized ADH retained higher activity over wider ranges of pH and temperature than those of the free. The optimum temperature and pH were 7.5 and 35 degrees C, respectively, and 58% of the original activity was retented after incubation at 35 degrees C for 32 h. More importantly, in bioreduction of EOB mediated by immobilized ADH, the conversion of substrate and enantiomeric excess (ee) of product reached 88% and 99.2%, respectively, within 2 h and retained about 42% of the initial activity after eight cycles.

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Improvement of the stability of alcohol dehydrogenase by covalent immobilization on glyoxyl-agarose

Cited by 87 publications

References 36 publications

Selective oxidation of glycerol to 1,3-dihydroxyacetone by covalently immobilized glycerol dehydrogenases with higher stability and lower product inhibition

Selective oxidation of glycerol to 1,3-dihydroxyacetone by covalently immobilized glycerol dehydrogenases with higher stability and lower product inhibition

Glucose Oxidase-dextran Conjugates with Enhanced Stabilities Against Temperature and pH

Characterization of Alcohol Dehydrogenase from Permeabilized Brewer's Yeast Cells Immobilized on the Derived Attapulgite Nanofibers

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