Title: Partial purification and characterization of various β-glucosidases associated with cellular components of corn roots
Abstract: β-Glucosidases were isolated from various cellular components from corn root cortical tissue. The subcellular components were separated and the enzymes were partially purified and characterized. The pH-activity profile of the cytosolic enzyme and the unidentified particulate-associated β-glucosidase were identical. Further kinetic analyses of these two enzymes at pH 5.5 and 7.5 suggests that the unidentified particulate-associated β-glucosidase is the bound from of the cytosolic enzyme. The ionically bound cell wall enzyme (in muro) had a pH optimum of 5.5 while the free from (salt solubilized) had a pH optimum of 5.0. The enzyme kinetics of the extracellular enzymes were compared to the intracellular forms with particular reference to bound versus free enzymes. The Km values and the shape of the kinetic curves of free enzymes were not changed when enzymes were assayed in the bound state. The tightly bound cell wall enzyme had a very broad pH-activity profile and had a Km value approximately one-half the Km value of the other β-glucosidases.
Publication Year: 1991
Publication Date: 1991-01-01
Language: en
Type: article
Indexed In: ['crossref']
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Cited By Count: 2
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