Effect of organic cosolvents on the stability and activity of the beta-1,4-galactosyltransferase from bovine colostrum.
S Riva, B Sennino, F Zambianchi, B Danieli, L Panza
Index: Carbohydr. Res. 305 , 525, (1998)
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Abstract
The influence of various organic cosolvents on the stability and activity of the beta-1,4-galactosyltransferase from bovine colostrum (GalT) and of its ancillary enzyme UDP-galactose-4'-epimerase has been investigated using the glucosylated alkaloid colchicoside (1) as a model substrate. It has been found that some cosolvents, such as Me2SO and MeOH, can be used up to 20% v/v without any influence on the performance of these enzymes, while others, such as tetrahydrofuran, rapidly inactivated GalT at concentrations as low as 5% v/v. These results have been exploited for the galactosylation of the poorly water soluble coumarinic glucoside fraxin (2).
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