Hypolipidaemic and anti-atherosclerotic effects of lupin proteins in a rabbit model

The British journal of nutrition (Impact Factor: 3.45). 09/2008; 100(04):707 - 710. DOI: 10.1017/S000711450894215X

ABSTRACT The biological activities of a protein isolate from lupin (Lupinus albus) were studied in a rabbit model of atherosclerosis. Focal plaque development was induced at both common carotid arteries by perivascular injury. After surgery, animals were fed three different diets for 90 d, all with 1 % cholesterol, 15 % SFA and 20 % protein; the protein source was casein (CAS), lupin proteins (LUP) or 50 % CAS+50 % LUP (CAS+LUP). Lower cholesterolaemia was detected in the LUP v. the CAS group at 60 and 90 d of treatment ( − 40·3 and − 33·5 %, respectively; P < 0·05). Cryosection analyses of the carotids indicated a significant reduction in focal lesion progression in the LUP v. the CAS group ( − 37·4 %; P < 0·05). In summary, in a rabbit model of atherosclerosis, a protein isolate from L. albus reduced cholesterolaemia and exerted a remarkable protective activity against atherosclerosis progression.

  • [Show abstract] [Hide abstract]
    ABSTRACT: The formation of a green or beany off-flavor during storage of legume protein extracts limits their application in foods. Pea protein extracts were submitted to lactic acid fermentations to improve the flavor by either reducing off-flavor formation or by masking undesirable green notes. The aroma profiles of untreated pea protein extract (PPE) and fermented pea protein extract (PPEF) were compared to each other and to a commercial whey protein as a benchmark. Kinetic measurements of n-hexanal and n-hexanol formation were used as an indicator for progressing lipid oxidation and storage stability. The nonfermented and fermented pea protein extracts showed a shelf-life comparable to the commercial whey protein reference. Volatiles were identified and quantified using dynamic headspace sampling with subsequent coupled TDS-GC-MS and TDS-GC-olfactometry flavor dilution analysis. A total of 18 odorants with dilution factors equal to or higher than 100 were determined in PPE and 17 in PPEF. Altogether, 23 highly odor-active compounds were identified according to their mass spectra, odor impressions, linear retention indices, and standard substances in PPE and PPEF, among them n-hexanal, 1-pyrroline, dimethyl trisulfide, 1-octen-3-one, 2,5-dimethyl pyrazine, 3-octen-2-one, β-damascenone, and guaiacol. The fermentation considerably amended the aroma profile of pea protein preparations resulting in a reduction or a masking of undesirable flavors.
    Food Biotechnology 01/2012; 26(1):58-74. · 0.49 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: This short paper presents an overview of the most important characteristics of lupin, a legume that is regaining much interest in human nutrition, after having been neglected for many years. Particular emphasis is placed on the nutraceutical properties of lupin protein that are able to impact positively on hypercholesterolemia, hypertension and hyperglycaemia.
    Nutrafoods. 10(4).
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: The molecular characterization of bioactive food components is necessary for understanding the mechanisms of their beneficial or detrimental effects on human health. This study focused on γ-conglutin, a well-known lupin seed N-glycoprotein with health-promoting properties and controversial allergenic potential. Given the importance of N-glycosylation for the functional and structural characteristics of proteins, we studied the purified protein by a mass spectrometry-based glycoproteomic approach able to identify the structure, micro-heterogeneity and attachment site of the bound N-glycan(s), and to provide extensive coverage of the protein sequence. The peptide/N-glycopeptide mixtures generated by enzymatic digestion (with or without N-deglycosylation) were analyzed by high-resolution accurate mass liquid chromatography-multi-stage mass spectrometry. The four main micro-heterogeneous variants of the single N-glycan bound to γ-conglutin were identified as Man2(Xyl) (Fuc) GlcNAc2, Man3(Xyl) (Fuc) GlcNAc2, GlcNAcMan3(Xyl) (Fuc) GlcNAc2 and GlcNAc 2Man3(Xyl) (Fuc) GlcNAc2. These carry both core β1,2-xylose and core α1-3-fucose (well known Cross-Reactive Carbohydrate Determinants), but corresponding fucose-free variants were also identified as minor components. The N-glycan was proven to reside on Asn131, one of the two potential N-glycosylation sites. The extensive coverage of the γ-conglutin amino acid sequence suggested three alternative N-termini of the small subunit, that were later confirmed by direct-infusion Orbitrap mass spectrometry analysis of the intact subunit.
    PLoS ONE 01/2013; 8(9):e73906. · 3.53 Impact Factor

Full-text (2 Sources)

Available from
Jun 1, 2014