Purification and characterization of a synergistic bioactive lectin from Pleurotus flabellatus (PFL-L) with potent antibacterial and in-vitro radical scavenging activity

Abstract

Lectin is a carbohydrate-binding protein, which exhibits a plethora of biological properties such as antimicrobial, antifungal, and anticancer activities. In the present study, lectin, with an antibacterial and antioxidant potential, was purified from the oyster mushroom Pleurotus flabellatus. The P. flabellatus Lectin (PFL-L) was purified by using a DEAE – cellulose anion exchange chromatography followed by gel-filtration chromatography. The PFL-L was characterized by CD, HPLC, and MALDI-TOF/MS. The purity of PFL-L increased to 62.40% with the recovery of hemagglutinating activity (HA) by 12.12%. On SDS – PAGE, the PFL-L gave a single band of 18 kDa. PFL-L, consisting of d-galactose, exhibits a strong hemagglutinating activity. It was stable at pH (6.0–7.5) and temperature (10–20 °C) in addition to having extensive hemagglutinating activity. PFL-L enhanced the HA with the use of different metal ions namely Mg2+, Ca2+, and Fe2+. The study of bacterial growth inhibition led to the inference that the PFL-L was more potent against gram-negative bacteria. PFL-L showed the highest radical scavenging activity for the DPPH assay at 100 μg/mL (89.9 ± 2.53%). The highest antioxidant activities with IC50 values (for DPPH assay) of 53.96 μg/mL were determined for PFL-L and the present study shows that lectin from P. flabellatus manifested distinctive character and potentially exploitable activities.