Purification and Characterization of a Novel Thermostable Mycelial Lectin from <Emphasis Type="Italic">Aspergillus terricola</Emphasis> |
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Authors: | Ram Sarup Singh Ranjeeta Bhari Hemant Preet Kaur Monika Vig |
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Institution: | (1) Carbohydrate and Protein Biotechnology Laboratory, Department of Biotechnology, Punjabi University, Patiala, 147 002, Punjab, India |
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Abstract: | Lectin has been isolated from mycelia of Aspergillus terricola by single step purification on porcine stomach mucin-Sepharose 4B affinity column. Lectin could be effectively purified with
75% recovery and 4.47-fold increase in specific activity. Lectin migrated as a single band on SDS-PAGE with an apparent molecular
mass of 32.5 kDa. Sugar inhibition assay revealed that the lectin did not strongly interact with most carbohydrates and their
derivatives tested while strong binding affinity to d-glucose, d-sucrose, N-acetyl-d-galactosamine, asialofetuin, porcine stomach mucin, and bovine submaxillary mucin was indicated. Neuraminidase and protease
treatment to erythrocytes enhanced lectin titre. Lectin activity was stable within the pH range of 7.0–10.5. A. terricola lectin displayed remarkable thermostability and remained unaffected upon incubation at 70 °C for 2.5 h. Lectin did not require
metal ions for its activity. Incubation with denaturants (urea, thiourea, and guanidine–HCl) substantially reduced lectin
activity. Carbohydrate analysis revealed that it is a glycoprotein with 9.76% total sugars. |
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