Detail of "9001-22-3"

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The role of "fecalase" in endogenous formation of quercetin from rutin as detected by the Ames assay: the effect of bile acids

The role of "fecalase" in endogenous formation of quercetin from rutin as detected by the Ames assay: the effect of bile acids. Macdonald, Ian A.; Mader, Judith A. (Dep. Med., Dalhousie Univ., Halifax, NS, Can.). Carcinog. Mutagens Environ., Volume 2, 41-52. Edited by: Stich, Hans F. CRC: Bota Raton, Fla. (English) 1983. 434-13-9 and 9032-92-2 which are cas registry numbers are also used here. CODEN: 49CGA9. DOCUMENT TYPE: Conference CA Section: 4 (Toxicology) Only a small fraction (~10%) of rutin [153-18-4] is converted to quercetin [117-39-5] during 1 h incubation with fecalase [9032-92-2] (obtained from human stool). A 1-h preincubation of rutin over a 10-fold concn. with fecalase or a cell-free prepn. of Bacteroides fragilis enhanced rutin mutagenicity ~3-fold in the absence or presence of S9, an even greater mutagenicity resulted. Fecalase prepd. in the presence of bile acids was less effective in enhancing the mutagenicity of rutin. Salivase prepns. were totally ineffective, compared to fecalase in enhancing the mutagenicity of rutin. Prepns. with a-glucosidase [9001-42-7] and a- [9025-35-8] and b-galactosidase [9031-11-2] failed to activate rutin in the Ames assay, whereas, b-glucosidase [9001-22-3] from sweet almonds enhanced the mutagenicity of rutin by 25-30%. .

Effect of glucose and other sugars on the b-1,4-glucosidase activity of Thermomonospora fusca

Effect of glucose and other sugars on the b-1,4-glucosidase activity of Thermomonospora fusca. Ferchak, John D.; Pye, E. Kendall (Sch. Med., Univ. 90-80-2 and 9001-22-3 are also occured in this study. Pennsylvania, Philadelphia, PA 19104, USA). Biotechnol. Bioeng., 25(12), 2855-64 (English) 1983. CODEN: BIBIAU. ISSN: 0006-3592. DOCUMENT TYPE: Journal CA Section: 17 (Food and Feed Chemistry) Section cross-reference(s): 7 The cell-assocd. b-glucosidase [9001-22-3] activity of T. fusca, strain YX, showed both p-nitrophenyl-b-D-glucosidase (I) [9001-22-3] and cellobiase [9001-22-3] activities. The cellobiase activity was found by high-pressure liq. chromatog. assay to have very low product inhibition, whereas the I activity was inhibited more significantly. Of the various sugars and sugar analogs tested for inhibition of the I activity, gluconolactone [90-80-2] had the greatest effect. The low product inhibition of the cellobiase activity was further demonstrated by the prodn. of glucose syrups at ￡20% concn. from both cellobiase and swollen cellulose [9004-34-6] (Avicel). This characteristic is of practical importance in the development of a com. process for the prodn. of glucose syrups from cellulose. Growth expts. gave further evidence for the probability of sep. enzymes for the I and cellobiase activities. .