Effect of neohesperidin dihydrochalcone on the activity and stability of alpha‐amylase: a comparative study on bacterial, fungal, and mammalian enzymes. Issue 10 (25th March 2015)

• Record Type: Journal Article
• Authors: Kashani‐Amin, Elaheh; Ebrahim‐Habibi, Azadeh; Larijani, Bagher; Moosavi‐Movahedi, Ali Akbar
• Is Part Of: Journal of molecular recognition. Volume 28:Issue 10(2015:Oct.)
• Page Start: 605
• Page End: 613
• Publication Date: 2015-03-25
• Subjects: Molecular recognition -- Periodicals; Models, Molecular -- Periodicals; Molecular Conformation -- Periodicals; Molecular Sequence Data -- Periodicals; Molecular Structure -- Periodicals; Carrier Proteins -- Periodicals; 572.8
• DOI: 10.1002/jmr.2473
• Languages: English
• ISSNs: 0952-3499

Abstract

<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Neohesperidin dihydrochalcone (NHDC) was recently introduced as an activator of mammalian alpha‐amylase. In the current study, the effect of NHDC has been investigated on bacterial and fungal alpha‐amylases. Enzyme assays and kinetic analysis demonstrated the capability of NHDC to significantly activate both tested alpha‐amylases. The ligand activation pattern was found to be more similar between the fungal and mammalian enzyme in comparison with the bacterial one. Further, thermostability experiments indicated a stability increase in the presence of NHDC for the bacterial enzyme. In silico (docking) test locates a putative binding site for NHDC on alpha‐amylase surface in domain B. This domain shows differences in various alpha‐amylase types, and the different behavior of the ligand toward the studied enzymes may be attributed to this fact. Copyright © 2015 John Wiley &amp; Sons, Ltd.</p> </abstract>