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Screening of Penicillium species for occurrence of lectins and their characterization
Author(s) -
Singh Ram Sarup,
Sharma Sonia,
Kaur Gagandeep,
Bhari Ranjeeta
Publication year - 2009
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.200800282
Subject(s) - lectin , biochemistry , c type lectin , concanavalin a , cd69 , wheat germ agglutinin , biology , agglutination (biology) , chemistry , in vitro , antibody , immunology , cytotoxic t cell , il 2 receptor
Out of 15 Penicillium species screened for lectin activities, P. griseofulvum and P. thomii were found to possess mycelial lectin activity. None of the species displayed extracellular or cell surface‐bound lectin activity. Both species agglutinated rabbit erythrocytes. P. griseofulvum lectin showed specificity to human type O erythrocytes. While P. thomii lectin specifically agglutinated human type A erythrocytes. Highest lectin activities from P. thomii and P. griseofulvum were expressed after 8 and 7 days of growth, respectively. Lectins from both the species displayed a high binding affinity to chondroitin‐6‐sulphate, mucin, asialofetuin, D‐sucrose, and D‐trehalose. Ammonium sulphate at 50% saturation yielded 80% of the total lectin activity. Dialysis and ultrafiltration of the precipitates resulted in 1.79 and 3.46 fold purification of P. griseofulvum and P. thomii lectins, respectively. Both lectins showed pH optima between 7.0–8.0 and were stable near the neutral pH after 2 h. P. thomii lectin exhibited optimal activity at 35–40 °C, and P. griseofulvum lectin at 30–40 °C. P. thomii lectin showed a complete loss of activity above 40 °C, P. griseofulvum lectin was stable at or below 35 °C. (© 2009 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)