Isolation and comparative characterization of α-amylase inhibitor from white kidney bean (Phaseolus Vulgaris): A serious in vitro assessment of the commercial product
Authors
Abstract
Plant α-amylase inhibitors (αAIs) show great potential as tools to manipulate resistance of crop plants against pests. They can be also considered as drug-design target for treatment of diabetes and digestion disorder. In this study, an amylase inhibitor-rich fraction was purified by ethanol precipitation and affinity chromatography on chitosan beads column from white common bean (Phaseolus vulgaris) extract, and then its in vitro interaction with porcine pancreatic α-amylase (PPA) was studied. A commercially available amylase inhibitor, Phase 2, was also used to serve as a comparative reference. The results showed that inhibitory activity of the αAI extracted from white kidney bean was much higher than that of Phase 2. The purified inhibitor displayed significant heat stability, so that remaining inhibitory activity was ~80%, even at 60 °C for 30 min incubation. Fraction 3 retained ~84% of its initial activity after long term (45 days) dry storage at room temperature. Due to potency and appropriate heat/storage stability, this αAI preparation may be reconsidered as raw material for preparation of commercial αAI to control appetite and energy intake.
Highlights
Copyright
© 2015, Author(s). This open-access article is available under the Creative Commons Attribution 4.0 (CC BY 4.0) International License (https://creativecommons.org/licenses/by/4.0/), which allows for unrestricted use, distribution, and reproduction in any medium, provided that the original work is properly cited.
Similar Articles
Enzyme Assay Guided Isolation of an α-Amylase Inhibitor Flavonoid from Vaccinium arctostaphylos Leaves
Nickavar B, Amin G. Enzyme Assay Guided Isolation of an α-Amylase Inhibitor Flavonoid from Vaccinium arctostaphylos Leaves. Iran J Pharm Res. 2011;10(4):e126025. doi: https://doi.org/10.22037/ijpr.2011.1050
Bioactivity-Guided Separation of an α-Amylase Inhibitor Flavonoid from Salvia virgata
Nickavar B, Abolhasani L. Bioactivity-Guided Separation of an α-Amylase Inhibitor Flavonoid from Salvia virgata. Iran J Pharm Res. 2013;12(1):e125638. doi: https://doi.org/10.22037/ijpr.2013.1244
In-vitro Studies on Calotropis procera Leaf Extracts as Inhibitors of Key Enzymes Linked to Diabetes Mellitus
Kazeem MI, Mayaki AM, Ogungbe BF, Ojekale AB. In-vitro Studies on Calotropis procera Leaf Extracts as Inhibitors of Key Enzymes Linked to Diabetes Mellitus. Iran J Pharm Res. 2016;15(Suppl):e125080. doi: https://doi.org/10.22037/ijpr.2016.1804
Inhibitory Effects of Six Allium Species on α-Amylase Enzyme Activity
Nickavar B, Yousefian N. Inhibitory Effects of Six Allium Species on α-Amylase Enzyme Activity. Iran J Pharm Res. 2022;8(1):e128615. doi: https://doi.org/10.22037/ijpr.2010.788
Chemical Composition and Enzymes Inhibitory, Brine Shrimp Larvae Toxicity, Antimicrobial and Antioxidant Activities of Caloplaca biatorina
Valadbeigi T. Chemical Composition and Enzymes Inhibitory, Brine Shrimp Larvae Toxicity, Antimicrobial and Antioxidant Activities of Caloplaca biatorina. Zahedan J Res Med Sci. 2016;18(11):e4267. doi: https://doi.org/10.17795/zjrms-4267
- Scopus by DOI: 0
Last Update: 6 days ago
- Scopus by Title: 4
Last Update: 6 days ago
- Scopus by Title (Ref): 5
Last Update: 6 days ago
- CrossRef: 0
Last Update: 9 hours ago
- OpenAlex: 0
Last Update: 11 hours ago
- OpenCitations: 0
Last Update: 5 days ago