The seed globulins of Lupinus albus

Duranti, Marcello; Restani, Patrizia; Poniatowska, M.; Cerletti, Paolo

doi:10.1016/0031-9422(81)80087-8

Cited by 116 publications

(114 citation statements)

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“…Dentre as espécies pesquisadas podemos destacar o tremoço (Lupinus), por constituir-se em uma das mais ricas fontes de proteínas entre as sementes de leguminosas, em que teores variáveis entre 28 e 51% de proteína tem sido reportado para diferentes variedades [7,11,13,24,33,45]. Estudos de caracterização das proteínas das sementes de tremoço demonstram diferenças consideráveis em função da variedade, método de extração e do procedimento físi-co-químico utilizado [6,7,18,34]. A presença de substân-1 Digestibilidade das proteínas de tremoço, Neves, Silva Jr. & Silva cias antinutricionais e tóxicas tem sido substancialmente reduzida por meio de cruzamentos intervariedades, em especial as variedades "doces".…”

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Isolamento da globulina majoritária, digestibilidade in vivo e in vitro das proteínas do tremoço-doce (Lupinus albus L.), var. Multolupa

Neves

Silva

2006

Ciênc. Tecnol. Aliment.

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RESUMOOs objetivos do trabalho foram isolar, purificar e estudar algumas propriedades da fração globulina majoritária de tremoço-doce, var. Multolupa; assim como avaliar as características de digestibilidade da farinha e frações isoladas. As frações protéicas foram separadas por fracionamento diferencial com uso de diferentes solventes. A globulina majoritária de tremoço-doce foi isolada, purificada por cromatografia em Q-Sepharose, revelando um único pico de proteína. Apresentou um peso molecular de 162,5 ± 10,0 kDa, determinado por cromatografia em Sephacryl S-300, e subunidades entre 20-70 kDa em PAGE-SDS. A solubilidade em função do pH e concentrações de NaCl revelaram curva típica dessa fração. A digestibilidade da proteína da farinha e das frações albumina, globulina e glutelina foi avaliada por experimentos in vitro e in vivo e se revelou alta para a fração globulina, seguida pela glutelina, albumina e farinha. A digestibilidade in vivo da fração globulina, tanto aparente quanto verdadeira, não diferiu significativamente daquela determinada para a caseína. Apesar da alta digestibilidade da fração majoritária e frações protéicas, a utilização como única fonte de proteína nas dietas revelou valores baixos de RPLR (razão protéica líquida relativa), indicando ser insuficiente para sustentar o crescimento dos animais, comparativamente à caseína. Palavras-chave: Lupinus albus, frações protéicas, globulina principal, digestibilidade in vitro e in vivo, ensaio biológico. SUMMARY ISOLATION OF MAJOR GLOBULIN, IN VIVO AND IN VITRO DIGESTIBILITY OF PROTEINS FROM SWEET LUPIN (Lupinus albus L.)VAR. MULTOLUPA. The aim of the present work was to isolate, purify and study some properties of the major globulin fraction from sweet lupin, var. Multolupa; as well as to evaluate the digestibility features of flour and isolated fractions. The protein fractions were separated by differential fractionation with different solvents. The lupin major globulin was isolated, purified by Q-Sepharose chromatography when it showed only one protein peak. The major protein presented a molecular weight of 162.5 ± 10.0 kDa, determined on Sephacryl S-300 chromatography; and subunits between 20 to 70 kDa on SDS-PAGE. The protein solubility in relation to pH and NaCl concentrations showed a typical S-like curve for globulins. The flour and the isolated protein fractions, albumins, globulins and glutelins were evaluated by in vitro and in vivo experiments. The in vitro and in vivo digestibility assays revealed a high digestibility for the globulin, followed by glutelin, albumin and the flour. The globulin in vivo digestibility did not differ significantly from that obtained to casein. Despite the high digestibility encountered for the major protein fraction and protein fractions, the use as the only protein source in the diets revealed low values for RNPR (relative net protein ratio), showing it to be insufficient in terms of sustaining the growth of animals, comparatively to casein. Keywords: Lupinus albus, protein fractions, major globulin, in ...

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Section: -Introduçãounclassified

Isolamento da globulina majoritária, digestibilidade in vivo e in vitro das proteínas do tremoço-doce (Lupinus albus L.), var. Multolupa

Neves

Silva

2006

Ciênc. Tecnol. Aliment.

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“…In lupin seeds, storage proteins are mainly represented by legumin-and vicilin-like proteins, also named 11s and 7s globulins respectively, which together account for about 80% of total globulins [2]. Other minor fractions have been found and some of them have also been isolated and partially char- Like most seed storage proteins, conglutin y is synthesized during early seed development as a precursor polypeptide of about 50 kDa, which is soon proteolytically cleaved to mature subunits [6, 71 and deposited in the protein bodies of lupin cotyledonary cells [7-91.…”

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confidence: 99%

Heat‐induced synthesis and tunicamycin‐sensitive secretion of the putative storage glycoprotein conglutin γ from mature lupin seeds

Duranti

Scarafoni

Gius

et al. 1994

European Journal of Biochemistry

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) -E.IB 94 0179/1 SDSRAGE, inmune blotting with specific antibodies and amino acid sequence analyses revealed that 90% of the protein released from Lupinus albus seeds incubated in water at 60°C for about 3 h was conglutin y , a putative storage glycoprotein already present in the protein bodies of mature seeds. Incorporation of ['4C]leucine into the protein demonstrated that conglutin y was newly synthesized during the treatment and the use of protein synthesis inhibitors ruled out the secretion of constitutive conglutin y. Synthesis and secretion took place only over a narrow temperature range, 57.5 -62.5 "C, and in a short time interval, 135 -180 min, of incubation of the seed. The amount of secreted conglutin y, i.e. 1 mg/seed, was about three times that present inside the treated or untreated seed.Secreted conglutin y contained covalently linked carbohydrate as well as the constitutive protein. Inhibition of the glycosylation by tunicamycin did not affect conglutin y synthesis, but prevented its secretion from the seed, as indicated by quantifying conglutin y remaining in the seed. An accumulation of the protein outside the protein bodies and at the cotyledonary cell periphery was shown in these samples by immunocytochemistry.Peptide mapping of the fragments obtained by incubation of constitutive and secreted conglutin y with trypsin and pepsin revealed no difference between the two proteins.Lupin seeds were still viable after the treatment. However no similarities between conglutin y and heat-shock proteins were observed either in the amino acid sequence or other molecular features.The essential role of seed storage proteins is to serve as nitrogen and carbon skeleton sources for the plantlet developing during germination [l].In lupin seeds, storage proteins are mainly represented by legumin-and vicilin-like proteins, also named 11s and 7s globulins respectively, which together account for about 80% of total globulins [2]. Other minor fractions have been found and some of them have also been isolated and partially char- Like most seed storage proteins, conglutin y is synthesized during early seed development as a precursor polypeptide of about 50 kDa, which is soon proteolytically cleaved to mature subunits [6, 71 and deposited in the protein bodies of lupin cotyledonary cells [7-91. However the amino acid Correspondence to M. Duranti,

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“…L. albus is rich in lupin proteins that belong to the vast families of 11S and 7S globulins of which conglutin-γ makes up 5% of the total globulins. Isolated lupin conglutin-γ has demonstrable hypoglycaemic effects in glucose loaded non diabetic experimental animals (Duranti et al, 1981;Magni et al, 2004; Bertoglio et al, 2011) and show insulin-mimetic effects in cultured cells (Komatsu and Hirano, 1991;Terruzzi et al, 2011). In addition, alkaloids from L. albus, is responsible for the bitter taste, also possess hypoglycaemic effects via increased insulin secretion in cultured pancreatic cells (Garzia Lopez et al, 2004;Oraby et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Investigation of hypogycemic and hypolipidemic effects of an aqueous extract of <i>Llupinus albus</i> legume seed in Streptozotocin-induced type I diabetic rats

Sewani-Rusike¹,

Jumbam²,

Chinhoyi³

et al. 2015

Afr. J. Trad. Compl. Alt. Med.

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Background: Lupinus albus (LA) seed is a legume food used traditionally for the treatment of diabetes. The aim of this study was to investigate the effects of an aqueous extract of LA on lipid and glucose levels in normal and STZ induced Type 1 diabetic rats. Methods: Aqueous extract of LA was prepared and used for animal treatments. Diabetes was induced by a single intraperitoneal injection of streptozotocin (60mg/kg body weight). Effects of LA on oral glucose tolerance in normal and diabetic rats were investigated by giving a single dose of distilled water (controls), 200 or 400mg/kg LA extract, metformin 300mg/kg or glibenclamide 500µg/kg after 12 hours of fasting (time 0 glucose). After 15 minutes, a glucose load (3g/kg) was given. Glucose levels were measured at 30, 60, and 120 minutes after glucose loading. To investigate long term effects, animals were given similar treatments daily for 4 weeks. At the end of the study, serum glucose, insulin, total cholesterol (TC), triglycerides (TG), low density lipoprotein (LDL-C), very low density lipoprotein (VLDL-C) and high density lipoprotein (HDL-C) cholesterol levels were measured or calculated. Results: LA demonstrated significant (P<0.001) hypoglycaemic effects in normal rats but not in diabetic rats after acute and long term treatment. Normal LA treated rats showed higher (P<0.001) insulin levels compared to normal controls but insulin remained very low in diabetic rats. Diabetic rats showed diabetes associated weight loss in both treated and untreated rats. However, LA was effective in reducing atherogenic lipid levels (TC, TG, LDL-C VLDLC; P<0.001) with no change (P>0.05) in HDL-C. Conclusion:We conclude that the use of Lupinus albus among various communities may not be effective in treating hyperglycaemia in type 1 diabetes but effective for treating diabetes induced dyslipidemia.Key words: glucose tolerance, lipids, Lupinus albus, streptozotocin, type 1 diabetes. IntroductionPlants have historically served as a source of food and drugs. The term "nutraceutical" was coined by Stephen De Feliceto blending the two plant functions (Scarafoni et al., 2007). Nutritionally, there is a worldwide shift towards using plant sources as protein in place of animal sources. This is deemed a healthier dietary choice towards the reduction of diet related diseases such as obesity, hypertension, cardiovascular disease and type II diabetes (Arnoldi and Greco, 2011). As such, storage proteins from legumes have been the choice substitute for animal proteins. Soya bean is the most used legume that also possesses cholesterol reducing effects (Anderson et al., 1995;Sirtori et al., 1998;Sirtori et al., 2007).Lately, there has been a growing interest in other legumes as protein sources for human nutrition. One such legume is white lupin, Lupinus albus. This is an annual plant belonging to the class Leguminosae. It is grown in the Middle East and Africa as a food legume. In South Africa it is mostly grown in the Western Cape for animal feed (Brand and Brandt, 2000). In addi...

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The seed globulins of Lupinus albus

Cited by 116 publications

References 21 publications

Isolamento da globulina majoritária, digestibilidade in vivo e in vitro das proteínas do tremoço-doce (Lupinus albus L.), var. Multolupa

Isolamento da globulina majoritária, digestibilidade in vivo e in vitro das proteínas do tremoço-doce (Lupinus albus L.), var. Multolupa

Heat‐induced synthesis and tunicamycin‐sensitive secretion of the putative storage glycoprotein conglutin γ from mature lupin seeds

Investigation of hypogycemic and hypolipidemic effects of an aqueous extract of <i>Llupinus albus</i> legume seed in Streptozotocin-induced type I diabetic rats

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