Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.21 (beta-glucosidase)
 3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Piromyces sp. strain E2, an anaerobic fungus isolated from an Indian elephant (hindgut fermenter) was tested for its ability to ferment a range of substrates. The fungus was able to use bagasse, cellobiose, cellulose, fructose, glucose, lactose, mannose, starch, wheat bran, wheat straw, xylan and xylose. Formate and acetate were the main fermentation products after growth on these substrates. The amount of carbon found in the fermentation products of cultures, in which substrate digestion was complete averaged 88.5 mM, or 59% of the carbon offered as substrate. No growth was observed on other substrates tested. Lactose, starch, cellobiose and filter paper cellulose were good inducers of cellulolytic and xylanolytic enzymes. Cellulolytic and xylanolytic enzymes were produced constitutively by Piromyces strain E2, although enzyme activities were generally lower after growth on glucose and other soluble sugars. Complex substrates (bagasse, wheat bran, and wheat straw) were good inducers for xylanolytic enzymes but not for cellulolytic enzymes. The extracellular protein banding pattern after SDS-PAGE was therefore only slightly affected by the growth substrate. Identical beta-glucosidase and endoglucanase activity patterns were found after growth on different substrates. This indicated that differences in enzyme activities were not the result of secretion of different sets of isoenzymes although it remains possible that the relative amount of each isoenzyme produced is influenced by the growth substrate.
 ...
PMID:Production of cellulolytic and xylanolytic enzymes during growth of the anaerobic fungus Piromyces sp. on different substrates. 152 5

Three different types of beta-D-galactosidase (EC 3.2.1.23) could be distinguished in rabbit tissues using electrophoretic procedures. (1) Acid beta-D-galactosidase with a low mobility and maximal activity at pH 3-5 was found in the particulate fraction of various tissue homogenates. This enzyme hydrolyzed 4-methylumbelliferyl-D-galactoside, but no activity against other glycoside substrates could be demonstrated. The enzyme was inhibited by galactono-(1 leads to 4)-lactone. (2) Lactose-hydrolyzing beta-D-galactosidase with an intermediate mobility was found only in juvenile small intestine. Most of the activity was found in the particulate fraction of the cell. The enzyme hydrolyzed several other synthetic glycoside substrates besides lactose. It was most active at pH 5-6 and strongly inhibited by glucono-(1 leads to 5)-lactone but not much affected by galactono-(1 leads to 4)-lactone. (3) Neutral beta-D-galactosidase with a fast mobility and maximal activity at pH 6-8 was found in the soluble fraction of homogenates from liver, kidney, and small intestine. This enzyme also showed a broad substrate specificity; it possessed activity against aryl-beta-D-glucoside, -fucoside, and -galactoside substrates but not against lactose. The enzyme was strongly inhibited by glucono-(1 leads to 5)-lactone and (less) by galactone-(1 leads to 4)-lactone. Neutral beta-D-galactosidase and neutral beta-D-glucosidase (EC 3.2.1.21) are probably identical enzymes in the rabbit. Individual variation, in both electrophoretic mobility and activity, was found for neutral beta-D-galactosidase. Genetic analysis of the electrophoretic variants revealed that two alleles at an autosomal locus are responsible for this variation.
 ...
PMID:Separation of beta-D-galactosidases in rabbit tissues: genetics of neutral beta-D-galactosidase. 640 44

Weanling or adult (9 wk old) rats were fed diets containing 0, 250 or 500 g lactose/kg for 10 days, after which the activities of six caecal microbial enzymes (azoreductase, beta-glucosidase, beta-glucuronidase, nitrate reductase, nitroreductase and urease) were determined. Adult controls had larger caeca than weanlings, but the numbers of bacteria were not significantly different. Expressed in relation to body weight, caecal microbial enzyme activities were significantly lower in adult controls, with the exceptions of beta-glucuronidase and urease. Lactose caused caecal enlargement; this was greatest in weanling animals, which also showed a decreased concentration of bacteria. Lactose increased total nitrate reductase and urease activities in both age groups, but decreased total azoreductase and nitroreductase activities in weanlings. Enzyme activities per 10(9) bacteria were decreased for azoreductase, beta-glucosidase, beta-glucuronidase and nitroreductase in both age groups, while urease activity increased. Azoreductase and nitroreductase activities were highly correlated but nitrate reductase and urease did not correlate significantly with any other enzyme activity.
 ...
PMID:Dietary lactose and the metabolic activity of the caecal microfloras of weanling and adult rats. 642 83