A lectin from the rhizomes of turmeric (Curcuma longa L.) and its antifungal, antibacterial, and α-glucosidase inhibitory activities

Pariyaphon Petnual, Polkit Sangvanich, Aphichart Karnchanatat

                                                                                          

Abstract

A Curcuma longa L. lectin was purified by aqueous extraction, 80% ammonium sulfate precipitation and ConA Sepharose affinity chromatography. Its specific activity was of 64,566 HU/mg protein for a yield of 41.2% total protein. The molecular weight is of 17.3 kDa. It has hemagglutinating activity against human blood group B, rabbit, mouse, rat, guinea pig, geese, and sheep erythrocytes. The optimum pH is between 6–7, and stable up to 40°C. Activity was stimulated by Ca²⁺ and Mn²⁺. The internal sequence indicated similarity with legume lectin family. Moreover, at concentration of 47 and 94 mg/0.3 cm² disc showed antifungal activity against Exserohilum turicicum, Fusarium oxysporum, and Colectrotrichum cassiicola. The minimal inhibitory concentration were 0.002, 0.005, 0.011, 0.09, and 0.046 mg/mL Pseudomonas aeruginosa, Staphylococcus aureus, Bacillus subtilis, Escheriehia coli, and Candida albicans, respectively. Additionally, it contains a high α-glucosidase inhibitory activity with an IC₅₀ of 8 mg/mL.

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Keywords :lectin ,Curcuma longa ,antifungal activity ,antibacterial activity ,α-glucosidase inhibitory.