Characteristics of immobilized urease onto modified zirconium (IV) oxide via glutaraldehyde: kinetic, stability, and operational stabilities in bioreactors

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Keyword(s):  
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Vol 224 (2) ◽  
pp. 577-580 ◽  
Author(s):  
M Madden ◽  
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C Thorpe

Pig kidney general acyl-CoA dehydrogenase is markedly stabilized against loss of flavin and activity in 7.3 M-urea or at 60 degrees C upon reduction with sodium dithionite or octanoyl-CoA. Electron transferring flavoprotein is similarly stabilized, whereas egg white riboflavin-binding protein loses flavin more readily on reduction. These and other data support the anticipated correlation between the kinetic stability of the holoproteins and the oxidation-reduction potential of their bound flavins.


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Vol 432 ◽  
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Musti J. Swamy ◽  
...  
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Vol 24 (5) ◽  
pp. 056103 ◽  
Author(s):  
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