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Lectin activity was assessed in sixteen Aspergillius species using human A, B, O, AB, rabbit, goat, pig and sheep erythrocytes. Neuraminidase and protease treated blood group O erythrocytes were also used to evaluate lectin activity from all the cultures unable to agglutinate native red blood cells. Lectin activity was revealed from Aspergillus acristatus, A. gorakhpurensis, A. panamensis and A. carbonarius extracts, while undiluted extract of A. fischeri showed weak haemagglutination. Lectin activity was expressed after 5 days of growth by A. acristatus, A. gorakhpurensis, A. panamensis and A. carbonarius and after 8 days of cultivation a sharp decline in lectin activity was observed. Higher titres were observed from these species with enzymatically modified blood type O erythrocytes. A variety of carbohydrates were used to study their minimum inhibitory concentration capable of inhibiting haemagglutination. Porcine stomach mucin was found to be the most potent inhibitor of all the lectins. A. gorakhpurensis lectin showed high specificity for chondroitin-6-sulphate and N-acetyl-D-galactosamine. Significant specificity for L-fucose, D-arabinose and 2-deoxy-D-ribose was identified with A. panamensis lectin. Low concentrations of 0.625 mM of D-galactosamine HCl and 0.12 mg/mL of chondroitin-6-sulphate were found optimal to prevent haemagglutination of A. carbonarius extract. A. carbonarius lectin was partially purified 2.75-fold using ammonium sulphate precipitation, dialysis and ultrafiltration. It was found to be stable upto 40°C and within the pH range of 7.0–8.0. Lectin activity was not affected by guanidine-HCl, while it was reduced to half after incubation with urea and thiourea after 24 h.

New lectins from aspergilli and their carbohydrate specificity