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...

the experiment was conducted to determine α-amylase activity and the effect of seven plant species extracts including punica granatum l. (punicaceae), rheum officinale b. (polygonaceae), rhus coriaria l. (anacardiaceae), artemisia sieberi b. ( compositae), peganum harmala l. (nitrariaceae) , datura stramonium l. (solanaceae) and thymus vulgaris l. (lamiaceae) on α-amylase activity of four store...

the experiment was conducted to determine α-amylase activity and the effect of seven plant species extracts including punica granatum l. (punicaceae), rheum officinale b. (polygonaceae), rhus coriaria l. (anacardiaceae), artemisia sieberi b. ( compositae), peganum harmala l. (nitrariaceae) , datura stramonium l. (solanaceae) and thymus vulgaris l. (lamiaceae) on α-amylase activity of four store...

BACKGROUND The miswak (Salvadora persica) is a natural toothbrush. It is well known that very little information has been reported on enzymes in miswak as medicinal plant. Recently, we study peroxidase in miswak. In the present study, the main goal of this work is to purify and characterize α-amylase from miswak. The second goal is to study the storage stability of α-amylase in toothpaste. ME...

We propose a method of activating an enzyme utilizing heat generation from ferromagnetic particles under an ac magnetic field. We immobilize α-amylase on the surface of ferromagnetic particles and analyze its activity. We find that when α-amylase/ferromagnetic particle hybrids, that is, ferromagnetic particles, on which α-amylase molecules are immobilized, are subjected to an ac magnetic field,...

The aim of this study was production and partial purification of α-amylase enzyme by Bacillus licheniformis. B. Licheniformis was allowed to grow in broth culture for purpose of inducing α-amylase enzyme. Optimal conditions for amylase production by B. Licheniformis are incubation period of 120 h, temperature of 37 °C and pH 7.0. The α-amylase enzyme was purified by ion exchange chromatography ...

The side effects associated with the usage of synthetic antidiabetic drugs make it imperative to search for alternative drugs from medicinal plants. Therefore, this study was aimed at evaluating the α-amylase and α-glucosidase inhibitory potential of Calotropis procera leaf, as well as its possible mode of inhibiting these enzymes. Acetone, aqueous and ethanolic extracts of C. procera leaf was ...

the aim of this study was production and partial purification of α-amylase enzyme by bacillus licheniformis. b. licheniformis was allowed to grow in broth culture for purpose of inducing α-amylase enzyme. optimal conditions for amylase production by b. licheniformis are incubation period of 120 h, temperature of 37 °c and ph 7.0. the α-amylase enzyme was purified by ion exchange chromatography ...

This study was designed to investigate the inhibitory effects of Polyopes lancifolia extract (PLE) on α-glucosidase activity, α-amylase activitiy, and postprandial hyperglycemia in streptozotocin (STZ)-induced diabetic mice. The results of this study revealed a marked inhibitory effect of PLE on α-glucosidase and α-amylase activities. The IC50s of PLE against α-glucosidase and α-amylase were 0....

In the major salivary glands of mice, acinar cells in the parotid gland (PG) are known to be the main site for the production of the digestive enzyme α-amylase, whereas α-amylase production in the submandibular gland (SMG) and sublingual gland (SLG), as well as the cell types responsible for α-amylase production, has been less firmly established. To clarify this issue, we examined the expressio...