Milano, Italy
Milano, Italy

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Grant
Agency: Cordis | Branch: FP7 | Program: BSG-SME | Phase: SME-2011-1 | Award Amount: 1.34M | Year: 2011

The objective is to assess the health benefits on dislipidemia prevention of innovative food products based on lupin proteins, starting from some preliminary results provided by 2 past European collaborative projects (Healthy-Profood & Bioprofibre). The core RTD activity is the implementation of a multicenter randomized dietary intervention study with LDL-cholesterol as main end-point aimed to compare the hypolipidemic effect of lupin proteins vs. animal proteins. Besides LDL-Cholesterol other inflammatory and metabolic markers will be investigated. In addition the metabolism of cholesterol will be analysed. All these data will be exploited at the end of the project by the submission of an application to the European Commission for the approval a health claim on lupin and cholesterol reduction. The project will include also product development and optimization, with particular reference to the nutrition profiles of the foods. Specific activities will be dedicated to assess the quality of the lupin proteins in the food products. Innovation activities will be dedicated also to the application of a New Concept Development for new products, new services and new markets for enterprises. To reach these objectives the LUPICARP consortium includes 5 food producing SMEs, 1 lupin ingredient manufacturer and 5 RTD performers expert in product innovation, food processing, clinical nutrition, pharmacology. Efficient technology transfer will be ensured to improve the competitiveness of participating SMEs.


Lammi C.,University of Milan | Zanoni C.,University of Milan | Scigliuolo G.M.,HPF Nutraceutics SRL | D'Amato A.,Polytechnic of Milan | Arnoldi A.,University of Milan
Journal of Agricultural and Food Chemistry | Year: 2014

Previous experiments in suitable animal models and in mild hypercholesterolemic individuals have shown that the consumption of lupin proteins may be useful for controlling total and low-density lipoprotein (LDL) cholesterol levels. With the objective of providing evidence that peptides deriving from the hydrolysis of lupin proteins may be responsible of the observed activities and for investigating the mechanism of action, HepG2 cells were treated with lupin peptides obtained by either pepsin (P) or trypsin (T) hydrolysis, and molecular and functional investigations were performed on the LDL receptor/SREBP2 pathway. For the first time, this paper provides experimental evidence that lupin peptides are able to interfere with the HMGCoAR activity, up-regulating the LDL receptor (136 and 84% vs the control for P and T peptides, respectively, at 1 mg/mL) and SREBP2 proteins (148 and 73% vs the control for P and T peptides, respectively, at 1 mg/mL) via the activation of PI3K/Akt/GSK3β pathways and increasing the LDL uptake at HepG2 cell line (40 and 50% vs the control for P and T peptides, respectively, at 1 mg/mL). These results may be useful in explaining the activities observed in vivo in animals and humans treated with lupin protein. © 2014 American Chemical Society.


Boschin G.,University of Milan | Scigliuolo G.M.,HPF Nutraceutics S.r.l. | Resta D.,HPF Nutraceutics S.r.l. | Arnoldi A.,University of Milan | Arnoldi A.,HPF Nutraceutics S.r.l.
Journal of Agricultural and Food Chemistry | Year: 2014

Recently, the enzymatic hydrolysis of Lupinus albus and Lupinus angustifolius proteins with pepsin was showed to produce peptides able to inhibit the angiotensin-converting enzyme (ACE). The objective of the present work was to test different hydrolytic enzymes and to investigate three lupin species (L. albus, L. angustifolius, Lupinus luteus) with the final goal of selecting the best enzyme/species combination for an efficient production of ACE-inhibitory peptide mixtures. Pepsin gave peptides with the best IC 50 values (mean value on three species 186 ± 10 μg/mL), followed by pepsin + trypsin (198 ± 16 μg/mL), chymotrypsin (213 ± 83 μg/mL), trypsin (405 ± 54 μg/mL), corolase PP (497 ± 32 μg/mL), umamizyme (865 ± 230 μg/mL), and flavourzyme (922 ± 91 μg/mL). The three species showed similar activity scales, but after pepsin + trypsin and chymotrypsin treatments, L. luteus peptide mixtures resulted to be significantly the most active. This investigation indicates that lupin proteins may be a valuable source of ACE-inhibitory peptides, which may explain the activity observed in experimental and clinical studies and foresee the application of lupin proteins into functional foods or dietary supplements. © 2014 American Chemical Society.


Boschin G.,University of Milan | Scigliuolo G.M.,HPF Nutraceutics S.r.l. | Resta D.,HPF Nutraceutics S.r.l. | Arnoldi A.,University of Milan | Arnoldi A.,HPF Nutraceutics S.r.l.
Food Chemistry | Year: 2014

The objective of this investigation was to compare the angiotensin converting enzyme (ACE)-inhibitory activity of the hydrolysates obtained by pepsin digestion of proteins of some legumes, such as chickpea, common bean, lentil, lupin, pea, and soybean, by using the same experimental procedure. The ACE-inhibitory activity was measured by using the tripeptide hippuryl-histidyl-leucine (HHL), as model peptide, and HPLC-DAD, as analytical method. The peptide mixtures of all legumes were active, with soybean and lupin the most efficient, with IC50 values of 224 and 226 μg/ml, respectively. Considering the promising results obtained with lupin, and aiming to identify the protein(s) that release(s) the peptides responsible for the activity, the peptides obtained from the pepsin digestion of some industrial lupin protein isolates and purified protein fractions were tested. The most active mixture, showing an IC50 value of 138 μg/ml, was obtained hydrolysing a mixture of lupin α + β conglutin. © 2013 Elsevier Ltd. All rights reserved.


Sirtori E.,University of Milan | Isak I.,University of Milan | Resta D.,HPF Nutraceutics Srl | Boschin G.,University of Milan | Arnoldi A.,University of Milan
Food Chemistry | Year: 2012

Pea protein is considered to be an emerging alternative for the formulation of numerous food products, including functional foods, because of its purported hypolipidemic, anti-hypertensive and hypoglycaemic activities. The present investigation was designed to evaluate the effects of thermal and mechanical treatments on an industrial pea protein isolate (Pisane®) from Pisum sativum L. As a preliminary step, the main protein components of P. sativum seed were identified, using the canonical proteomic approach, including 2D-separation and mass spectrometry. Most of the main spots were assigned to the major pea storage proteins: legumin, vicilin and convicilin. Differential scanning calorimetry and proteomic techniques were used to investigate the effects of processing on the protein profile and to assess the availability of stable peptides. After prolonged treatments, no proteins were present in their native forms and the protein solubility was greatly decreased; however, some intense spots were still present on 2D-gels. The spot identity was confirmed by HPLC-Chip-MS/MS, showing that the vicilin 30 kDa fragment and legumin acidic subunits were resistant and some specific peptides remained intact. DSC thermograms showed that strong treatments decreased the denaturation enthalpy. The mechanical treatments, instead, did not modify (in a relevant way) either the protein profile or DSC thermograms. © 2012 Elsevier Ltd. All rights reserved.


Resta D.,HPF Nutraceutics SRL | Brambilla F.,HPF Nutraceutics SRL | Arnoldi A.,University of Milan
Food Chemistry | Year: 2012

In food science there is a growing demand of methods for the absolute quantification of proteins, such as allergens or bioactive proteins, and shotgun proteomics based on mass spectrometry is a promising analytical tool in this area. This paper describes an innovative label-free method for the absolute quantification of γ-conglutin, one of the most relevant lupin seed proteins, which is hypoglycaemic and a major allergen. The main features of the method are: (a) the chromatographic separation was performed on an HPLC-chip system coupled with an ion trap mass spectrometer; (b) five proteotypic peptides of γ-conglutin were selected and analysed with a multiple reaction monitoring (MRM) method; (c) absolute quantification was obtained by the standard addition method after purification of a reference sample of γ-conglutin from lupin seed; (d) the matrix effect was overcome by spiking with an exogenous protein, i.e. BSA, as internal standard. © 2011 Elsevier Ltd. All rights reserved.


Sirtori E.,University of Milan | Resta D.,HPF Nutraceutics Srl | Arnoldi A.,University of Milan | Arnoldi A.,HPF Nutraceutics Srl | And 2 more authors.
Food Chemistry | Year: 2011

Peanut-allergic individuals may also react to lupin, which, for this reason, has been included in the EU list of food allergens. Since there is not yet any general consensus on the major allergen/s in lupin, the objective of this investigation was to compare the reactivity of the main lupin proteins towards the IgE of the sera of allergic patients. Both Lupinus albus and Lupinus angustifolius were investigated. ELISA's, Western blotting and mass spectrometry, including also de novo sequencing of the unknown lupin proteins, were used for identifying the IgE-binding proteins. Significant differences in the protein reactivities were observed. In particular, there was a direct relationship between the level of peanut-specific IgE's and the cross-reactivity to lupin proteins; also the reactivity of each serum appeared to be unique. Although numerous lupin proteins bind IgE's, our data suggest a predominant contribution of α-conglutin in the reactivity of both L. albus and L. angustifolius. © 2010 Elsevier Ltd. All rights reserved.


It is provided a production process (1) for compounds having hypotensive activity adapted to be used for preparing foods, drinks and dietary supplements; said production process (1) being adapted to obtain compounds having hypotensive activity (10) from processing/working of Lupinus seeds (11) and comprising an extraction step (3) in which a protein solution (13) is obtained from the seeds; and a hydrolysis step (4) in which the proteins of the protein solution (13) are fragmented thus obtaining the compounds having hypotensive activity (10), which consist of peptides of a molecular weight lower than 3000 Da and having an aromatic or hydrophobic amino acid as the terminal group so as to determine an IC_(50) lower than 1000 g/mL.

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