Application of the proteinaceous .ALPHA.-amylase inhibitor Haim to horse and carp .ALPHA.-amylase purification and some properties of the purified .ALPHA.-amylase.

Purification of alpha amylase pdf

Bacterial alpha amylase pdf

Of alpha-amylases and other starch-digesting enzymes from bacteria and plants.ess was supplemented with bacterial and fungal amylases or scalded flour. Immunochemical characteristics of alpha-amylase sensitization.Alpha-amylase production and its activity was compared in two different. Bacterial amylases are resistant to high temperatures, they can active in wide pH.fungal amylascs lowest, liqu...

effects of some alpha-amylase inhibitors on the salivary alpha-amylase activity of the stripped bug, graphosoma lineatum (heteroptera: scutelleridae)

abstract digestive enzyme inhibitors are proteinacious or nonproteinacious compounds which reduce an enzyme activity through attaching to its active site and/or its substrate. nowadays, plant enzyme inhibitors are of great importance because 1) these have considerable effects on insect digestive enzymes and as a result on their development; and 2) the transgenic plants expressing them are safe....

Purification and properties of phaseolamin, an inhibitor of alpha-amylase, from the kidney bean, Phaseolus vulgaris.

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...

Production, purification, and characterization of alpha-amylase from Thermomonospora curvata.

Thermomonospora curvata produces an extracellular alpha-amylase. Maximal amylase production by cultures in a starch-mineral salts medium occurred at pH 7.5 and 53 degrees C. The crude enzyme was unstable to heating (65 degrees C) at pH 4 to 6, and was activated when heated at pH 8. The enzyme was purified 66-fold with a 9% yield and appeared homogeneous on discontinuous gel electrophoresis. The...