Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

We examined the inhibitory effects of aqueous ethanol extract from mulberry leaves (ME) on postprandial hyperglycemia in normal Wistar rats. ME dose-dependently suppressed the postprandial rise of blood glucose in rats, when ME (0.02-0.5 g/kg) was given 0.5 h before the administration of carbohydrates such as sucrose, maltose and starch. The ME dose showing 50% inhibition of the increment of blood glucose (ED50) was 0.11 g/kg for sucrose, 0.44 g/kg for maltose, and 0.38 g/kg for starch. ME and its basic fraction (MB) containing 1-deoxynojirimycin were assayed for their inhibitory effects (IC50) on disaccharidase derived from the small intestine of rats. The IC50 value of ME was 3.2 microg/mL for sucrase, 10 microg/mL for isomaltase, and 51 microg/mL for maltase. The IC50 value of MB was 0.36 microg/mL for sucrase, 1.1 microg/mL for isomaltase, and 6.2 microg/mL for maltase. The IC50 value of 1-deoxynojirimycin as the principle component in ME was 0.015 microg/mL for sucrase and 0.21 microg/mL for maltase, and this value was comparable to the IC50 of voglibose. The inhibitory activity of ME in a-amylase was weak. These results suggest that ME strongly suppresses postprandial hyperglycemia after carbohydrate loading by inhibiting the activity of disaccharidases in the small intestine of rats.
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PMID:Inhibitory effects of mulberry leaf extract on postprandial hyperglycemia in normal rats. 1538 27

The 40% ethanol eluent of the fraction of hot-water extract from adzuki beans (EtEx.40) adsorbed onto DIAION HP-20 resin has many biological activities, for example, antioxidant, antitumorigenesis, and intestinal alpha-glucosidase suppressing activities. This study examined the inhibitory effect of EtEx.40 on experimental lung metastasis and the invasion of B16-BL6 melanoma cells. EtEx.40 was found significantly to reduce the number of tumor colonies. It also inhibited the adhesion and migration of B16-BL6 melanoma cells into extracellular matrix components and their invasion into reconstituted basement membrane (matrigel) without affecting cell proliferation in vitro. These in vivo data suggest that EtEx.40 possesses a strong antimetastatic ability, which might be a lead compound in functional food development.
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PMID:Potential ability of hot water adzuki (Vigna angularis) extracts to inhibit the adhesion, invasion, and metastasis of murine B16 melanoma cells. 1578 70

The Inactivation kinetics of alpha-glucosidase, glucoamylase, alpha-amylase, and acid carboxypeptidase in fresh sake using a continuous flow system for high-pressure carbonation were investigated. In addition, the effects of ethanol and sugar concentrations on inactivation of the enzymes in high-pressure carbonated sake were investigated. Among the enzymes investigated, alpha-glucosidase was the most stable and alpha-amylase was the most labile on inactivation under carbonation. The decimal reduction times (D values) of alpha-glucosidase, glucoamylase, alpha-amylase (extrapolated from the Z value), and acid carboxypeptidase were 29, 6, 2, and 5 min respectively at 45 degrees C. These values are lower than those subjected to heat treatment. On the carbonation treatment as well as the heat treatment, ethanol accelerated the inactivation of all four enzymes, but glucose depressed the inactivation of these enzymes, except for acid carboxypeptidase. These results suggest that this continuous flow system enabled effective inactivation of enzymes in fresh sake.
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PMID:Inactivation of enzymes in fresh sake using a continuous flow system for high-pressure carbonation. 1630 90

Mutants of an industrial-type strain of Saccharomyces cerevisiae which rapidly and completely fermented equimolar mixtures of glucose and galactose to ethanol were isolated. These mutants fell into two general phenotypic classes based upon their fermentation kinetics and enzyme induction patterns. One class apparently specifically effects the utilization of galactose and allows sequential utilization of first glucose and then galactose in an anaerobic fermentation. The second class of mutants was resistant to general catabolite repression and produced maltase, invertase, and galactokinase in the presence of repressive levels of glucose. These mutants were completely dominant and appear to represent an as yet undescribed class of mutant.
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PMID:Saccharomyces cerevisiae Mutants Resistant to Catabolite Repression: Use in Cheese Whey Hydrolysate Fermentation. 1634 92

The production of alpha-amylase, pullulanase, and alpha-glucosidase and the formation of fermentation products by the newly isolated thermophilic Clostridium sp. strain EM1 were investigated in continuous culture with a defined medium and an incubation temperature of 60 degrees C. Enzyme production and excretion were greatly influenced by the dilution rate and the pH of the medium. The optimal values for the formation of starch-hydrolyzing enzymes were a pH of 5.9 and a dilution rate of 0.075 to 0.10 per h. Increase of the dilution rate from 0.1 to 0.3 per h caused a drastic drop in enzyme production. The ethanol concentration and optical density of the culture, however, remained almost constant. Growth limitation in the chemostat with 1% (wt/vol) starch was found optimal for enzyme production. Under these conditions 2,800 U of pullulanase per liter and 1,450 U of alpha-amylase per liter were produced; the amounts excreted were 70 and 55%, respectively.
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PMID:Production of Thermostable alpha-Amylase, Pullulanase, and alpha-Glucosidase in Continuous Culture by a New Clostridium Isolate. 1634 93

In the current study, we screened 7 clonal lines from single seed phenotypes of Lamiaceae family for the inhibition of alpha-amylase, alpha-glucosidase and angiotensin converting enzyme (ACE) inhibitory activity. Water extracts of oregano had the highest alpha-glucosidase inhibition activity (93.7%), followed by chocolate mint (85.9%) and lemon balm (83.9%). Sage (78.4 %), and three different clonal lines of rosemary: rosemary LA (71.4%), rosemary 6 (68.4%) and rosemary K-2 (67.8%) also showed significant alpha-glucosidase inhibitory activity. The alpha-glucosidase inhibitory activity of the extracts was compared to selected specific phenolics detected in the extracts using HPLC. Catechin had the highest alpha-glucosidase inhibitiory activity (99.6 %) followed by caffeic acid (91.3 %), rosmarinic acid (85.1%) and resveratrol (71.1 %). Catechol (64.4%), protocatechuic acid (55.7%) and quercetin (36.9%) also exhibited significant alpha-glucosidase inhibitory activity. Results suggested that alpha-glucosidase inhibitory activity of the clonal extracts correlated to the phenolic content, antioxidant activity and phenolic profile of the extracts. The clonal extracts of the herbs and standard phenolics tested in this study did not have any effect on the alpha-amylase activity. We also investigated the ability of the clonal extracts to inhibit rabbit lung angiotensin I-converting enzyme (ACE). The water extracts of rosemary, rosemary LA had the highest ACE inhibitory activity (90.5%), followed by lemon balm (81.9%) and oregano (37.4 %). Lower levels of ACE inhibition were observed with ethanol extracts of oregano (18.5 %) and lemon balm (0.5 %). Among the standard phenolics only resveratrol (24.1 %), hydroxybenzoic acid (19.3 %) and coumaric acid (2.3 %) had ACE inhibitory activity.
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PMID:Evaluation of clonal herbs of Lamiaceae species for management of diabetes and hypertension. 1650 Aug 86

In the current study, we investigated 2 species of the genus Rhodiola for the inhibition of alpha-amylase,alpha-glucosidase and angiotensin converting enzyme (ACE) inhibitory activity. Water extracts of Rhodiola crenulata had the highest alpha-amylase inhibitory activity (IC50,98.1 microg total phenolic /ml) followed by ethanol extract of R.crenulata (IC50, 120.9 microg total phenolic/ml) and ethanol extract of R.rosea (IC50, 173.4 microg total phenolic /ml). Ethanol R.rosea (IC50, 44.7 microg total phenolic/ml), water extract of R.rosea (IC50, 52.3 microg total phenolic/ml), water extract of R.crenulata (IC50, 60.3 microg total phenolic /ml) and ethanol extract of R.crenulata (IC50, 60.2 microg total phenolic/ml) also showed significant alpha-glucosidase inhibitory activity. The alpha-glucosidase inhibitory activity of the extracts was compared to standard tyrosol, which was significantly detected in the extracts using HPLC. Tyrosol had strong alpha-glucosidase inhibitory activity (IC50, 70.8 microg total phenolic/ml) but did not have any inhibitory effect on the alpha-amylase activity. Results suggested that alpha-glucosidase inhibitory activities of both Rhodiola extracts correlated to the phenolic content, antioxidant activity and phenolic profile of the extracts. The ability of the above Rhodiola extracts to inhibit rabbit lung angiotensin I-converting enzyme (ACE) was investigated. The ethanol extracts of R.rosea had the highest ACE inhibitory activity (38.5 %) followed by water extract of R.rosea (36.2 %) and R.crenulata (15.4 %).
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PMID:Evaluation of Rhodiola crenulata and Rhodiola rosea for management of type II diabetes and hypertension. 1683 37

A crude acerola polyphenol fraction (C-AP) was prepared by subjecting an acerola extract to a C18 cartridge column, and eluting the adsorbed fraction with ethanol containing 10% of acetic acid. C-AP appeared in a previous study to have an inhibitory effect on alpha-glucosidase and particularly on maltase activities. To elucidate the antihyperglycemic effect of C-AP further, we examined the regulation by C-AP of glucose uptake in Caco-2 cell; this resulted in the inhibition of glucose uptake. We next conducted single administration tests of glucose and maltose to ICR mice to investigate whether C-AP really controlled the intestinal glucose absorption in an animal body. The results showed that C-AP significantly suppressed the plasma glucose level after administering both glucose and maltose, suggesting that C-AP had a preventive effect on hyperglycemia in the postprandial state. The mechanism for this effect is considered to have been both suppression of the intestinal glucose transport and the inhibition of alpha-glucosidase. Despite such a preventive effect, the therapeutic effect of C-AP on hyperglycemia appeared to be low from the experiment with KKAy mice.
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PMID:Antihyperglycemic effect of polyphenols from Acerola (Malpighia emarginata DC.) fruit. 1692 91

In Saccharomyces cerevisiae, genes encoding maltose permeases and maltases are located in the telomeric regions of different chromosomes. The COMPASS methylation complex, which methylates lysine 4 on histone H3, controls the silencing of telomeric regions. Yeast strains deleted for SWD1, SWD3, SDC1, SET1, BRE2, or SPP1, encoding components of the COMPASS complex, fermented a medium containing 22% maltose with noticeably higher attenuation than did the wild type, resulting in production of up to 29% more ethanol. The least effective strain was spp1. Absence of COMPASS components had no effect on the fermentation of media with 20% glucose, 20% sucrose, or 16% maltose. Deletion of SWD3 resulted in larger amounts of MAL12 transcript, encoding maltase, at the late stages of fermentation of 22% maltose. A similar effect on maltase activity and maltose uptake capability was seen. The lysine 4 residue of histone H3 was trimethylated in wild-type cells at the late stages, while only small amounts of the dimethylated form were detected. Trimethylation and dimethylation of this residue were not detected in strains deleted for SWD1, SWD3, SET1, BRE2, or SDC1. Trimethylated lysine 4 was apparent only at the early stages (48 and 96 h) of fermentation in an spp1 strain. This work indicates that the COMPASS complex represses the expression of maltose utilization genes during the late stages of fermentation of a high concentration of maltose.
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PMID:Fermentation of high concentrations of maltose by Saccharomyces cerevisiae is limited by the COMPASS methylation complex. 1698 Apr 27

The highly osmo- and cryotolerant yeast species Torulaspora delbrueckii is an important case study among the non-Saccharomyces yeast species. The strain T. delbrueckii PYCC 5321, isolated from traditional corn and rye bread dough in northern Portugal, is considered particularly interesting for the baking industry. This paper reports the sugar utilization patterns of this strain, using media with glucose, maltose and sucrose, alone or in mixtures. Kinetics of growth, biomass and ethanol yields, fermentation and respiration rates, hydrolase activities and sugar uptake rates were used to infer the potential applied relevance of this yeast in comparison to a conventional baker's strain of Saccharomyces cerevisiae. The results showed that both maltase and maltose transport in T. delbrueckii were subject to glucose repression and maltose induction, whereas invertase was subject to glucose control but not dependent on sucrose induction. A comparative analysis of specific sugar consumption rates and transport capacities suggests that the transport step limits both glucose and maltose metabolism. Specific rates of CO(2) production and O(2) consumption showed a significantly higher contribution of respiration to the overall metabolism in T. delbrueckii than in S. cerevisiae. This was reflected in the biomass yields from batch cultures and could represent an asset for the large-scale production of the former species. This work contributes to a better understanding of the physiology of a non-conventional yeast species, with a view to the full exploitation of T. delbrueckii by the baking industry.
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PMID:Sugar utilization patterns and respiro-fermentative metabolism in the baker's yeast Torulaspora delbrueckii. 1732 10


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