![]() α-Amylase structure
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Common Name | α-Amylase | ||
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CAS Number | 9000-90-2 | Molecular Weight | N/A | |
Density | N/A | Boiling Point | N/A | |
Molecular Formula | N/A | Melting Point | N/A | |
MSDS | Chinese USA | Flash Point | N/A | |
Symbol |
![]() GHS08 |
Signal Word | Danger |
In vitro and in vivo effects of standardized extract and fractions of Phaleria macrocarpa fruits pericarp on lead carbohydrate digesting enzymes.
BMC Complement Altern. Med. 13 , 39, (2013) One vital therapeutic approach for the treatment of type 2 diabetes mellitus is the use of agents that can decrease postprandial hyperglycaemia by inhibiting carbohydrate digesting enzymes. The present study investigated the effects of bioassay-guided extract... |
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Combined effects of green tea extracts, green tea polyphenols or epigallocatechin gallate with acarbose on inhibition against α-amylase and α-glucosidase in vitro.
Molecules 18(9) , 11614-23, (2013) Green tea, green tea polyphenols and epigallocatechin gallate (EGCG) are confirmed to have beneficial effects in the treatment of diabetes mellitus, and a possible mechanism can be ascribed to their inhibitory effect against α-amylase and α-glucosidase in the... |
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alpha-Glucosidase and alpha-amylase inhibitory activities of saponins from traditional Chinese medicines in the treatment of diabetes mellitus.
Pharmazie 68(4) , 300-4, (2013) Extracts of eleven traditional Chinese medicines (TCM) with a reputation of usefulness in treating diabetes mellitus were examined for alpha-glucosidase and alpha-amylase inhibitory activities in vitro. The extract with the highest activity was selected for f... |
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In vitro inhibitory effects of Limonium contortirameum and L. virgatum extracts from sardinia on alpha-amylase, alpha-glucosidase and pancreatic lipase.
Nat. Prod. Commun. 9(2) , 181-4, (2014) Pancreatic triacylglycerol lipase (PL), alpha-amylase and alpha-glucosidase are interesting pharmacological targets for the management of dyslipidemia, atherosclerosis, and obesity-diabetes. Limonium spp (Plumbaginaceae) are endemic to Sardinia, Italy. Compar... |
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Estimation of resveratrol content in peanut pericarp and its relation to the in vitro inhibitory activity on carbohydrate metabolizing enzymes.
Pharmazie 69(2) , 92-5, (2014) The aim of this work was the estimation of resveratrol content in two successive extracts (EtOAc and MeOH) of peanuts (Arachis hypogaea L.) pericarp of Egypt, by TLC and HPLC methods. Results showed the presence of 3.0 and 0.5 microg/mL resveratrol in EtOAc a... |
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Inhibitory effect of Azadirachta indica A. juss leaf extract on the activities of alpha-amylase and alpha-glucosidase.
Pak. J. Biol. Sci. 16(21) , 1358-62, (2013) In recent decades, there has been a drastic increase in the incidence and prevalence of diabetic mellitus. The aim of this study was to evaluate the in vitro inhibitory effect of Azadirachita indica leaf extract on the activity of alpha-amylase and alpha-gluc... |
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High performance liquid chromatography coupled to mass spectrometry for profiling and quantitative analysis of folate monoglutamates in tomato.
Food Chem. 179 , 76-84, (2015) Folates are essential micronutrients for animals as they play a major role in one carbon metabolism. Animals are unable to synthesize folates and obtain them from plant derived food. In the present study, a high performance liquid chromatography coupled to ma... |
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A starch-binding domain identified in α-amylase (AmyP) represents a new family of carbohydrate-binding modules that contribute to enzymatic hydrolysis of soluble starch.
FEBS Lett. 588(7) , 1161-7, (2014) A novel starch-binding domain (SBD) that represents a new carbohydrate-binding module family (CBM69) was identified in the α-amylase (AmyP) of the recently established alpha-amylase subfamily GH13_37. The SBD and its homologues come mostly from marine bacteri... |
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A new raw-starch-digesting α-amylase: production under solid-state fermentation on crude millet and biochemical characterization.
J. Microbiol. Biotechnol. 23(4) , 489-98, (2013) A new Bacillus strain degrading starch, named Bacillus sp. UEB-S, was isolated from a southern Tunisian area. Amylase production using solid-state fermentation on millet, an inexpensive and available agro-resource, was investigated. Response surface methodolo... |
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Polymeric amylase nanoparticles as a new semi-synthetic enzyme system for hydrolysis of starch.
Mater. Sci. Eng. C. Mater. Biol. Appl. 33(4) , 1900-6, (2013) α-Amylase (EC 3.2.1.1; α-D-1,4,glucan glucanohydrolase) catalyzes the hydrolysis of α-D-(1,4)-glucosidic linkages in starch, glycogen, and various malto-oligosaccharides, by releasing α-anomeric products. In this study, a novel method has been developed to pr... |