Isolation, Identification and Characterization of a New Type of Lectin with α-Amylase Inhibitory Activity in Chickpea (Cicer arietinum L.)

Plant lectins are a group of highly diverse proteins that possess at least one non-catalytic domain that binds reversibly to a specific mono- or oligosaccharide. So far, only a few members in the lectin-arcelin-aAI1 supergene family in legume lectins have been reported to have inhibitory activity of α-amylases. A proteinaceous a-amylase inhibitor was isolated and purified using Ammonium sulfate precipitation (ASP), Ion exchange chromatography (IEC) and Reversed phase liquid chromatography (RPLC) from the mature seeds of chickpea. Identification by Ultra-performance liquid chromatography-tandem mass spectrometry (UPLC/MS-MS) indicated that the purified proteinaceous α-amylase inhibitor was identified as a chickpea lectin CAL in GenBank (accession No. AGL46982.1). CAL had 227 aa containing a hemopexin-like repeats domain and was a cytoplasm protein in chickpea. It had very low ( 0.05). Our results indicated that CAL is a new type of lectin with inhibitory activity against α-amylases in legume lectins, which can be used as a candidate in genetics engineering for breeding for pest resistance