Premium
A Lectin from S patholobus parviflorus Inhibits A spergillus flavus α ‐Amylase: Enzyme Kinetics and Thermodynamic Studies
Author(s) -
Tintu Ignatius,
Abhilash Joseph,
Dileep Kalarickal V.,
Augustine Anu,
Haridas Madathilkovilakath,
Sadasivan Chittalakkottu
Publication year - 2014
Publication title -
chemical biology and drug design
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.59
H-Index - 77
eISSN - 1747-0285
pISSN - 1747-0277
DOI - 10.1111/cbdd.12291
Subject(s) - aspergillus flavus , enzyme , biochemistry , chemistry , aflatoxin , enzyme kinetics , lectin , amylase , isothermal titration calorimetry , kinetics , microbiology and biotechnology , biology , food science , active site , physics , quantum mechanics
Aspergillus flavus is a commonly found fungal pathogen which produces structurally related and highly toxic secondary metabolites, aflatoxins. It has been proposed that α ‐amylase inhibitors may limit the ability of the fungus to produce aflatoxins. Hence, this enzyme is a potent target for the development of antifungal agents. In this study, it was found that Spatholobus parviflorus seed lectin ( SPL ) can inhibit the growth of A. flavus with a MIC value of 1.5 mg/mL. The enzyme kinetics, molecular modeling and isothermal titration calorimetric studies suggest that SPL can inhibit α ‐amylase with K i value of 0.0042 m m . Hence, it is suggested that the antifungal activity of SPL might be partly due to its ability to inhibit the enzyme α ‐amylase.