Di- and oligosaccharide substrate specificities and subsite binding energies of pig intestinal glucoamylase-maltase.

@article{Gnther1998DiAO,
  title={Di- and oligosaccharide substrate specificities and subsite binding energies of pig intestinal glucoamylase-maltase.},
  author={Stefan G{\"u}nther and Hans Heymann},
  journal={Archives of biochemistry and biophysics},
  year={1998},
  volume={354 1},
  pages={111-6}
}
The substrate specificity of pig intestinal glucoamylase-maltase was investigated. The alpha-1, beta-2-glycosidic bond of the disaccharide sucrose was not hydrolyzed. Various substrates with alpha-1,4-glycosidic bonds (maltose, maltooligosaccharides) were hydrolyzed with high maximal reaction velocities. Reduction lowered the rate of hydrolysis drastically: k'0 decreases from 75 s-1 for maltose to 3 s-1 for maltitol while the K(m) value increases from 4.2 to 50 mM. Leucrose with alpha-1,5… CONTINUE READING

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