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WO2006003110A1 - Procede de purification de fractions de proteines provenant de graines de lupin et agissant sur le metabolisme lipidique - Google Patents

Procede de purification de fractions de proteines provenant de graines de lupin et agissant sur le metabolisme lipidique Download PDF

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Publication number
WO2006003110A1
WO2006003110A1 PCT/EP2005/052940 EP2005052940W WO2006003110A1 WO 2006003110 A1 WO2006003110 A1 WO 2006003110A1 EP 2005052940 W EP2005052940 W EP 2005052940W WO 2006003110 A1 WO2006003110 A1 WO 2006003110A1
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Prior art keywords
lupin
proteins
protein
process according
extraction
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Ceased
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PCT/EP2005/052940
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English (en)
Inventor
Anna Arnoldi
Cesare Sirtori
Andreas Waesche
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Fraunhofer Gesellschaft zur Foerderung der Angewandten Forschung eV
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Fraunhofer Gesellschaft zur Foerderung der Angewandten Forschung eV
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    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
    • A23J1/14—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from leguminous or other vegetable seeds; from press-cake or oil-bearing seeds
    • A23J1/142—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from leguminous or other vegetable seeds; from press-cake or oil-bearing seeds by extracting with organic solvents
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
    • A23J1/14—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from leguminous or other vegetable seeds; from press-cake or oil-bearing seeds
    • A23J1/142—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from leguminous or other vegetable seeds; from press-cake or oil-bearing seeds by extracting with organic solvents
    • A23J1/144—Desolventization
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
    • A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs

Definitions

  • the present invention refers to a process for the purification from lupin seed of protein fractions, active on lipid metabolism.
  • lupin seeds for example of the species Lupinus albus (white lupin) and Lupinus angustifolius (narrow-leafed lupin), are purified in conditions that maintain their biological features and without the use of organic and inorganic reagents or the use of metals that rule out the use for direct human consumption.
  • VLDL + LDL triglyceridemia
  • triglyceridemia (Sirtori et al, 2004. "The proteins of white lupin seed- a naturally isoflavone free legume - reduce cholesterolemia in rats and increase LDL receptor activity in HepG2 cells", J. Nutr., 134: 18-23).
  • Lupin seeds contain two classes of protein, which, according to the Osborne classification, belong to the albumins and globulins in a relative ratio of 1 to 9.
  • the globulins in turn consist of two major components, 7S and 1 IS, called beta and alpha conglutin, respectively, and of two minor components, defined gamma and delta conglutin, respectively (Blagrove et al, 1975, "Isolation, purification and characterization of the seed conglutins of Lupinus albus", Aust. J. Plant Physiol. 2: 13-27).
  • lupin proteins unlike soy proteins, have the significant advantage of being essentially free of isoflavonoid components (''phytoestrogens") (Katagiri et al, 2000. ' ⁇ PLC analysis of white lupin isoflavonoids", Biosci. Biotechnol. Biochem. 64: 1118-1125;
  • the object of this invention is to develop a process that enables protein fractions active on lipid metabolism to be obtained from lupin seeds.
  • the present invention refers to a process for the purification of protein concentrates and isolates from lupin seeds, for example of Lupinus albus and Lupinus angustifolius, comprehensive of the following steps: a) The lupin seeds of one of the two indicated species are coarsely ground and transformed into flakes. During this process the temperature is kept below 60 °C to prevent denaturation of the proteins and non-enzymatic browning of the flakes. At the end of the process, the flakes have a yellowish colour.
  • the lipids are or are not extracted with a suitable solvent (prevalently hexane) by percolation of the solvent through the flakes placed in a tubular reactor using a multistage procedure.
  • a suitable solvent prevalently hexane
  • the solvent is eliminated in stripping conditions with superheated solvent and steam under vacuum and finally by air blowing. After this stage tihe flakes are almost white and have a protein content exceeding 50 %.
  • lipids can also be extracted with supercritical carbondioxide (CO 2 ) by percolation through the flakes placed in a tubular reactor using a multistage procedure.
  • CO 2 supercritical carbondioxide
  • the protein is extracted using acid water solutions (pH 4.3-4.9) to separate a solution enriched with gamma conglutin (extract A) and a partially purified precipitate that contains most of the beta and alpha conglutins (7S and 1 IS globulins) of the lupin seed (precipitate A).
  • extract A From extract A, after clarification, ultrafiltration and diafiltration, a water solution is obtained that is enriched with gamma conglutin, which then is HTST pasteurised or UHT treated and spray-dried to give a powder protein concentrate or isolate prevalently containing gamma conglutin (LUPI-F), as confirmed by the SDS-PAGE analysis and two-dimension electrophoresis.
  • Precipitate A is extracted in two successive steps with a weakly basic solution (7.0-7.5 pH) and is decanted by centrifugation to obtain two extracts enriched with globulins 7S and 1 IS, which are combined (extract B).
  • lupin proteins selected from native isolated lupin proteins, for example from Lupinus albus (white lupin) or Lupinus angustifolius (narrow-leafed lupin), which can provide a protein content of at least 50 % of the total protein content of the dry matter (calculated on the basis of the nitrogen content, N x 6.25), in such a way that the protein content provides at least 25% of the total energy content of the composition;
  • ⁇ or at least 50 % of gamma conglutin from sweet lupin ⁇ or at least 50 % of a mixture of total lupin proteins: alpha, beta, and gamma conglutins;
  • This composition may be used for preparing functional and dietary food products for the clinical control of hyperlipidemia, and for the preparation of dietary supplements and nutraceutical products, again for the clinical control of hyperlipidemia.
  • the process according to the present invention completely eliminates the problems connected with the presence in lupin seeds of bitter quinolizidine alkaloids displaying an antifeedant role in seeds.
  • HepG2 cells a human hepatoma cell line, provided with a wide range of enzymes involved in intermediary metabolism.
  • HepG2 cells are widely used to assess the regulatory properties on the lipoprotein system of proteins/peptides of vegetable origin. Studies have been conducted on the modulation of the LDL receptors, responsible for cholesterol homeostasis hi HepG2 cells.
  • LDL receptors bind and internalise circulating LDL cholesterol, thus regulating the levels of LDL and the distribution of cholesterol to tissues and cells.
  • LDL receptors bind and internalise circulating LDL cholesterol, thus regulating the levels of LDL and the distribution of cholesterol to tissues and cells.
  • a product obtained with the process described in this invention was subjected to experiments on a universally accepted animal model, i.e. rats on a lipid-rich diet, conducted hi parallel to the administration of a lipid- lowering drug with well known activity hi rats. These experiments have "*' clearly shown the potential of certain lupin-protein isolates to exert a significant lipid-lowering activity.
  • the total lupin protein extract and the different purified fractions were administered as described by Sirtori et al. (2004), i.e. by feeding the different products suspended hi 0.5 % carboxymethylcellulose.
  • a number of experimental groups were thus investigated: 1. standard diet with daily gavage of 0.5% carboxymethylcellulose; 2. hyperlipidemic Nath diet (Nath et al, 1959.
  • LUPI-F protein isolate mainly consisting of gamma conglutin from Lupinus angustifolius, administered at daily doses of 10, 20 and 50 mg/kg.
  • the major results from the biological experiments can be summarized in the following way: a) the highest lipid lowering activity (significantly greater than that of Clofibrate) was achieved with the protein isolates LUPI-F at the highest doses, the Lupinus albus fraction being slightly more effective than that from L. angustifolius. b) the protein isolates LUPI-E were also very effective at slightly higher doses, again a greater activity being exerted by the Lupinus albus proteins.
  • the lipid lowering activity was mainly hypocholesterolemic, also considering the modest rise of triglyceridemia in the model. It can be thus reasonably concluded that the lipid lowering activity is almost exclusively exerted on the atherogenic fractions VLDL+LDL, as typically induced by the experimental diet in the rat.
  • Proteins enriched with alpha and beta conglutin (LUPI-E) and proteins enriched with gamma conglutin (LUPI-F) can be prepared from different species and varieties of sweet and bitter lupins by different embodiments of the process according to the invention.
  • the crushed seeds were transferred to a rotating mill (equipped with wheels for flaking) for flaking (phase 2). During flaking, the temperature of the flaking wheels was kept below 40 0 C to avoid browning and/or protein denaturing. The resulting flakes were yellowish ("yellow flakes") and had an average density of 300-330 kg/m 3 . Table 2. Composition of the yellow flakes of Lupinus albus
  • Table 3a shows the chemical composition of the lupin flakes ("white flakes") that have been defatted by hexane. About 867 kg of white flakes were obtained from 1,027 kg of yellow flakes. Table 3a. Chemical composition of the white flakes of L. albus after extraction with hexane
  • the lipids were extracted from 250-kg batches of yellow flakes, which formed a 2-metre high column in a vertical tube measuring 900 mm in diameter. Defatting was carried out by percolating supercritical CO 2 (SCF- CO2) through the fixed bed of yellow flakes in 4 stages. The temperature was maintained between 40 and 69°C, preferably 45-5O 0 C. Pressure was controlled between 240 and 300 bar, preferably between 250 and 260 bar. After each stage, the SCF-CO2 was evaporated from the extracted oil and from the defatteS flakes by evaporation at atmospheric pressure. Table 3b shows the chemical composition of the lupin flakes ("white flakes") defatted using SCFCO2.
  • the lupin protein extract was prepared from the white flakes in two extraction phases 4 and 5, the first of which (4) was carried out in an acid water solution and the second (5) was conducted in an alkaline water solution in two stages (5-1 and 5-2).
  • phase 4 the white flakes were suspended in acid cold water in order to separate a soluble fraction A enriched with gamma conglutin from an insoluble solid precipitate B containing the proteins with an acid isoelectric point (beta and alpha conglutin).
  • phase 4 extraction of phase 4 was carried out on a 185-kg batch of white flakes using 1,800 litres tap water acidified at pH 4.5-4.8, in a 2000-litre tank stirred at a controlled temperature between 13.5 and 15.2 0 C.
  • a two-arm stirrer was adjusted to 55 rpm.
  • About 23.6 litres of 3 M HCl were used to control the pH during extraction, which lasted for a total of 1 hour.
  • a centrifugal decanter (CB300. GEA Westfalia GmbH, Oelde/Germany) was used for the separation of the solid residue (approximate speed 4,400 rpm). Starting with 185 kg of white flakes and using 1,800 kg of tap water, approximately 385 kg of residue or solid precipitate B and 1,600 litres of acid extract A were obtained.
  • phase 5 the solid precipitate B was suspended in slightly alkaline hot water in order to separate a protein extract C enriched with beta and alpha conglutin and a solid precipitate D, which is insoluble in these conditions.
  • the solid residue of the first extraction phase was again extracted in a tank equipped in the same way, using 540 litres of tap water with 7.3-7.4 pH and at 29.0-32.0°C. About 0.3 litres of the solution 3 M of sodium hydroxide were used to control pH during the extraction lasting 15 min.
  • phase 6 the protein extract C obtained in phase 5 was added with hydrochloric acid to precipitate a protein fraction E that was rich in alpha and beta conglutin.
  • the precipitated protein solution F (about 1,550 litres) was separated using a self-cleaning disc separator with a speed of 6,830 rpm (10,000*g) and a supply speed of 1,800 litres/hour.
  • the solids suspended in the supply fluid varied from 11.0 to 11.5 vol %.
  • the separated protein precipitate F was unloaded at intervals of about 250 seconds.
  • the solids suspended in the clarified extract varied from 0.0 to 0.1 vol %.
  • About 1330 litres of clarified supernatant SP and 213 litres of protein precipitate F were separated.
  • the SP dry matter content varied from 0.4 to 0.5 % and contained about 70 % of total proteins (N*6.25).
  • the acid extract A (1,600 litres) was clarified using a self-cleaning disk separator at a speed of 7,500 rpm (approximately 12,000*g) at a supply speed of 1,800 litres per hour.
  • the solids content of the supply liquid varied between 2 and 2.5 vol %.
  • the separated protein precipitate G was discharged at intervals of about 280 seconds.
  • the solid content of the clarified extract H varied from 0.1 to 0.15 vol %.
  • About 1,500 litres of clarified protein extract H and 100 litres of protein precipitate G were separated.
  • the dry matter content of the extract H varied from 2.2 to 2.5 % and about 25% of total proteins (N*6.25).
  • phase 9 the extract H was ultrafiltered (cross-flow membrane filtering). More precisely, 700 litres of extract H were taken from pH 4.5 to a pH value in the range of 6.0 and 7.0 and were placed in the ultrafiltration unit. At this pH the obstruction of the membrane surface by the protein was at a more reduced level than with acid pH.
  • the solution was subsequently recirculated on the membrane unit (Pall, Germany, 2*4.5 m 2 ' cut-off 10,000 Dalton) at a pressure of 3 bar and at a temperature of 40°C, until the volume of clarified acid extract H was reduced to a tenth of the initial volume.
  • the dry matter content of the retentate I was 7 % and had a protein content of approximately 50% (N*6.25).
  • the retentate I was subsequently diluted by adding SP and subjecting the resulting mixture to diafiltration in a second membrane filtration unit.
  • Each dilution stage was comprehensive of adding 233 litres of (SC) to the retentate I deriving from the ultrafiltration of phase 9 and of recirculating the diluted retentate on the membrane until the retentate volume was returned to the initial value. After the last dilution phase, on the other hand, recirculating was continued until the dry matter content had reached maximum levels.
  • the dry matter content of the diafiltrated retentate L varied from 14.5 to 15 % and the dry matter contained approximately 84% of total proteins (N*6.25).
  • phase 12 the fraction with readjusted pH (fraction M) was heated from 40 0 C to 65°C in a small scale heat exchanger with continuous circulation, consisting of a single lined pipe with an internal diameter of 6 mm. The length of this pipe was adjusted in such a way that the residual circulation time was about 1 minute. Alternatively, this material can be subjected to UHT treatment for just a few seconds.
  • Fraction M after heating, was then directly introduced into a spray dryer (Niro-Minor, GEA NIRO Ltd, Copenhagen) together with hot air.
  • the inlet air temperature was 195 0 C
  • the liquid supply speed was 8-10 litres per hour
  • the resulting air outlet temperature was 77 0 C.
  • the dry powder was separated from the air flow using a 150-mtn cyclonic separator.
  • the dry matter content of the resulting powder varied from 94.0 to 95.2 %. Ignoring the losses of fine particles, starting with 40 kg of fraction L approximately 4.5 kg of dry protein fraction enriched with gamma conglutin (LUPI-F) were obtained.
  • LUPI-F prepared according to the described process, contains 84.7% proteins (N*6.25), 0.6 % lipids and 6.4 % ash (of dry matter). In addition, the dry matter contains 8.3 % of nitrogen-free products.
  • phase 13 consisting of an extract in a slightly basic conditions, enabled a fraction N to be obtained, which was enriched in beta and alpha conglutin, by processing phase 7 solids F and phase 8 solids G.
  • the analyses were conducted on a 3-micron, 150 x 2.1 mm Alltima Cl 8 microbore column. Conditions: 0.1 % eluent A, acetic acid in acetonitrile, 0.1 % eluent B 5 acetic acid in water, 15 % A to 35 % A gradient in 50 min, then 35 % A for 10 min; flow 0.2 mL/min; temperature 30 °C.
  • the isofiavones were identified by LC-ESI- MS/MS on an Agilent SL 100 Series LC/MSD trap equipped with an
  • the alkaloids were extracted and analysed in the manner described by Ruiz and Soleto ("Chemical composition, nutritive value, and toxicology evaluation of Mexican wild lupin", J. Agric. Food Chem. J 2001, 49:5336-9). Each sample (500 mg) was homogenised in a vortex with 5 mL of 5% trichloroacetic acid for 1 minute and was then centrifuged. Extraction was repeated twice. After basification with 1 ml of NaOH 10 M, the samples were extracted with dichloromethane (3 x 5 ml), the solvent was evaporated and the.analyses were conducted by GC-MS by comparison with authentic standards, using a PB-I capillary column (30 m x 0.25 mm id). Equipment used: GC-MS QP-5000 (Shimadzu), with injector temperature 240 °C and detector temperature 290 °C, in EI mode.
  • Sprague-Dawley rats (Charles River Italy, Calco, Italy) were used, with mean body weights 200-225 g. They were kept in the laboratory under controlled lighting for 12 hours a day at a constant temperature (18°C) and relative humidity of 55-65%. For a week the animals were fed a standard commercial pellet diet (Piccioni, Gessate, Italia) and were then divided into sixteen experimental groups, all of 12 animals.
  • Group 1 continued with the commercial pellet diet whereas all the other groups received the Nath diet (1% cholesterol, 0.5% cholic acid, 25% hydrogenated coconut oil) (Piccioni, Gessate, Italia). All the animals had free access to water and fed ad libitum.
  • the proteins can be extracted only in an acid environment at pH 4.0-5.0 and at a temperature of 277-340 Kelvin, without beforehand extracting the lipids from the lupin products, i.e. without phase 3 of Figure 1, but at the same time avoiding the formation of emulsions.
  • the crude extract that is thus obtained is then filtered on a membrane to recover the proteins.
  • the operations of washing, pH adjustment, pasteurisation and spray drying then follow as described. Additional recovery of the acid soluble proteins is also possible.

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Abstract

Selon l'invention, des graines provenant du lupin, notamment Lupinus albus et Lupinus angustifolius, sont broyées et transformées en flocons. Les éléments des isolats ou concentrats protéiques désirés et la teneur en lipide de la matière originale sont pris en compte pour extraire ou ne pas extrairre les lipides (huiles) au moyen d'un solvant (essentiellement l'hexane), par percolation du solvant au travers des flocons placés dans un réacteur tubulaire. Le solvant est ensuite éliminé dans des conditions de température contrôlées. En variante, les lipides peuvent être éliminés, également par extraction réalisée avec un CO2 supercritique, par percolation à travers une colonne. Après broyage, la protéine est extraite dans une solution aqueuse, par traitements alternés, dans un environnement faiblement basique et acide, afin d'obtenir la dissolution et la précipitation subséquente des protéines des différentes fractions. Après une centrifugation appropriée des matières insolubles, les protéines sont recueillies sous forme de solution aqueuse, laquelle est ensuite essentiellement reconcentrée par ultrafiltration. Pour assurer une stérilité microbiologique des ingrédients protéiques, une pasteurisation haute (HTST) ou une stérilisation à ultra haute température (UHT) est effectuée. Enfin, les solutions protéiques sont transformées en poudre par séchage par atomisation (Fig. 1). Des propriétés notables d'abaissement des lipide plasmatiques sont détectées dans les isolats de la protéine totale (TPE) du lupin lorsqu'ils sont administrés à des rats alimentés selon un régime hyperlipidémique. Des fractions séparées, particulièrement LUPI-F, ou LUPIE dans une moindre mesure, indiquent une activité d'abaissement des lipides sensiblement supérieure, à la différence du TPE.
PCT/EP2005/052940 2004-06-29 2005-06-23 Procede de purification de fractions de proteines provenant de graines de lupin et agissant sur le metabolisme lipidique Ceased WO2006003110A1 (fr)

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Cited By (13)

* Cited by examiner, † Cited by third party
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WO2009144278A3 (fr) * 2008-05-30 2010-05-06 Fondazione Centro San Raffaele Del Monte Tabor Utilisations de conglutine-γ
WO2010097237A1 (fr) * 2009-02-27 2010-09-02 Fraunhofer-Gesellschaft zur Förderung der angewandten Forschung e.V. Préparations protéiques à base de graines de lupin et leur production
CN101361533B (zh) * 2008-09-27 2011-01-12 北京中农康元粮油技术发展有限公司 一种浸出溶剂在制取食用油脂中的应用
ITMI20101267A1 (it) * 2010-07-09 2012-01-10 Sirtori Prof Cesare R Procedimento per l'estrazione di proteine da semi di pisum sativum e simili
WO2012049215A1 (fr) * 2010-10-12 2012-04-19 Consumo Em Verde - Biotecnologia Das Plantas, S.A. Protéine antimicrobienne
WO2016000939A1 (fr) * 2014-06-30 2016-01-07 Fraunhofer-Gesellschaft Zur Foerderung Der Angewanden Forschung E.V. Émulsion renfermant une protéine de lupin
US20160309744A1 (en) * 2015-04-23 2016-10-27 Nutriati, Inc. Dry fractionation for plant based protein extraction
EP3123871A1 (fr) * 2015-07-30 2017-02-01 Lupino AG Deutschland Extraction mécanique de protéine de lupin
WO2018060528A3 (fr) * 2016-09-30 2018-07-05 Instituto Superior De Agronomia Protéine thérapeutique
CN110256547A (zh) * 2019-07-04 2019-09-20 天津科技大学 一种从澳大利亚甜羽扇豆粉中提取β-conglutin的方法
WO2020192865A1 (fr) 2019-03-22 2020-10-01 Symrise Ag Peptides de plante et leurs utilisations
EP3897183A4 (fr) * 2018-12-21 2022-08-17 Botaneco Inc. Concentrés de protéines végétales
WO2023079159A1 (fr) 2021-11-08 2023-05-11 Gea Westfalia Separator Group Gmbh Procédé d'obtention de protéines à partir de chanvre

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Cited By (25)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2009144278A3 (fr) * 2008-05-30 2010-05-06 Fondazione Centro San Raffaele Del Monte Tabor Utilisations de conglutine-γ
US8609161B2 (en) 2008-05-30 2013-12-17 Ospedale San Raffaele S.R.L. Conglutin-gamma as medicament and diet supplement
CN101361533B (zh) * 2008-09-27 2011-01-12 北京中农康元粮油技术发展有限公司 一种浸出溶剂在制取食用油脂中的应用
WO2010097237A1 (fr) * 2009-02-27 2010-09-02 Fraunhofer-Gesellschaft zur Förderung der angewandten Forschung e.V. Préparations protéiques à base de graines de lupin et leur production
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