نتایج جستجو برای: amylase inhibition
تعداد نتایج: 338032 فیلتر نتایج به سال:
Alpha amylase inhibitors derived from plants pose a new commercial dimension in designing potent drug targets for the treatment of postprandialhyper glycemia (PPHG), a major concern for type-2 Diabetes. A large number of traditionally known medicinal plants are being screened for their natural amylase inhibitors. The present study was carried out to screen six ornamental plants wildly grown in ...
Kidney beans, Phaseolus vulgaris, contain a proteinaceous inhibitor of a-amylase, which we have named phaseolamin. The inhibitor has been purified to homogeneity by conventional protein fractionation methods involving heat treatment, dialysis, and chromatography on DEAE-cellulose, Sephadex G-100, and CM-cellulose. Phaseolamin is specific for animal a-amylases, having no activity towards the cor...
It is believed that the inhibition of carbohydrate hydrolyzing enzymes including α-amylase and α-glucosidase is one of the therapeutic approaches to decrease the postprandial glucose level after a meal, especially in the people with type 2 diabetes. Medicinal plants and their extracts are one of the main sources to find new inhibitors to the enzymes. In our study four flavonoids, namely luteoli...
Background: The mechanism of hypoglycemic and hypolipidemic activities of Pyrus biossieriana Buhse leaf extract (PbBLE) and its phytochemical component arbutin, have not been well determined. The present study was performed to understand the hypoglycemic activity mechanisms of pbBLE and arbutin more clearly.Methods: In vitro enzymatic carbohydrate digestion with PbBLE and arbutin was assessed u...
Kidney beans, Phaseolus vulgaris, contain a proteinaceous inhibitor of alpha-amylase, which we have named phaseolamin. The inhibitor has been purified to homogeneity by conventional protein fractionation methods involving heat treatment, dialysis, and chromatography on DEAE-cellulose, Sephadex G-100, and CM-cellulose. Phaseolamin is specific for animal alpha-amylases, having no activity towards...
α-Amylase from Trichoderma harzianum was covalently immobilized on activated wool by cyanuric chloride. Immobilized α-amylase exhibited 75% of its initial activity after 10 runs. The soluble and immobilized α-amylases exhibited maximum activity at pH values 6.0 and 6.5, respectively. The immobilized enzyme was more thermally stable than the soluble one. Various substrates were hydrolyzed by imm...
background: the mechanism of hypoglycemic and hypolipidemic activities of pyrus biossieriana buhse leaf extract (pbble) and its phytochemical component arbutin, have not been well determined. the present study was performed to understand the hypoglycemic activity mechanisms of pbble and arbutin more clearly.methods: in vitro enzymatic carbohydrate digestion with pbble and arbutin was assessed u...
it is now believed that the inhibition of carbohydrate hydrolyzing enzymes (ches) in the digestive tract can significantly prolong the overall carbohydrate digestion time and decrease the postprandial hyperglycemia after a meal. therefore, inhibitors of ches can be useful therapeutic approaches in the management of diabetes mellitus, especially in the type 2, and complications associated with t...
Midgut α-amylase is an important digestive enzyme involved in larval energy metabolism and carbohydrate assimilation. In this article, the properties of midgut α-amylase from the Oriental armyworm, Mythimna separata (Lepidoptera: Noctuidae), larvae were characterized, and its in vitro responses to chemical inhibitors were also determined. The kinetic parameters Km and Vmax of midgut α-amylase w...
Alpha-amylase was immobilized onto polyaniline-polyvinyl alcohol (PAni-PVA) film by cross linking with glutaraldehyde. The activity yield and immobilization efficiency was calculated as 13.58% and 30.60% respectively. The PAni-PVA-Amylase films were characterized by Fourier Transform Infrared Spectroscopy (FTIR) and amylase activity assay. The immobilized α-amylase had its optimum activity at p...
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