Authors: Elena Sironi Fabio Sessa Marcello Duranti
Publish Date: 2005/02/22
Volume: 221, Issue: 1-2, Pages: 145-150
Abstract
A simple procedure aimed at fractionating the main proteins of lupin seeds is proposed The protocol consisted of alkali extraction of all proteins and isoelectric precipitation of two classical storage globulins namely conglutins α and β and one albumin conglutin δ The supernatant of this separation contained conglutin γ the other main lupin protein Conglutin γ could easily be purified further by selective Zn2+ precipitation leading to a more than eightfold enrichment with respect to the amount in the flour Resuspension of the isoelectric precipitate in saline water/ethanol solution allowed us to isolate conglutin δ a 2S sulphurrich lupin protein at a very high purity level Conglutins α and β could not be separated further by simple procedures Sodium dodecyl sulphate–polyacrylamide gel electrophoresis analysis confirmed the identities of the isolated protein fractions The distribution of each separated protein type is close to that of the corresponding proteins in the seed The results are discussed in view of the applicability of the method and the potential use of each protein type as a food ingredientThis work was supported by grants from MIUR of Italy Progetto autonomo FIRB 2002 RBAU01JS5C 002 and from the EC Fifth Framework Programme Quality of Life and Management of Living Resources Programme HealthyProfood QLRT 2001002235 The authors thank Salvatore Ciappellano for Zn2+ determinations
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