Abstract
Analysis of nectar from leek (Allium porrum) flowers by SDS-PAGE revealed the presence of two major polypeptide bands of 50 kDa and 13 kDa, respectively. Using a combination of agglutination tests, enzyme assays and N-terminal sequencing, the polypeptides have been identified as subunits of alliin lyase (alliinase, EC 4.4.1.4) and mannose-binding lectin, respectively. The latter protein is particularly abundant since it represents about 75% of the total nectar protein. Honey produced by bees foraging on flowering leek plants still contains biologically active lectin and alliinase. However, the levels of both proteins are strongly reduced as compared to those in the original nectar. It is evident, therefore, that the lectin as well as the alliinase are inactivated/degraded during the conversion of nectar into honey.
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This work was supported in part by grants from the KULeuven and the National Fund for Scientific Research (Belgium). E.V.D is a Senior Research Assistant and W.P. a Research Director of the National Fund for Scientific Research (Belgium).
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Peumans, W.J., Smeets, K., Van Nerum, K. et al. Lectin and alliinase are the predominant proteins in nectar from leek (Allium porrum L.) flowers. Planta 201, 298–302 (1997). https://doi.org/10.1007/s004250050070
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DOI: https://doi.org/10.1007/s004250050070