Porcine pancreatic α-amylase inhibition by the kidney bean (Phaseolus vulgaris) inhibitor (α-AI1) and structural changes in the α-amylase inhibitor complex

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Heterologous expression of an α-amylase inhibitor from common bean (Phaseolus vulgaris) in Kluyveromyces lactis and Saccharomyces cerevisiae

BACKGROUND Phaseolamin or α-amylase inhibitor 1 (αAI) is a glycoprotein from common beans (Phaseolus vulgaris L.) that inhibits some insect and mammalian α-amylases. Several clinical studies support the beneficial use of bean αAI for control of diabetes and obesity. Commercial extracts of P. vulgaris are available but their efficacy is still under question, mainly because some of these extracts...

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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...

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Bioactivity-Guided Separation of an α-Amylase Inhibitor Flavonoid from Salvia virgata

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...

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Mutants of common bean alpha-amylase inhibitor-2 as an approach to investigate binding specificity to alpha-amylases

Despite the presence of a family of defense proteins, Phaseolus vulgaris can be attacked by bruchid insects resulting in serious damage to stored grains. The two distinct active forms of α-amylase inhibitors, α-AI1 and α-AI2, in P. vulgaris show different specificity toward α-amylases. Zabrotes subfasciatus α-amylase is inhibited by α-AI2 but not by α-AI1. In contrast, porcine α-amylase is inhi...

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ژورنال

عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

سال: 2004

ISSN: 1570-9639

DOI: 10.1016/j.bbapap.2003.11.001