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Research Article
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2
); 1-16

Biochemical Characterization of α-Amylase Inhibitor Extracted from Saussurea Costus

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This is an open-access article distributed under the terms of the Creative Commons Attribution-Non Commercial-Share Alike 4.0 License, which allows others to remix, transform, and build upon the work non-commercially, as long as the author is credited and the new creations are licensed under the identical terms.
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This article was originally published by Qassim University and was migrated to Scientific Scholar after the change of Publisher.

Abstract

A wide variety of diseases can be treated effectively and safely with many plant-based remedies. In the current study, Saussurea Costus was considered due to its medicinal benefits. The main objective of the current study was enzymatic characterization of a potent proteinaceous amylase inhibitor from Saussurea Costus. The α-amylase inhibitor was aqueous extracted (with an inhibitory activity of 80%). The optimum activity was observed at pH 7 in 0.1 M phosphate buffer at 80°C. Thermal stability was notably significant, with inhibitory activity maintained at up to 80% after 6 h of incubation at 100°C. The fact that the Saussurea Costus amylase inhibitor seems to have the greatest affinity for human salivary and pancreatic -amylase is indicative of the action of the current purified inhibitor against amylase derived from various sources. Keywords: Biochemical Characterization, α-Amylase Inhibitor, Saussurea Costus, Hypoglycemic.


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