Elsevier

Phytochemistry

Volume 20, Issue 9, 1981, Pages 2071-2075
Phytochemistry

The seed globulins of Lupinus albus

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Abstract

The seed globulins of Lupinus albus were extracted and 12 ditterent proteins were separated: four of them correspond to vicilins and two to legumin

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      The detailed information on structural characteristics and isolation methods of α, β, δ-conglutins have previously been outlined (Duranti, Consonni, Magni, Sessa, & Scarafoni, 2008). Very few reports (Blagrove & Gillespie, 1975; Duranti, Restani, Poniatowska, & Cerletti, 1981) however are available for the purification of γ-conglutin, and these reports focus only on lab scale preparation of γ-conglutin (Duranti, Scarafoni, Di Cataldo, & Sessa, 2001). Therefore, there is a lack of effective larger scale technology for γ-conglutin purification for nutraceutical application, making it unavailable on a commercial scale.

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      Conglutin γ (also termed 7S protein) is an exceptional globulin soluble in both water and salt solutions. In contrast to the other lupin conglutins, the isoelectric point of the 7S protein lies within the alkaline range (7.9, Arnoldi et al., 2007; Duranti, Restani, Poniatowska, & Cerletti, 1981; Duranti et al., 2008). The glycoprotein shows a very high sulfur content, although it represents only 5% of total globulins.

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    1

    On leave of absence from the Institute of Plant Genetics, Polish Academy of Sciences, Pozanan. Poland.

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