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Pectin 3-galactosidase

In tomato pericarp, the loss of pectin-associated galactose appears to occur via at least two mechanisms. One Involves the EDG-medlated release of a galactan-rich pectin, as demonstrated by Pressey (60). Pressey has also shown that a 6-galactosidase from ripe fruit will depolymerize this galactan in vitro (61), representing an EDG-independent means of gaTactose loss. Gross... [Pg.154]

Galactanases (and a- or j3-D-galactosidase), arabinases (and a-L-arabinosidase) and pectinases (polygalacturonase 5/20 species and pectin methyl-esterase 7/20 species [30] have rarely been studied. Amylase was found in almost all species tested by Gessner [30], Cuomo [16] and Rohrmann [20]. [Pg.1004]

As their name implies, hydrolysis is the preferred reaction for hydrolases in water under optimal conditions. Some exanq>les in the polysaccharide area include cellulolytic enzymes for biomass conversion (5), proteases for the degradation of guar gum (21), cellulase for viscosity reduction of xanthan gum (21), and P-D-galactosidase for pectin hydrolysis (21). [Pg.4]

A search of the literature indicated that P-D-galactosidase is known to be biologically active towards pectin (8). In fact, P-D-galactosidase is one of the enzymes involved in the ripening process of fruits (8a). Thus, the observed P-D-galactosidase activity is not inconsistent with the literature. [Pg.273]

Case 3. The enzyme is a mixture of several components. It may have one component that can react with a polymer. This is most likely the situation with P-galactosidase and pectin. [Pg.276]


See other pages where Pectin 3-galactosidase is mentioned: [Pg.79]    [Pg.767]    [Pg.373]    [Pg.374]    [Pg.15]    [Pg.34]    [Pg.148]    [Pg.19]    [Pg.378]    [Pg.153]    [Pg.132]    [Pg.139]    [Pg.26]    [Pg.79]    [Pg.177]    [Pg.267]    [Pg.273]    [Pg.275]    [Pg.276]    [Pg.235]    [Pg.462]   
See also in sourсe #XX -- [ Pg.30 , Pg.177 ]




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