Lactose-hydrolyzing beta-glycosidases of barley meal.
A beta-glucosidase and a beta-galactosidase were purified to homogeneity from barley meal. The beta-glucosidase is a single basic polypeptide (pI greater than 8.5) with an Mr of 53,000 acting optimally at pH 4.5-5.0. The beta-galactosidase is composed of two subunits with an Mr of 42,000 and 33,000, respectively, and is acidic in nature (pI less than 5.7). Both enzymes are able to hydrolyze lactose with Michaelis constants lower than the concentration of this sugar in milk whey. Consequently, barley seems to be an inexpensive source of lactose-splitting enzymes.
D005696:Galactosidases / Q000378:metabolism*; D005959:Glucosidases / Q000378:metabolism*; D001467:Hordeum; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D007700:Kinetics; D007785:Lactose / Q000378:metabolism*; D008970:Molecular Weight; D010944:Plants / Q000201:enzymology*; D013379:Substrate Specificity; D001616:beta-Galactosidase / Q000378:metabolism*; D001617:beta-Glucosidase / Q000378:metabolism*
D005696:Galactosidases; D005959:Glucosidases; D001617:beta-Glucosidase; D001616:beta-Galactosidase; D007785:Lactose