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Journal articles on the topic 'Conglutin'

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Author: Grafiati

Published: 3 May 2023

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1

Ferreira, RB, TS Melo, and AN Teixeira. "Catabolism of the Seed Storage Proteins From Lupinus Albus: Fate of Globulins During Germination and Seedling Growth." Functional Plant Biology 22, no. 3 (1995): 373. http://dx.doi.org/10.1071/pp9950373.

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The degradation of the major seed storage globulins of Lupinus albus L. was studied during the first 11 days after the onset of germination. The collagenolytic activity present in cotyledonary extracts was found to closely follow the rate and pattern of total globulin degradation. Little or no degradation of the three main globulins was observed during the first days of germination and seedling growth. The rate of proteolysis of the �-conglutin main subunit, composed of one heavy glycopolypeptide chain and one light non-glycosylated polypeptide chain, occurs gradually between days 3 and 11, with no apparent change in the globulin structure being detected during this time. Between days 3 and 5, �-conglutin, with at least 14 of its heavier polypeptide chains glycosylated, suffers a dramatic change in its structure and concentration, involving the appearance of a new set of polypeptides including a higher molecular mass group, whose concentration steadily declines until complete disappearance after 11 days, and a lighter molecular mass group, whose concentration surprisingly increases from 5 to 11 days. Finally, �-conglutin, with each of its four main subunits composed of a heavy glycopolypeptide chain and a 19 kDa non-glycosylated polypeptide chain, undergoes a pattern of degradation intermediate to those described for �- and �-conglutins in the sense that the new set of polypeptides coexist with polypeptides that were already present in the dry seed. The degradation of a-conglutin subunits starts at the level of their heavier polypeptide chains, releasing the intact 19 kDa polypeptide which gradually disappears after day 7. Our results indicate that �-, �- and �-conglutins are subjected to differential proteolysis during germination and seedling growth. Furthermore, the different polypeptide chains of each conglutin are also degraded at significantly different rates.

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2

Lima-Cabello, Elena, Julia Escudero-Feliu, Andreina Peralta-Leal, Pedro Garcia-Fernandez, Kadambot H. M. Siddique, Karam B. Singh, Maria I. Núñez, Josefa León, and Jose C. Jimenez-Lopez. "β-Conglutins’ Unique Mobile Arm Is a Key Structural Domain Involved in Molecular Nutraceutical Properties of Narrow-Leafed Lupin (Lupinus angustifolius L.)." International Journal of Molecular Sciences 24, no. 8 (April 21, 2023): 7676. http://dx.doi.org/10.3390/ijms24087676.

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Narrow-leafed lupin (NLL; Lupinus angustifolius L.) has multiple nutraceutical properties that may result from unique structural features of β-conglutin proteins, such as the mobile arm at the N-terminal, a structural domain rich in α-helices. A similar domain has not been found in other vicilin proteins of legume species. We used affinity chromatography to purify recombinant complete and truncated (without the mobile arm domain, tβ5 and tβ7) forms of NLL β5 and β7 conglutin proteins. We then used biochemical and molecular biology techniques in ex vivo and in vitro systems to evaluate their anti-inflammatory activity and antioxidant capacity. The complete β5 and β7 conglutin proteins decreased pro-inflammatory mediator levels (e.g., nitric oxide), mRNA expression levels (iNOS, TNFα, IL-1β), and the protein levels of pro-inflammatory cytokine TNF-α, interleukins (IL-1β, IL-2, IL-6, IL-8, IL-12, IL-17, IL-27), and other mediators (INFγ, MOP, S-TNF-R1/-R2, and TWEAK), and exerted a regulatory oxidative balance effect in cells as demonstrated in glutathione, catalase, and superoxide dismutase assays. The truncated tβ5 and tβ7 conglutin proteins did not have these molecular effects. These results suggest that β5 and β7 conglutins have potential as functional food components due to their anti-inflammatory and oxidative cell state regulatory properties, and that the mobile arm of NLL β-conglutin proteins is a key domain in the development of nutraceutical properties, making NLL β5 and β7 excellent innovative candidates as functional foods.

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3

Tesarowicz, Iwona, Agnieszka Zawiślak, Ireneusz Maciejaszek, and Krzysztof Surówka. "Effect of Alcalase Modification of Yellow Lupin (Lupinus luteus L.) Protein Isolate on Some Functional Properties and Antioxidant Activity." International Journal of Food Science 2022 (November 18, 2022): 1–10. http://dx.doi.org/10.1155/2022/6187441.

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Protein isolate obtained from sweet yellow lupin (Lupinus luteus L.) and its Alcalase hydrolysates were examined for their functional and antioxidant properties in relation to surface hydrophobicity of proteins and peptides and molecular weight distribution. Enzymatic hydrolysis improved the foaming characteristics of lupin proteins, while the emulsifying properties deteriorated. It means that good foaming properties of preparations are determined by the presence of low-molecular δ conglutin and small subunits of γ conglutins. In turn, larger proteins such as α and β conglutin are responsible for maintaining good emulsifying properties. The measured surface hydrophobicity was consistent with the results of emulsifying properties. It has also been shown that the scope of changes in antioxidant properties due to hydrolysis, measured by DPPH method and as reducing power, is more pronounced than with the use of ABTS and FRAP methods.

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4

Bush, Roy S., and Helen Tai. "Preparation of rabbit polyclonal antibodies against lupin storage proteins." Canadian Journal of Plant Science 74, no. 1 (January 1, 1994): 93–96. http://dx.doi.org/10.4141/cjps94-016.

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Agarose gel electrophoresis was used to separate three globular storage proteins from crude extracts of Lupinus albus seeds. Conglutin α, β, and γ purified by this technique were used as antigens to stimulate the production of antibodies in rabbits. The specificity of polyclonal antibodies produced was analysed by Western blot. Each antibody reacted with the specific antigen used to stimulate production of that antibody. In addition the anti-conglutin α preparation also showed binding to a region of the gel that comigrates with conglutin β. Key words: Lupin, conglutin, polyclonal antibody

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5

Rosa Lovati, Maria, Cristina Manzoni, Silvia Castiglioni, Anna Parolari, Chiara Magni, and Marcello Duranti. "Lupin seed γ-conglutin lowers blood glucose in hyperglycaemic rats and increases glucose consumption of HepG2 cells." British Journal of Nutrition 107, no. 1 (June 28, 2011): 67–73. http://dx.doi.org/10.1017/s0007114511002601.

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The aim of the present study was to evaluate the effect of a chronic oral γ-conglutin treatment in male Sprague–Dawley rats in which hyperglycaemia had been induced by supplying 10 %d-glucose in drinking-water. A γ-conglutin dosage of 28 mg/kg body weight was daily administered to animals for 21 d. Plasma glucose, insulin and glucose overloading were monitored. Chronic administration of glucose resulted in a statistically significant (P < 0·05) increase in fasting blood glucose (2·5-fold) and insulin (2·7-fold)v.the values recorded in control rats. Simultaneous treatment with γ-conglutin attenuated the rise in plasma glucose (1·9-fold) and insulin (1·8-fold) levels in the glucose-fed rats (P < 0·05). Fasting insulin and homeostasis model of insulin resistance were decreased by 34 and 48 % (P < 0·05), respectively, in the γ-conglutin-treated ratsv.the values found in pair-fed animals. To confirm these results with a different approach, HepG2 cells, grown for 24 and 48 h in Dulbecco's minimum essential medium containing different glucose concentrations (5·5, 11·1 and 16·5 mmol/l), were exposed to 10 μmol/l γ-conglutin with or without 10 mmol/l metformin or 100 nmol/l insulin. γ-Conglutin increased glucose consumption (from 1·5- to 2·5-fold) in HepG2 cells, under all experimental conditions; this effect was more evident after 48 h incubation. Moreover, in thisin vitromodel, the addition of γ-conglutin potentiated the activity of insulin and metformin in cell glucose consumption. These findings extend the previous ones and suggest the potential use of lupin γ-conglutin in the control of glycaemia.

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6

Devkota, Lavaraj, Konstantina Kyriakopoulou, Robert Bergia, and Sushil Dhital. "Structural and Thermal Characterization of Protein Isolates from Australian Lupin Varieties as Affected by Processing Conditions." Foods 12, no. 5 (February 21, 2023): 908. http://dx.doi.org/10.3390/foods12050908.

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Proteins from the full and defatted flours of L. angustifolius cv Jurien and L. albus cv Murringo were prepared using alkaline extraction and iso-electric precipitation. Isolates were either freeze dried or spray dried or pasteurized at 75 ± 3 °C/5 min before freeze-drying. Various structural properties were investigated to elucidate the varietal and processing-induced effect on molecular and secondary structure. Irrespective of processing, isolated proteins had a similar molecular size, with α-conglutin (412 kDa) and β-conglutin (210 kDa) being principal fractions for the albus and angustifolius variety, respectively. Smaller peptide fragments were observed for the pasteurized and spray dried samples, indicating some degree of processing-induced changes. Furthermore, secondary structure characterization by Fourier-transform-infrared and circular dichroism spectroscopy showed β-sheet and α-helical structure being the dominant structure, respectively. Thermal characterization showed two denaturation peaks corresponding to β-conglutin (Td = 85–89 °C) and α-conglutin (Td = 102–105 °C) fractions. However, the enthalpy values for α-conglutin denaturation were significantly higher for albus species, which corroborates well with higher amounts of heat stable α-conglutin present. Amino acid profile was similar for all samples with limiting sulphur amino acid. In summary, commercial processing conditions did not have a profound effect on the various structural properties of lupin protein isolates, and properties were mainly determined by varietal differences.

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7

Czubinski, Jaroslaw, Jakub Barciszewski, Miroslaw Gilski, Kamil Szpotkowski, Janusz Debski, Eleonora Lampart-Szczapa, and Mariusz Jaskolski. "Structure of γ-conglutin: insight into the quaternary structure of 7S basic globulins from legumes." Acta Crystallographica Section D Biological Crystallography 71, no. 2 (January 23, 2015): 224–38. http://dx.doi.org/10.1107/s1399004714025073.

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γ-Conglutin from lupin seeds is an unusual 7S basic globulin protein. It is capable of reducing glycaemia in mammals, but the structural basis of this activity is not known. γ-Conglutin shares a high level of structural homology with glycoside hydrolase inhibitor proteins, although it lacks any kind of inhibitory activity against plant cell-wall degradation enzymes. In addition, γ-conglutin displays a less pronounced structural similarity to pepsin-like aspartic proteases, but it is proteolytically dysfunctional. Only one structural study of a legume 7S basic globulin, that isolated from soybean, has been reported to date. The quaternary assembly of soybean 7S basic globulin (Bg7S) is arranged as a cruciform-shaped tetramer comprised of two superposed dimers. Here, the crystal structure of γ-conglutin isolated fromLupinus angustifoliusseeds (LangC) is presented. The polypeptide chain of LangC is post-translationally cleaved into α and β subunits but retains its covalent integrity owing to a disulfide bridge. The protomers of LangC undergo an intricate quaternary assembly, resulting in a ring-like hexamer with noncrystallographicD3symmetry. The twofold-related dimers are similar to those in Bg7S but their assembly is different as a consequence of mutations in a β-strand that is involved in intermolecular β-sheet formation in γ-conglutin. Structural elucidation of γ-conglutin will help to explain its physiological role, especially in the evolutionary context, and will guide further research into the hypoglycaemic activity of this protein in humans, with potential consequences for novel antidiabetic therapies.

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8

Aiello, Gilda, Yuchen Li, Giovanna Boschin, Marco Stanziale, Carmen Lammi, and Anna Arnoldi. "Analysis of Narrow-Leaf Lupin Proteins in Lupin-Enriched Pasta by Untargeted and Targeted Mass Spectrometry." Foods 9, no. 8 (August 8, 2020): 1083. http://dx.doi.org/10.3390/foods9081083.

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The supplementation of different food items with grain legumes and, in particular, with lupin has been demonstrated to provide useful health benefits, especially in the area of cardiovascular disease prevention. In this work, label free quantitative untargeted and targeted approaches based on liquid chromatography−electrospray ionization−tandem mass spectrometry (LC−ESI−MS/MS) for investigating the protein profile of three pasta samples containing different percentages of narrow-leaf lupin flour were carried out. The untargeted method permitted the identification of the main acidic globulins (α-conglutin, β-conglutin, and δ-conglutin) and the comparison of their profile with raw lupin flour. The targeted method, based on High-performance liquid chromatography electrospray ionization tandem mass spectrometry HPLC-Chip-Multiple Reaction Monitoring (MRM) mode, allowed the quantification of γ-conglutin, the main hypoglycemic component of lupin protein: its concentration was around 2.25 mg/g in sample A, 2.16 mg/g in sample D, and 0.57 mg/g in sample F.

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9

Dooper, Maaike M. B. W., Lise Holden, Christiane K. Fæste, Keith M. Thompson, and Eliann Egaas. "Monoclonal Antibodies against the Candidate Lupin Allergens α-Conglutin and β-Conglutin." International Archives of Allergy and Immunology 143, no. 1 (December 28, 2006): 49–58. http://dx.doi.org/10.1159/000098224.

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10

Lima-Cabello, Elena, Juan D. Alché, Sonia Morales-Santana, Alfonso Clemente, and Jose C. Jimenez-Lopez. "Narrow-Leafed Lupin (Lupinus angustifolius L.) Seeds Gamma-Conglutin is an Anti-Inflammatory Protein Promoting Insulin Resistance Improvement and Oxidative Stress Amelioration in PANC-1 Pancreatic Cell-Line." Antioxidants 9, no. 1 (December 23, 2019): 12. http://dx.doi.org/10.3390/antiox9010012.

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(1) Background: Inflammation molecular cues and insulin resistance development are some of the main contributors for the development and advance of the pathogenesis of inflammatory-related diseases; (2) Methods: We isolated and purified γ-conglutin protein from narrow-leafed lupin (NLL or blue lupin) mature seeds using affinity-chromatography to evaluate its anti-inflammatory activities at molecular level using both, a bacterial lipopolysaccharide (LPS)-induced inflammation and an insulin resistance pancreatic cell models; (3) Results: NLL γ-conglutin achieved a plethora of functional effects as the strong reduction of cell oxidative stress induced by inflammation through decreasing proteins carbonylation, nitric oxide synthesis and inducible nitric oxide synthase (iNOS) transcriptional levels, and raising glutathione (GSH) levels and modulation of superoxide dismutase (SOD) and catalase enzymes activities. γ-conglutin induced up-regulated transcriptomic and protein levels of insulin signalling pathway IRS-1, Glut-4, and PI3K, improving glucose uptake, while decreasing pro-inflammatory mediators as iNOs, TNFα, IL-1β, INFγ, IL-6, IL-12, IL-17, and IL-27; (4) Conclusion: These results suggest a promising use of NLL γ-conglutin protein in functional foods, which could also be implemented in alternative diagnosis and therapeutic molecular tools helping to prevent and treat inflammatory-related diseases.

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11

Lima-Cabello, Elena, Juan D. Alché, and Jose C. Jimenez-Lopez. "Narrow-Leafed Lupin Main Allergen β-Conglutin (Lup an 1) Detection and Quantification Assessment in Natural and Processed Foods." Foods 8, no. 10 (October 18, 2019): 513. http://dx.doi.org/10.3390/foods8100513.

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The increasing prevalence of lupin allergy as a consequence to the functional characteristics of a growing number of sweet lupin-derived foods consumption makes the imperious necessity to develop analytical tools for the detection of allergen proteins in foodstuffs. The current study developed a new highly specific, sensitive and accurate ELISA method to detect, identify and quantify the lupin main allergen β-conglutin (Lup an 1) protein in natural and processed food. The implementation of accurate standards made with recombinant conglutin β1, and an anti-Lup an 1 antibody made from a synthetic peptide commonly shared among β-conglutin isoforms from sweet lupin species was able to detect up to 8.1250 ± 0.1701 ng (0.0406 ± 0.0009 ppm) of Lup an 1. This identified even lupin traces present in food samples which might elicit allergic reactions in sensitized consumers, such as β-conglutin proteins detection and quantification in processed (roasted, fermented, boiled, cooked, pickled, toasted, pasteurized) food, while avoiding cross-reactivity (false positive) with other legumes as peanut, chickpea, lentils, faba bean, and cereals. This study demonstrated that this new ELISA method constitutes a highly sensitive and reliable molecular tool able to detect, identify and quantify Lup an 1. This contributes to a more efficient management of allergens by the food industry, the regulatory agencies and clinicians, thus helping to keep the health safety of the consumers.

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12

Lima-Cabello, Elena, Sonia Morales-Santana, Josefa León, Victor Alché, Alfonso Clemente, Juan D. Alché, and Jose C. Jimenez-Lopez. "Narrow-leafed lupin (Lupinus angustifoliusL.) seed β-conglutins reverse the induced insulin resistance in pancreatic cells." Food & Function 9, no. 10 (2018): 5176–88. http://dx.doi.org/10.1039/c8fo01164h.

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13

Johnson, E. D., J. Knight, and K. R. Gayler. "Biosynthesis and processing of legumin-like storage proteins in Lupinus angustifolius (lupin)." Biochemical Journal 232, no. 3 (December 15, 1985): 673–79. http://dx.doi.org/10.1042/bj2320673.

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Synthesis, secretion and post-translational proteolysis of the storage proteins in cotyledons of Lupinus angustifolius L. (lupin) have been examined in vivo and in vitro by using a combination of pulse-chase experiments with [3H]- or [35S]-labelled amino acids, subcellular fractionation and cell-free translation from poly(A)+ (polyadenylylated) RNA or membrane-bound polyribosomes. Related polypeptides were identified by immunoprecipitation, separation on sodium dodecyl sulphate/polyacrylamide gels and fluorography. The synthesis and processing of two proteins were compared. Conglutin alpha, the 11 S protein, was found as a family of precursor polypeptides of Mr 68000-88000 when translated from poly(A)+ RNA under conditions where signal segments were not cleaved, and Mr 64000-85000 both when sequestered into the endoplasmic reticulum and when accumulated in the protein bodies. Pulse-chase labelling showed that cotyledons from early stages of development were completely incapable of further proteolysis of these precursors. Nevertheless, in the same juvenile cotyledons, the precursors of the minor storage protein conglutin gamma, two polypeptides with Mr 50000-51000, were proteolytically cleaved to mature subunits of Mr 32000 and 17000 within 2 h. Further cleavage of the precursors of conglutin alpha into families of mature subunits of Mr 21000-24000 and 42000-62000 was detected in more mature cotyledons. A model is proposed which suggests that the mature subunits are produced by a single proteolytic cleavage of each of the three major precursors of conglutin alpha and also suggests that a close similarity exists between these subunits and those of other legumin-like proteins. The enzyme responsible for this cleavage, which appears at a specific stage in the middle of cotyledonary development, seems to be an integral part of the programmed developmental sequence in these pods.

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14

Jauset Rubio, Miriam, Markéta Svobodová, Teresa Mairal, Thomas Schubert, Stefan Künne, Günter Mayer, and Ciara K. O’Sullivan. "β-Conglutin dual aptamers binding distinct aptatopes." Analytical and Bioanalytical Chemistry 408, no. 3 (November 19, 2015): 875–84. http://dx.doi.org/10.1007/s00216-015-9179-z.

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15

MARTÍNEZ-AYALA, ALMA LETICIA, and OCTAVIO PAREDES-LÓPEZ. "MOLECULAR CHARACTERIZATION OF THE ?-CONGLUTIN OF LUPIN SEEDS." Journal of Food Biochemistry 25, no. 1 (February 2001): 15–31. http://dx.doi.org/10.1111/j.1745-4514.2001.tb00722.x.

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16

Jauset-Rubio, Miriam, Mayreli Ortiz, and Ciara K. O’Sullivan. "Exploiting the Nucleic Acid Nature of Aptamers for Signal Amplification." Biosensors 12, no. 11 (November 4, 2022): 972. http://dx.doi.org/10.3390/bios12110972.

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Aptamer-based assays and sensors are garnering increasing interest as alternatives to antibodies, particularly due to their increased flexibility for implementation in alternative assay formats, as they can be employed in assays designed for nucleic acids, such as molecular aptamer beacons or aptamer detection combined with amplification. In this work, we took advantage of the inherent nucleic acid nature of aptamers to enhance sensitivity in a rapid and facile assay format. An aptamer selected against the anaphylactic allergen β-conglutin was used to demonstrate the proof of concept. The aptamer was generated by using biotinylated dUTPs, and the affinity of the modified aptamer as compared to the unmodified aptamer was determined by using surface plasmon resonance to calculate the dissociation constant (KD), and no significant improvement in affinity due to the incorporation of the hydrophobic biotin was observed. The modified aptamer was then applied in a colorimetric competitive enzyme-linked oligonucleotide assay, where β-conglutin was immobilized on the wells of a microtiter plate, competing with β-conglutin free in solution for the binding to the aptamer. The limit of detection achieved was 68 pM, demonstrating an improvement in detection limit of three orders of magnitude as compared with the aptamer simply modified with a terminal biotin label. The concept was then exploited by using electrochemical detection and screen-printed electrodes where detection limits of 326 fM and 7.89 fM were obtained with carbon and gold electrodes, respectively. The assay format is generic in nature and can be applied to all aptamers, facilitating an easy and cost-effective means to achieve lower detection limits.

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17

Duranti, M., A. Scarafoni, A. Di Cataldo, and F. Sessa. "Interaction of metal ions with lupin seed conglutin γ." Phytochemistry 56, no. 6 (March 2001): 529–33. http://dx.doi.org/10.1016/s0031-9422(00)00426-x.

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18

Svobodova, Marketa, Teresa Mairal, Pedro Nadal, M. Carmen Bermudo, and Ciara K. O’Sullivan. "Ultrasensitive aptamer based detection of β-conglutin food allergen." Food Chemistry 165 (December 2014): 419–23. http://dx.doi.org/10.1016/j.foodchem.2014.05.128.

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19

Czubiński, Jarosław, Magdalena Montowska, and Emilia Fornal. "Post-translational cleavage pattern of Lupinus angustifolius γ-conglutin." Journal of the Science of Food and Agriculture 98, no. 14 (May 24, 2018): 5212–19. http://dx.doi.org/10.1002/jsfa.9057.

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20

Liang, X. Q., C. C. Holbrook, R. E. Lynch, and B. Z. Guo. "β-1,3-Glucanase Activity in Peanut Seed (Arachis hypogaea) is Induced by Inoculation with Aspergillus flavus and Copurifies with a Conglutin-Like Protein." Phytopathology® 95, no. 5 (May 2005): 506–11. http://dx.doi.org/10.1094/phyto-95-0506.

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Infection of peanut (Arachis hypogaea) seed by Aspergillus flavus and A. parasiticus is a serious problem that can result in aflatoxin contamination in the seed. Breeding resistant cultivars would be an effective approach to reduce aflatoxin accumulation. The objective of this study was to investigate the expression of the pathogenesis-related (PR) protein β-1,3-glucanase and the isoform patterns in peanut seed inoculated with A. flavus. Peanut genotypes GT-YY9 and GT-YY20 (both resistant to A. flavus infection) and Georgia Green and A100 (both susceptible to A. flavus infection) were used in this study. The activities of β-1,3-glucanase were similar in the uninfected seed of all genotypes, but increased significantly in the resistant genotypes after inoculation in comparison with the susceptible genotypes. An in-gel (native polyacrylamide gel electrophoresis [PAGE]) enzymatic activity assay of β-1,3-glucanase revealed that there were more protein bands corresponding to β-1,3-glucanase isoforms in the infected seed of resistant genotypes than in the infected seed of susceptible genotypes. Both acidic and basic β-1,3-glucanase isoforms were detected in the isoelectric focusing gels. Thin-layer chromatography analysis of the hydrolytic products from the reaction mixtures of the substrate with the total protein extract or individual band of native PAGE revealed the presence of enzymatic hydrolytic oligomer products. The individual bands corresponding to the bands of β-1,3-glucanase isoforms Glu 1 to 5 were separated on the sodium dodecyl sulfate-PAGE, resulting in two bands of 10 and 13 kDa, respectively. The sequences of fragments of the 13-kDa major protein band showed a high degree of homology to conglutin, a storage protein in peanut seed. Conglutin is reported as a peanut allergen, Ara h2. Our data provide the first evidences for peanut having β-1,3-glucanase activities and the association with the resistance to A. flavus colonization in peanut seed. We have not directly demonstrated that conglutin has β-1,3-glucanase activity.

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21

Villa, Caterina, Mónica B. M. V. Moura, Joana Costa, and Isabel Mafra. "Immunoreactivity of Lupine and Soybean Allergens in Foods as Affected by Thermal Processing." Foods 9, no. 3 (February 27, 2020): 254. http://dx.doi.org/10.3390/foods9030254.

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Lupine and soybean are important technological aids for the food industry. However, they are also capable of inducing severe allergic reactions in food-sensitized/allergic individuals. In this context, this work intended to study the combined effects of thermal processing and food matrix on the immunoreactivity of lupine and soybean proteins used as ingredients in bakery and meat products, respectively. For this purpose, the effects of baking, mild oven cooking, and autoclaving on the protein profiles were evaluated, using model mixtures simulating the production of lupine-containing breads and soybean-containing cooked hams/sausages, by native- and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and immunoblotting using specific antibodies. The results showed that lupine gamma-conglutin immunoreactivity was slightly decreased in wheat flour mixtures compared to rice, but it was more pronounced in baked products. In meat mixtures, substantial protein fragmentation was noted after autoclaving, with decreased immunoreactivity of soybean trypsin inhibitor. The analysis of 22 commercial products enabled the identification of lupine gamma-conglutin in four bakery samples and soybean trypsin-inhibitor in five sausages, and further differentiated autoclaved from other milder thermally treated products. Generally, the immunoreactivity of target proteins was reduced by all the tested thermal treatments, though at a higher extent after autoclaving, being slightly altered by the food matrix.

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22

Duranti, Marcello, Fabio Sessa, Alessio Scarafoni, Tiziana Bellini, and Franco Dallocchio. "Thermal Stabilities of Lupin Seed Conglutin γ Protomers and Tetramers." Journal of Agricultural and Food Chemistry 48, no. 4 (April 2000): 1118–23. http://dx.doi.org/10.1021/jf9907384.

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23

Mane, Sharmilee P., Stuart K. Johnson, Marcello Duranti, Vishnu K. Pareek, and Ranjeet P. Utikar. "Lupin seed γ-conglutin: Extraction and purification methods - A review." Trends in Food Science & Technology 73 (March 2018): 1–11. http://dx.doi.org/10.1016/j.tifs.2017.12.008.

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24

Czubinski, Jaroslaw. "Insight into thermally induced structural changes of lupin seed γ-conglutin." Food Chemistry 354 (August 2021): 129480. http://dx.doi.org/10.1016/j.foodchem.2021.129480.

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25

Wojciechowicz, Tatiana, Jarosław Czubiński, Maria Billert, Artur Półciennik, Krzysztof W. Nowak, and Marek Skrzypski. "Suppressive effects of γ-conglutin on differentiation of 3T3-L1 preadipocytes." International Journal of Food Science & Technology 53, no. 11 (June 19, 2018): 2624–30. http://dx.doi.org/10.1111/ijfs.13860.

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26

Santos, Cláudia N., Marta Alves, António Oliveira, and Ricardo B. Ferreira. "β-N-Acetylhexosaminidase involvement in α-conglutin mobilization in Lupinus albus." Journal of Plant Physiology 170, no. 12 (August 2013): 1047–56. http://dx.doi.org/10.1016/j.jplph.2013.03.009.

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27

Monteiro, Sara, Regina Freitas, Baru T. Rajasekhar, Artur R. Teixeira, and Ricardo B. Ferreira. "The Unique Biosynthetic Route from Lupinus β-Conglutin Gene to Blad." PLoS ONE 5, no. 1 (January 6, 2010): e8542. http://dx.doi.org/10.1371/journal.pone.0008542.

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28

Tapadia, Mrunmai, Stuart Johnson, Ranjeet Utikar, Philip Newsholme, and Rodrigo Carlessi. "Antidiabetic effects and mechanisms of action of γ-conglutin from lupin seeds." Journal of Functional Foods 87 (December 2021): 104786. http://dx.doi.org/10.1016/j.jff.2021.104786.

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29

Jauset Rubio, Miriam, Markéta Svobodová, Teresa Mairal, and Ciara K. O’Sullivan. "Surface plasmon resonance imaging (SPRi) for analysis of DNA aptamer:β-conglutin interactions." Methods 97 (March 2016): 20–26. http://dx.doi.org/10.1016/j.ymeth.2015.10.013.

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Species, Within Lupin, M. A. Esnault, V. Pichereau, and J. Klingler. "Variability of the Low Molecular Weight Globulin, Conglutin δ, Within Lupin Species." Botanica Acta 110, no. 2 (April 1997): 164–71. http://dx.doi.org/10.1111/j.1438-8677.1997.tb00624.x.

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Mota, Joana, Rosa Direito, João Rocha, João Fernandes, Bruno Sepodes, Maria Eduardo Figueira, Anabela Raymundo, Ana Lima, and Ricardo Boavida Ferreira. "Lupinus albus Protein Components Inhibit MMP-2 and MMP-9 Gelatinolytic Activity In Vitro and In Vivo." International Journal of Molecular Sciences 22, no. 24 (December 10, 2021): 13286. http://dx.doi.org/10.3390/ijms222413286.

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Matrix metalloproteinases 2 and 9 (MMP-2 and MMP-9) are regarded as important clinical targets due to their nodal-point role in inflammatory and oncological diseases. Here, we aimed at isolating and characterizing am MMP-2 and-9 inhibitor (MMPI) from Lupinus albus and at assessing its efficacy in vitro and in vivo. The protein was isolated using chromatographic and 2-D electrophoretic procedures and sequenced by using MALDI-TOF TOF and MS/MS analysis. In vitro MMP-2 and 9 inhibitions were determined on colon adenocarcinoma (HT29) cells, as well as by measuring the expression levels of genes related to these enzymes. Inhibitory activities were also confirmed in vivo using a model of experimental TNBS-induced colitis in mice, with oral administrations of 15 mg·kg−1. After chromatographic and electrophoretic isolation, the L. albus MMP-9 inhibitor was found to comprise a large fragment from δ-conglutin and, to a lower extent, small fragments of β-conglutin. In vitro studies showed that the MMPI successfully inhibited MMP-9 activity in a dose-dependent manner in colon cancer cells, with an IC50 of 10 µg·mL−1 without impairing gene expression nor cell growth. In vivo studies showed that the MMPI maintained its bioactivities when administered orally and significantly reduced colitis symptoms, along with a very significant inhibition of MMP-2 and -9 activities. Overall, results reveal a novel type of MMPI in lupine that is edible, proteinaceous in nature and soluble in water, and effective in vivo, suggesting a high potential application as a nutraceutical or a functional food in pathologies related to abnormally high MMP-9 activity in the digestive system.

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32

Olczak, Mariusz, Ewa Nizioł, Wiesława Widłak, and Bronisława Morawiecka. "The activity of acid phosphatase and the level of storage proteins during the early stages of germination of Lupinus luteus L. and Lupinus angustifolius L. seeds." Acta Societatis Botanicorum Poloniae 61, no. 2 (2014): 177–85. http://dx.doi.org/10.5586/asbp.1992.015.

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Changes in the level of protein and in the activity of acid phosphatase in seeds of <i>Lupinus luteus</i> L. and <i>Lupinus angustifolius</i> L. during storage and germination were studied. The protein level decreased during germination, mainly as the result of a fall in the concentration of β-conglutin. After an initial decrease in the activity of acid phosphatase activity during the first five days of germination, the activity of this enzyme began to rise with the appearance of two new molecular forms. No significant effect of gibberelin A3 on the specific ativity of acid phosphatase was observed.

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33

Czubinski, Jaroslaw, and Krzysztof Dwiecki. "Molecular structure-affinity relationship of selected phenolic compounds for lupin seed γ-conglutin." Food Hydrocolloids 128 (July 2022): 107561. http://dx.doi.org/10.1016/j.foodhyd.2022.107561.

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34

Schiarea, Silvia, Lolita Arnoldi, Roberto Fanelli, Eric De Combarieu, and Chiara Chiabrando. "In-Depth Glycoproteomic Characterization of γ-Conglutin by High-Resolution Accurate Mass Spectrometry." PLoS ONE 8, no. 9 (September 12, 2013): e73906. http://dx.doi.org/10.1371/journal.pone.0073906.

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35

Terruzzi, I., P. Senesi, C. Magni, A. Montesano, A. Scarafoni, L. Luzi, and M. Duranti. "Insulin-mimetic action of conglutin-γ, a lupin seed protein, in mouse myoblasts." Nutrition, Metabolism and Cardiovascular Diseases 21, no. 3 (March 2011): 197–205. http://dx.doi.org/10.1016/j.numecd.2009.09.004.

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36

Nadal, P., M. Svobodova, T. Mairal, and C. K. O’Sullivan. "Probing high-affinity 11-mer DNA aptamer against Lup an 1 (β-conglutin)." Analytical and Bioanalytical Chemistry 405, no. 29 (October 15, 2013): 9343–49. http://dx.doi.org/10.1007/s00216-013-7385-0.

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37

Mane, Sharmilee, Scott Bringans, Stuart Johnson, Vishnu Pareek, and Ranjeet Utikar. "Reverse phase HPLC method for detection and quantification of lupin seed γ-conglutin." Journal of Chromatography B 1063 (September 2017): 123–29. http://dx.doi.org/10.1016/j.jchromb.2017.08.025.

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38

Ramos, M. Laura, Geraldine Fleming, Ye Chu, Yukio Akiyama, Maria Gallo, and Peggy Ozias-Akins. "Chromosomal and phylogenetic context for conglutin genes in Arachis based on genomic sequence." Molecular Genetics and Genomics 275, no. 6 (April 14, 2006): 578–92. http://dx.doi.org/10.1007/s00438-006-0114-z.

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39

Czubinski, Jaroslaw. "Influence of temperature on secretion and functionality of lupin seed γ ‐conglutin." Journal of the Science of Food and Agriculture 102, no. 7 (November 13, 2021): 2773–82. http://dx.doi.org/10.1002/jsfa.11618.

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40

Jauset-Rubio, Miriam, Jonathan Sabaté del Río, Teresa Mairal, Markéta Svobodová, Mohammad S. El-Shahawi, Abdulaziz S. Bashammakh, Abdulrahman O. Alyoubi, and Ciara K. O’Sullivan. "Ultrasensitive and rapid detection of β-conglutin combining aptamers and isothermal recombinase polymerase amplification." Analytical and Bioanalytical Chemistry 409, no. 1 (October 20, 2016): 143–49. http://dx.doi.org/10.1007/s00216-016-9973-2.

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41

Bertoglio, Juan C., Mario A. Calvo, Juan L. Hancke, Rafael A. Burgos, Antonella Riva, Paolo Morazzoni, Cesare Ponzone, Chiara Magni, and Marcello Duranti. "Hypoglycemic effect of lupin seed γ-conglutin in experimental animals and healthy human subjects." Fitoterapia 82, no. 7 (October 2011): 933–38. http://dx.doi.org/10.1016/j.fitote.2011.05.007.

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42

Kolivas, Sotirios, and Kenwyn R. Gayler. "Structure of the cDNA coding for conglutin ?, a sulphur-rich protein from Lupinus angustifolius." Plant Molecular Biology 21, no. 2 (January 1993): 397–401. http://dx.doi.org/10.1007/bf00019956.

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43

Lilley, Glenn G. "Isolation of conglutin δ, a sulphur-rich protein from the seeds ofLupinus angustifolius L." Journal of the Science of Food and Agriculture 37, no. 1 (January 1986): 20–30. http://dx.doi.org/10.1002/jsfa.2740370104.

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44

Scarafoni, Alessio, Alessandro Consonni, Stefano Pessina, Silvia Balzaretti, Jessica Capraro, Elisabetta Galanti, and Marcello Duranti. "Structural basis of the lack of endo-glucanase inhibitory activity of Lupinus albus γ-conglutin." Plant Physiology and Biochemistry 99 (February 2016): 79–85. http://dx.doi.org/10.1016/j.plaphy.2015.11.008.

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45

Lilley, Glenn G., and Adam S. Inglis. "Amino acid sequence of conglutin δ, a sulfur-rich seed protein of Lupinus angustifolius L." FEBS Letters 195, no. 1-2 (January 20, 1986): 235–41. http://dx.doi.org/10.1016/0014-5793(86)80167-3.

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46

Escudero-Feliu, Julia, María García-Costela, Sara Moreno-SanJuan, Jose D. Puentes-Pardo, Sandra Ríos Arrabal, Paula González-Novoa, María Isabel Núñez, Ángel Carazo, Jose C. Jimenez-Lopez, and Josefa León. "Narrow Leafed Lupin (Lupinus angustifolius L.) β-Conglutin Seed Proteins as a New Natural Cytotoxic Agents against Breast Cancer Cells." Nutrients 15, no. 3 (January 19, 2023): 523. http://dx.doi.org/10.3390/nu15030523.

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Breast cancer (BC) is the most widespread tumor in women and the second type of most common cancer worldwide. Despite all the technical and medical advances in existing therapies, between 30 and 50% of patients with BC will develop metastasis, which contributes to the failure of existing treatments. This situation urges the need to find more effective prevention and treatment strategies like the use of plant-based nutraceutical compounds. In this context, we purified three Narrow Leafed Lupin (NLL) β-conglutins isoforms using affinity-chromatography and evaluated their effectiveness in terms of viability, proliferation, apoptosis, stemness properties, and mechanism of action on both BC cell lines and a healthy one. NLL β-conglutins proteins have very promising effects at the molecular level on BC cells at very low concentrations, emerging as a potential natural cytotoxic agent and preserving the viability of healthy cells. These proteins could act through a dual mechanism involving tumorigenic and stemness-related genes such as SIRT1 and FoxO1, depending on the state of p53. More studies must be carried out to completely understand the underlying mechanisms of action of these nutraceutical compounds in BC in vitro and in vivo, and their potential use for the inhibition of other cancer cell types.

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47

Czubinski, Jaroslaw, and Krzysztof Dwiecki. "Heat-induced changes in lupin seed γ-conglutin structure promote its interaction with model phospholipid membranes." Food Chemistry 374 (April 2022): 131533. http://dx.doi.org/10.1016/j.foodchem.2021.131533.

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48

Capraro, Jessica, Chiara Magni, Alessio Scarafoni, and Marcello Duranti. "Susceptibility of Lupin γ-Conglutin, the Plasma Glucose-Lowering Protein of Lupin Seeds, to Proteolytic Enzymes." Journal of Agricultural and Food Chemistry 57, no. 18 (September 23, 2009): 8612–16. http://dx.doi.org/10.1021/jf9017542.

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49

Goggin, Danica E., Gisela Mir, William B. Smith, Martin Stuckey, and Penelope M. C. Smith. "Proteomic Analysis of Lupin Seed Proteins To Identify Conglutin β as an Allergen, Lup an 1." Journal of Agricultural and Food Chemistry 56, no. 15 (August 2008): 6370–77. http://dx.doi.org/10.1021/jf800840u.

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50

Capraro, Jessica, Chiara Magni, Franco Faoro, Dario Maffi, Alessio Scarafoni, Gabriella Tedeschi, Elisa Maffioli, et al. "Internalisation and multiple phosphorylation of γ-Conglutin, the lupin seed glycaemia-lowering protein, in HepG2 cells." Biochemical and Biophysical Research Communications 437, no. 4 (August 2013): 648–52. http://dx.doi.org/10.1016/j.bbrc.2013.07.026.

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