Showing papers on "Arabitol published in 1969"
TL;DR: In this article, the inhibition of crystalline d-xylose isomerase from Lactobacillus brevis by pentitols and carbohydrate derivatives has been examined, and the kinetic data indicate that the substrate, d xylose, and these inhibitors combine at the active site(s) through a manganous ion bridge.
52 citations
TL;DR: At 50 °C, particulate-bound β-1,3-glucanase hydrolyzes most of the glucan previously formed at 22 °C in the presence of glycerol, leaving a resistant glucan residue.
Abstract: Glucan synthesis from uridine diphosphate glucose (UDP-glucose), mediated by particulate-bound enzyme from a variety of plants, is stimulated by a number of sugars and glycols. Glucose and glycerol appear to have a common site of action. Erythritol competitively inhibits glycerol-stimulated glucan synthesis. A marked disparity in stimulation by optical isomers of arabitol is indicative of a stereospecific activator mechanism.At 50 °C, particulate-bound β-1,3-glucanase hydrolyzes most of the glucan previously formed at 22 °C in the presence of glycerol, leaving a resistant glucan residue. Glucan formed in the absence of glycerol was not hydrolyzed.The supernatant above the 12 000 × g particulate fraction contains a heat-stable stimulator, and a heat-labile inhibitor, of glucan synthesis.
13 citations
4 citations