Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.20 (alpha-glucosidase)
4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Feeding manufactured liquid diets to early-weaned pigs improves growth performance and reduces days to market weight compared with pigs receiving pelleted dry feed. Few alternative dietary ingredients are utilized in manufactured liquid diets other than byproducts of the dairy industry, especially for sources of carbohydrates. This experiment was designed to evaluate the efficacy of starch from partially hydrolyzed corn syrup solids (CSS), at two different levels of hydrolyzation, as a replacement for lactose in manufactured liquid diets. Forty-eight pigs were removed from sows at 1 d of age and randomly assigned to one of three treatments: 1) control with lactose as the carbohydrate source, 2) lactose replaced (gram for gram) with CSS (dextrose equivalent [DE]-20), and 3) lactose replaced with DE-42. In addition, 10 pigs were randomly removed from several litters to provide estimates of initial body composition and small intestinal variables. Twenty-four pigs were removed from the study on d 10 of treatment, and the remaining 24 pigs were removed on d 20 of treatment. Pigs averaged 9,845 +/- 191 g at d 20 of treatment regardless of dietary treatment (P > 0.20). No differences in ADG, ADFI, or feed efficiency were detected between treatment groups from d 0 to 20 (P > 0.19). Whole-body water, protein, lipid, and ash accretion rates were unaffected by dietary treatment from d 0 to 10 or from d 0 to 20 (P > 0.20). The replacement of lactose with CSS did not affect intestinal villi height or width, or crypt depth (P > 0.10). Pigs fed lactose tended to have greater lactase activity on d 10 than pigs fed CSS (P < 0.07). Also, pigs fed lactose tended to have lower oligosaccharidase activity than pigs fed the DE-20 diet on d 20 (P < 0.07). No other differences in lactase, maltase, or long oligosaccharidase specific activity on d 10 or 20 of treatment were detected (P > 0.12). Plasma urea nitrogen concentrations were unaffected by diet on d 10 and 20 of treatment. In addition, dry matter digestibility of the diets averaged approximately 85.6 +/- 0.8% and was unaffected by dietary treatment or day of treatment. These results suggest that partially hydrolyzed CSS can be used as a replacement for lactose in manufactured liquid diets for neonatal pigs.
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PMID:Efficacy of partially hydrolyzed corn syrup solids as a replacement for lactose in manufactured liquid diets for neonatal pigs. 1183 12

Plant extracts from the Salacia genus have been found to have intestinal alpha-glucosidase inhibitor activity, which may have application to the development of medical foods for people with diabetes. We evaluated the safety of a hot water extract of S. oblonga (salacinol extract) supplemented to or processed into a medical food. Thirty male Sprague-Dawley rats were assigned among one of three treatments: (1) EN-0178 (control, liquid diet), (2) EN-0178+salacinol (as 1 plus 500 mg of salacinol extract per 253 g diet, which was added to product immediately prior to feeding), (3) EN-0195 (as 1 plus 500 mg of salacinol extract per 253 g diet, which was added during product manufacture). After 14 days of free access to dietary treatments, rats were sacrificed, blood collected and organs weighed. Rats consuming salacinol extract had reduced (P <0.05) weight gain and feed intake. The relative (% of body weight) testicular weight was higher (P<0.05) for rats consuming salacinol extract, whereas, the relative liver and spleen weight was lower (P<0.05) for rats consuming salacinol extract. Of the serum chemistries analyzed, blood urea nitrogen and alkaline phosphatase was lower (P<0.05) for rats consuming salacinol extract. No differences in blood hematology were found. We conclude that salacinol extract, in a medical food consumed for 2 weeks in amounts estimated at 10-fold greater than proposed for human intake, did not result in clinical chemistry or histopathologic indications of toxic effects in male Sprague-Dawley rats.
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PMID:Safety evaluation of an extract from Salacia oblonga. 1273 92

4-Methylumbelliferyl-alpha-D-glucoside, the fluorogenic substrate of alpha-glucosidase, was used as a selective marker to develop a differential medium for Enterobacter sakazakii. This bacterium showed strong fluorogenic characteristics clearly distinguishable from other microorganisms. On the basis of reducing background noise, an optimum basal medium and nitrogen source were selected. Incubation conditions were optimized.
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PMID:Fluorogenic selective and differential medium for isolation of Enterobacter sakazakii. 1534 62

A series of 16 new chiral nonracemic polyhydroxylated piperidines was synthesized utilizing several chiral beta-amino-alcohols. They act as a nitrogen source, chirality inducer and iminium stabilizer, in the desymmetrization of meso-trihydroxylated glutaraldehyde. The biological activity of these compounds towards several glycosidases (alpha-D-glucosidase, alpha-D-mannosidase, alpha-L-fucosidase) has been evaluated.
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PMID:Synthesis of polyhydroxylated piperidines and evaluation as glycosidase inhibitors. 1535 92

Thermophilic and amylolytic aerobic bacteria were isolated from soil through a selective enrichment procedure at 60 degrees C with starch as the carbon source. One of the isolates designated as HRO10 produced glucose aside from limit dextrin as the only hydrolysis product from starch and was characterized in detail. The starch-degrading enzymes produced by strain HRO10 were determined to be alpha-amylase and alpha-glucosidase. Whereas the alpha-amylase activity was detected exclusively in the culture supernatant, alpha-glucosidase occurred intracellular, extracellular, or on the surface of the bacteria depending on the growth phase. The optimum temperature and pH required for the growth of strain HRO10 were about 50 degrees C and pH 6.5 to 7.5. The strain used different carbohydrates as the carbon source, but the maximum production of alpha-amylase occurred when 1.0% (w/v) starch or dextrin was used. The use of organic vs. inorganic nitrogen favored the production of alpha-amylase in strain HRO10. The metal ions Li+, Mg2+, and Mn2+ stimulated the production of both enzymes. Identification of strain HRO10 by physiological and molecular methods including sequencing of the 16S rDNA showed that this strain belongs to the species Geobacillus thermodenitrificans. Biochemically, strain HRO10 differs from the type strain DSM 465 only in its ability to hydrolyze starch.
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PMID:Isolation, characterization, and identification of Geobacillus thermodenitrificans HRO10, an alpha-amylase and alpha-glucosidase producing thermophile. 1623 66

Bat species in the monophyletic family Phyllostomidae feed on blood, insects, small vertebrates, nectar, fruit and complex omnivorous mixtures. We used nitrogen stable isotope ratios to characterize bat diets and adopted a phylogenetically informed approach to investigate the physiological changes that accompany evolutionary diet changes in phyllostomids. We found that nitrogen stable isotopes separated plant-eating from animal-eating species. The blood of the latter was enriched in (15)N. A recent phylogenetic hypothesis suggests that with the possible exception of carnivory, which may have evolved twice, all diets evolved only once from insectivory. The shift from insectivory to nectarivory and frugivory was accompanied by increased intestinal sucrase and maltase activity, decreased trehalase activity, and reduced relative medullary thickness of kidneys. The shift from insectivory to sanguinivory and carnivory resulted in reduced trehalase activity. Vampire bats are the only known vertebrates that do not exhibit intestinal maltase activity. We argue that these physiological changes are adaptive responses to evolutionary diet shifts.
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PMID:Diet and the evolution of digestion and renal function in phyllostomid bats. 1635 19

Protein bodies and spherosomes isolated from mature seeds of Sorghum bicolor (Linn.) Moench have measurable activity of acid protease, alpha-glucosidase, beta-glucosidase, beta-galactosidase, phytase, acid pyrophosphatase, p-nitrophenyl phosphatase, and RNase. Protein bodies have largely insoluble activities, and produce soluble protein and soluble amino nitrogen during autolysis. They have the dual function of protein storage and protein catabolism. Spherosomes have considerable amounts of soluble enzymes and autolytically produce soluble amino nitrogen and inorganic phosphate but release little soluble protein. Spherosomes are similar to animal lysosomes but have an additional storage function for protein, phosphorus, and metals. Mature sorghum seed contains the necessary enzymes and substrates to generate two basic metabolites, amino acids and inorganic phosphate.
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PMID:Acid Hydrolases and Autolytic Properties of Protein Bodies and Spherosomes Isolated from Ungerminated Seeds of Sorghum bicolor (Linn.) Moench. 1665 31

Several protein-bound uremic retention solutes (including p-cresol) originate from colonic bacterial fermentation of protein. Higher colonic availability of carbohydrates drives this process towards lower production of toxic metabolites. Small intestinal alpha-glucosidase inhibitors like Acarbose (Glucobay) enhance the amount of undigested carbohydrates reaching the colon. We studied the effect of Acarbose on generation and serum concentrations of p-cresol. Nine healthy volunteers (age 25 (22-36) years) with a creatinine clearance of 89.6 ml/min/1.73 m(2) (85.5-116.4) were treated with Acarbose for 3 weeks. Dose was gradually increased to reach 300 mg/day after 1 week. Blood sampling, 24-h urine and stool collections on 3 consecutive days were performed before and during the last days of the treatment period. p-Cresol generation was estimated from mean 24-h urinary elimination. Gastrointestinal side effects, if present, were mild to moderate. Serum concentrations of p-cresol declined significantly after Acarbose treatment (before: 1.14 mg/l (0.93-3.03); after: 1.11 mg/l (0.31-1.82); P=0.047). Urinary excretion of p-cresol, reflecting its colonic generation rate, was significantly lower after treatment (before: 29.93 mg/day (6.79-75.19); after: 10.54 mg/day (1.08-30.85); P=0.031). The fecal excretion of nitrogen increased after treatment (before: 1.04 g/day (0.47-2.29); after: 1.99 g/day (0.76-3.08); P=0.047). This pilot study suggests that Acarbose treatment lowers generation and serum concentrations of the protein-bound uremic solute p-cresol. Although further confirmation is warranted, the data may point to a novel treatment option for chronic kidney disease patients in view of the potential toxic effects of p-cresol and related substances.
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PMID:Acarbose treatment lowers generation and serum concentrations of the protein-bound solute p-cresol: a pilot study. 1668 14

The fission yeast Schizosaccharomyces pombe CBS 356 exhibits extracellular maltase activity. This activity may be of commercial interest as it exhibited a low pH optimum (3.5) and a high affinity for maltose (Km of 7.0+/-1.8 mM). N-terminal sequencing of the protein indicates that it is the product of the AGL1 gene. Regulation of this gene occurs via a derepression/repression mechanism. In sugar- or nitrogen-limited chemostat cultures, the specific rate of enzyme production (q(p)) was independent of the nature of the carbon source (i.e. glucose or maltose), but synthesis was partially repressed by high sugar concentrations. Furthermore, q(p) increased linearly with specific growth rate (mu) between 0.04 and 0.10 h(-1). The enzyme is easily mass-produced in aerobic glucose-limited fed-batch cultures, in which the specific growth rate is controlled to prevent alcoholic fermentation. In fed-batch cultures in which biomass concentrations of 83 g L(-1) were attained, the enzyme concentration reached 58,000 Units per liter culture supernatant. Extracellular maltase may be used as a dough additive in order to prevent mechanisms such as maltose-induced glucose efflux and maltose-hypersensitivity that occur in maltose-consuming Saccharomyces cerevisiae.
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PMID:Physiological characterization and fed-batch production of an extracellular maltase of Schizosaccharomyces pombe CBS 356. 1691 11

The synthesis of two novel amino acids, nitrogen analogues of the naturally occurring glycosidase inhibitor, salacinol, containing a carboxylate inner salt are described, along with the crystal structure of one of these analogues in the active site of Drosophila melanogaster Golgi mannosidase II (dGMII). Salacinol, a naturally occurring sulfonium ion, is one of the active principals in the aqueous extracts of Salacia reticulata that are traditionally used in Sri Lanka and India for the treatment of diabetes. The synthetic strategy relies on the nucleophilic attack of 2,3,5-tri-O-benzyl-1,4-dideoxy-1,4-imino l- or d-arabinitol at the least hindered carbon of 5,6-anhydro-2,3-di-O-benzyl-l-ascorbic acid to yield coupled adducts. Deprotection, stereoselective catalytic reduction, and hydrolysis of the coupled products give the target compounds. The compound derived from d-arabinitol inhibits dGMII, one of the critical enzymes in the glycoprotein processing pathway, with an IC(50) of 0.3mM. Inhibition of GMII has been identified as a target for control of metastatic cancer. An X-ray crystal structure of the complex of this compound with dGMII provides insight into the requirements for an effective inhibitor. The same compound inhibits recombinant human maltase glucoamylase, one of the key intestinal enzymes involved in the breakdown of glucose oligosaccharides in the small intestine, with a K(i) value of 21microM.
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PMID:Synthesis, enzymatic activity, and X-ray crystallography of an unusual class of amino acids. 1701 Jun 21


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