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biotechnology
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Concavalin A-alpha-galactosidase complex entrapped in calcium alginate and crosslinked Concavalin A-alpha-galactosidase complex entrapped calcium alginate retain 74 and 61% activity, respectively. Crosslinked Concavalin A-alpha-galactosidase entrapped complex exhibit enhanced thermostability and show 62% of activity (38%) after 360 min at 65°C. Entrapped crosslinked Concavalin A-alpha-galactosidase complex preparation is superior in the continuous hydrolysis of oligosaccharides in soymilk by batch processes compared to the other entrapped preparations
molecular biology
alpha-galactosidase is used as a simple yet powerful reporter enzyme system in Saccharopolyspora erythraea. This reporter sytem has the distinct advantage of quantitatively measuring the level of alpha-galactosidase activity quickly and easily from culture supernatant
analysis
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comparison of glycolytic and chitinolytic enzyme activities between desert and oasis flies of Phlebotomus papatasi to evaluate potential differences in susceptibility to infection with Leishmania major
analysis
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determinantion of alpha-galactosidase A activity in samples from patients with Fabry disease and healthy controls. Average enzyme activity in dried blood spot samples prepared using EDTA tubes is higher compared to those spotted directly irrespective of disease status
degradation
enzyme completely hydrolyzes raffinose and stachyose present in soybeans and kidney beans at 50°C within 60 min
degradation
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enzyme completely hydrolyzes raffinose and stachyose present in soybeans and kidney beans at 50°C within 60 min
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medicine
Coffea sp.
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seroconversion from blood group B to 0 of human erythrocytes
medicine
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Fabry disease is a X-linked inborn error of glycolipid metabolism caused by deficiency of the lysosomal enzyme alpha-galactosidase A. An improved method of production of recombinant alpha-galactosidase A for use in humans is needed in order to develop new approaches for enzyme therapy. Purified recombinant enzyme is taken up by fibroblasts derived from fabry disease patients and normal enzyme levels can be restored under theses conditions
medicine
Fabry disease is an X-linked genetic disorder resulting from a deficiency of alpha-galactosidase activity. Correlation of structural changes and clinical and biochemical phenotypes is demonstrated. Structural investigation is useful for elucidating the bases of Fabry disease and clinical treatment
medicine
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transgenic mouse expressing human mutant alpha-galactosidase R301Q in an endogenous enzyme deficient background is a biochemical animal model for studying active site specific chaperone therapy for Fabry disease
medicine
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determinantion of alpha-galactosidase A activity in samples from patients with Fabry disease and healthy controls. Average enzyme activity in dried blood spot samples prepared using EDTA tubes is higher compared to those spotted directly irrespective of disease status
medicine
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enzyme activity is detected in unstimulated whole saliva and mainly due to isoform A activity. Activity is higher in unclarified samples than in clarified ones and shows wide daily variations. Activity in whole salivea is significantly higher than in glandular saliva. There is no difference in activity according to gender, blood type, and secretor status
medicine
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Fabry disease is a lysosomal storage disorder caused by deficient lysosomal alpha-galactosidase A activity. Rapid degradation of mutant R301Q is observed in TgM/KO mouse fibroblasts treated with brefeldin A, and the amount of R301Q enzyme markedly increases by pretreatment with 1-deoxygalactonojirimycin starting 12 h prior to addition of brefeldin A. The enhancement of alpha-galactosidase A activity and its protein level by 1-deoxygalactonojirimycin-treatment is selectively observed in brefeldin A-treated COS-7 cells expressing R301Q
medicine
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in male patients with Fabry disease, an X-linked disorder of glycosphingolipid metabolism caused by deficient activity of the lysosomal enzyme alpha-galactosidase A, treatment with agalsidase alfa, i.e. alpha-galactosidase A produced by gene activation in a human cell line, does not affect proteinuria. Agalsidase alfa may stabilize kidney function
medicine
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in patients with sporadic Parkinson's disease, the activities of alpha-D-galactosidase A are significantly decreased, compared to age- and sex-matched healthy controls. No significant differences in activities of other ten lysosomal acid hydrolases are observed
medicine
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T-cells from normal controls resond with 28% increase in alpha-galactosidase activity to treatment with 1-deoxygalactonojirimycin. In cells from patients with Fabry disease, response depends on he mutantion and ranges from no increase to fully normal activity. In normal cells and in cells from patients responding more than 25%, an increase in the mature lysosomal form of enzyme is observed after treatment. In the group of intermediate respoders with increases of 7-25% in activity upon treatment, an increase in protein stain but incomplete processing of the enzyme to the mature form is detected
medicine
the enzyme is used for Fabry disease diagnosis, since in leukocytes, pre-incubation at 50°C for 60 min is effective to differentiate Fabry disease patients from healthy controls
nutrition
Coffea sp.
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nutrition
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soymilk processing
nutrition
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beet sugar refining
nutrition
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food ingredients containing alpha-1,6-galactoside bond elicit gastrointestinal disturbances in monogastric animals, including humans. Pretreatment of such ingredients with alpha-galactosidase has the potential to alleviate this condition
nutrition
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potential for the removal of raffinose and stachyose from soymilk
nutrition
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in soymilk, Lactobacillus curvatus R08 completely hydrolyzes the non-digestive oligosaccharides after 18-24 h of fermentation. The abilities to degrade raffinose sugars and, particularly, to produce organic acids from sugar, could contribute to reductions in the anti-nutritional properties of soy, and to the accumulation of compounds with beneficial properties during food processing
nutrition
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in soymilk, Leuconostoc mesenteroides JK55 completely hydrolyzes the non-digestive oligosaccharides after 18-24 h of fermentation. The abilities to degrade raffinose sugars and, particularly, to produce organic acids from sugar, could contribute to reductions in the anti-nutritional properties of soy, and to the accumulation of compounds with beneficial properties during food processing
nutrition
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incubation of intracellular enzyme with soy milk for 6 h at 55°C reduces stachyose and raffinose amounts by 100% and 73%, respectively
nutrition
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in soymilk, Lactobacillus curvatus R08 completely hydrolyzes the non-digestive oligosaccharides after 18-24 h of fermentation. The abilities to degrade raffinose sugars and, particularly, to produce organic acids from sugar, could contribute to reductions in the anti-nutritional properties of soy, and to the accumulation of compounds with beneficial properties during food processing
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nutrition
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in soymilk, Leuconostoc mesenteroides JK55 completely hydrolyzes the non-digestive oligosaccharides after 18-24 h of fermentation. The abilities to degrade raffinose sugars and, particularly, to produce organic acids from sugar, could contribute to reductions in the anti-nutritional properties of soy, and to the accumulation of compounds with beneficial properties during food processing
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nutrition
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incubation of intracellular enzyme with soy milk for 6 h at 55°C reduces stachyose and raffinose amounts by 100% and 73%, respectively
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synthesis
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production of extracellular alpha-galactosidase by solid-state fermentation. Soybean flour is the best solid substrate, and packed-bed bioreactors perform well giving a yield of 197 U/gds, with a forced aeration of 2 vvm. Highest yield is obtained after 96 h of incubation
synthesis
the mutant is an efficient alpha-galactosynthase producing different galactosylated disaccharides from beta-galactosyl-azide donors and 4-nitrophenyl-alpha-and beta-glycosides as acceptors
synthesis
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the mutant is an efficient alpha-galactosynthase producing different galactosylated disaccharides from beta-galactosyl-azide donors and 4-nitrophenyl-alpha-and beta-glycosides as acceptors
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