Format:
Online-Ressource
ISSN:
1521-4028
Content:
Abstract: 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)
In:
volume:49
In:
number:5
In:
year:2009
In:
pages:471-476
In:
extent:6
In:
Journal of basic microbiology, Weinheim : Wiley-VCH, 1960-, 49, Heft 5 (2009), 471-476 (gesamt 6), 1521-4028
Language:
English
DOI:
10.1002/jobm.200800282
URN:
urn:nbn:de:101:1-2023041405334813613863
URL:
https://doi.org/10.1002/jobm.200800282
URL:
https://nbn-resolving.org/urn:nbn:de:101:1-2023041405334813613863
URL:
https://d-nb.info/1286214157/34
URL:
https://doi.org/10.1002/jobm.200800282
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