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Partial characterization of proteins from baru (Dipteryx alata Vog) seeds

CRUZ, Kezia Soares da; SILVA, Maraiza Aparecida da; FREITAS, Osvaldo de; NEVES, Valdir Augusto
Fonte: WILEY-BLACKWELL Publicador: WILEY-BLACKWELL
Tipo: Artigo de Revista Científica
ENG
Relevância na Pesquisa
35.98%
BACKGROUND: Baru (Dipteryx alata Vog.) is a fruit distributed throughout the Brazilian savanna and contains a seed with a high protein content, whose properties have been rarely explored. The purpose of this study was to characterize this protein, especially by isolation and quantifying its fractions and measuring some of its molecular properties. RESULTS: Baru seeds contain 244 g kg(-1) protein on a dry weight basis. Solubility profiles showed a preponderance of globulins. This fraction dominated the seed composition, with 61.7 wt% of the total soluble proteins. Albumins and glutelins accounted for 14 and 3.3 wt%, respectively. SDS-PAGE resolution of albumin and globulin showed main bands with molecular weights of 84 kDa and 64,66 and 73 kDa, respectively. The total protein of the flour and the globulin showed values of in vitro digestibility of 85.59% and 90.54%, relative to casein. Total globulin produced only one chromatographic peak, both on Sepharose CL-6B gel filtration and on DEAE-cellulose ion-exchange columns, eluted at a concentration of 0.12 mol L(-1) NaCl. CONCLUSION: The baru seed had high protein content with large quantities of storage proteins. The chromatographic and solubility profiles indicate the predominance of a fraction with characteristics of a legumin-type protein. (C) 2011 Society of Chemical Industry; FUNDUNESP

Lipídios, carboidratos e proteínas de sementes de leguminosas do Cerrado; Lipids, carbohydrates and proteins of cerrado legume seeds

Sasaki, Mayumi
Fonte: Biblioteca Digitais de Teses e Dissertações da USP Publicador: Biblioteca Digitais de Teses e Dissertações da USP
Tipo: Dissertação de Mestrado Formato: application/pdf
Publicado em 18/04/2008 PT
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35.93%
O cerrado é o segundo maior bioma do país, ocupando em torno de 20 a 25% do território brasileiro, sendo detentor de grande diversidade vegetal. Entretanto, agressões a áreas de cerrado vêm ocorrendo em escala crescente, o que torna urgente estudos detalhados sobre espécies representativas do bioma. O objetivo deste trabalho foi o de analisar o conteúdo de nutrientes orgânicos das sementes de leguminosas, uma das famílias de maior riqueza no cerrado. Foram analisados lipídios, carboidratos e proteínas de oito espécies: Acosmium subelegans, Anadenanthera peregrina var. falcata, Andira laurifolia, Copaifera langsdorfii, Crotalaria flavicoma, Dimorphandra mollis, Hymenaea stigonocarpa e Inga uraguensis. Em geral, as amostras apresentaram baixos teores de lipídios (aproximadamente 5%) e a composição de ácidos graxos mostrou predominância do ácido linoléico na maioria das espécies e também uma tendência a alta proporção de ácidos graxos saturados, principalmente ácido palmítico. A espécie com maior teor foi Acosmium subelegans (13%), que apresentou valor comparável ao de semente de lupino e sua composição de ácidos graxos é similar aos de óleos de girassol, gergelim e milho. As espécies apresentaram teores consideráveis de açúcares solúveis totais (5-10%). Os rendimentos de amido foram baixos (inferior a 1%)...

Accessing gelling ability of vegetable proteins using rheological and fluorescence techniques

Sousa, Isabel; Batista, Ana Paula; Portugal, Carla A.M.; Crespo, João G.; Raymundo, Anabela
Fonte: Elsevier Publicador: Elsevier
Tipo: Artigo de Revista Científica
Publicado em //2005 ENG
Relevância na Pesquisa
35.98%
This work aims to present a comprehensive study about the macroscopic characteristics of globular vegetable proteins, in terms of their gelling ability, by understanding their molecular behaviour, when submitted to a thermal gelling process. The gels of soy, pea and lupin proteins were characterized by rheological techniques. Gelation kinetics, mechanical spectra, as well as the texture of these gels were analyzed and compared. Additionally, capillary viscometry, steady-state fluorescence and fluorescence anisotropy were used to monitor the structural changes induced by the thermal denaturation, which constitutes the main condition for the formation of a gel structure. Based on these techniques it was possible to establish a relationship between the gelling ability of each protein isolate and their structural resistance to thermal unfolding, enabling us to explain the weakest and the strongest gelling ability observed for lupin and soy proteins isolates, respectively

Gelled vegetable desserts containing pea protein, k-carrageenan and starch

Sousa, Isabel; Nunes, M.C.; Raymundo, Anabela
Fonte: Springer Publicador: Springer
Tipo: Artigo de Revista Científica
Publicado em //2006 ENG
Relevância na Pesquisa
36.21%
Due to recent animal diseases, cholesterol in take worries and strong demand for healthy food, there is a greater pressure for the direct consumption of vegetable proteins in food products. In this work, the objective is to develop alternative of strictly vegetable origin desserts based on gelled systems with required physical structure and perceived texture. For this reason, it is important to control the properties of the biopolymer mixtures and understand the phase separation behaviour un- der different physicochemical conditions. The firmness and storage modulus of different formulations of pea protein/k-carrageenan/starch systems processed and cooled at different conditions are compared with those parameters obtained for commercial products. Formulation and thermal conditions were determined to influence the texture and storage modulus of the mixed systems. Confocal microscopic images showed that phase separation between pea protein and k-carrageenan takes place, leading to the formation of two network systems. The binding of water effect, of the starch swollen granules, promotes the concentration of pea protein and k-carrageenan, reinforcing the gel structure.

Vegetable proteins and milk puddings

Sousa, Isabel; Nunes, M.C.; Batista, P.; Raymundo, Anabela; Alves, M.M.
Fonte: Elsevier Publicador: Elsevier
Tipo: Artigo de Revista Científica
Publicado em //2003 ENG
Relevância na Pesquisa
36.17%
In recent years, interest in animal free foods has increased tremendously due to factors like BSE crisis, rise of nutritionally dependent illnesses, like diabetes type II, cardiovascular and digestive diseases, along with ethic orientations of denying animal intakes of any kind. The use of proteins from leguminous seeds as an alternative to the animal proteins in dairy desserts was studied. Lupin, pea and soya protein isolates were used in combination with k- carrageenan, gellan and xanthan gum, in order to obtain a synergistic effect. Milk puddings were also produced for comparison. Texture studies suggested that mixed protein /polysaccharide systems, with vegetable proteins and k- carrageenan or gellan gum, would be good systems to develop vegetable gelled desserts. Rheological oscillatory measurements were carried out to clarify the kinetics of gelation and characterise the microstructure of the best performing products. Results from time sweep tests showed that formulations with gellan gum present an industrial advantage over formulations with k-carrageenan, since the maturation time for gellan gels is of the order of 5 /10 h compared with 4 /6 days in the case of k-carrageenan. All the mixed gels presented the typical weak gel structure; therefore...

Avaliação das propriedade gelificantes e emulsionantes de misturas de proteinas vegetais

Tomé, Ana Sofia Araújo
Fonte: ISA/UTL Publicador: ISA/UTL
Tipo: Dissertação de Mestrado
Publicado em //2012 POR
Relevância na Pesquisa
46.19%
Mestrado em Engenharia Alimentar - Processamento de Alimentos - Instituto Superior de Agronomia; In present work fish proteins from Cape-hake by-products were recovered using alkaline solubilization followed by precipitation at the isoelectric point. Mixtures of these proteins (PRP) and pea proteins (PE) were used to produce gels and emulsions. Functional and nutrition aspects, colour, texture and rheological properties of these gels and emulsions were studied. The gels and emulsions prepared with different protein mixtures presented high whiteness values. The firmness of gels increased with increasing levels of PRP in mixtures. A gel network was rapidly formed upon heating (20 to 90 ºC) and reinforced when cooling down to 5 ºC. Mechanical spectra obtained for gels with different mixtures showed typical patterns of weak gels. Storage modulus (G’) and loss modulus (G’’) increased with PRP concentrations which correspond to more structured systems. Mechanical spectra for emulsions prepared with mixtures of PRP and PE (pH 7,0 and 3,8) are typical of protein-stabilized emulsions in which G’ is higher than G’’ in the frequency range studied. For all emulsions studied, a clear shear-thinning behaviour was noticed upon flow at steady shear. In sensory analysis...

Molecular cloning and characterization of rho, a ras-related small GTP-binding protein from the garden pea.

Yang, Z; Watson, J C
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em 15/09/1993 EN
Relevância na Pesquisa
26.42%
The rho proteins, members of the ras superfamily of small GTP-binding proteins, play a central role in the modulation of cellular functions involving the actin cytoskeleton such as in the establishment of cell polarity and morphology. As a first step in elucidating signal transduction pathways leading to processes mediated by the actin cytoskeleton in plants, we initiated cloning and characterization of rho proteins from pea. One rho-related, partial cDNA clone of 167 bp was isolated utilizing a polymerase chain reaction-based cloning strategy, using degenerate primers that correspond to conserved domains within the rho proteins. A full-length cDNA was isolated by screening a pea cDNA library using the 167-bp cDNA as a probe. The Rho1Ps cDNA contains an open reading frame encoding a polypeptide (Rho1Ps) of 197 amino acids that shows 45-64% sequence identity to members of the rho family and about 30% identity to other members of the ras superfamily. In addition to the nucleotide-binding and GTPase domains, Rho1Ps shares conserved residues and motifs unique to the rho proteins. Purified Rho1Ps protein expressed in Escherichia coli retains specific GTP-binding activity. These data indicate that Rho1Ps encodes a small GTP-binding protein of the rho family. The Rho1Ps transcript is expressed in all organs of pea seedlings...

Recognition of RNA Editing Sites Is Directed by Unique Proteins in Chloroplasts: Biochemical Identification of cis-Acting Elements and trans-Acting Factors Involved in RNA Editing in Tobacco and Pea Chloroplasts

Miyamoto, Tetsuya; Obokata, Junichi; Sugiura, Masahiro
Fonte: American Society for Microbiology Publicador: American Society for Microbiology
Tipo: Artigo de Revista Científica
Publicado em /10/2002 EN
Relevância na Pesquisa
26.34%
RNA editing in higher-plant chloroplasts involves C-to-U conversions at specific sites. Although in vivo analyses have been performed, little is known about the biochemical aspects of chloroplast editing reactions. Here we improved our original in vitro system and devised a procedure for preparing active chloroplast extracts not only from tobacco plants but also from pea plants. Using our tobacco in vitro system, cis-acting elements were defined for psbE and petB mRNAs. Distinct proteins were found to bind specifically to each cis-element, a 56-kDa protein to the psbE site and a 70-kDa species to the petB site. Pea chloroplasts lack the corresponding editing site in psbE since T is already present in the DNA. Parallel in vitro analyses with tobacco and pea extracts revealed that the pea plant has no editing activity for psbE mRNAs and lacks the 56-kDa protein, whereas petB mRNAs are edited and the 70-kDa protein is also present. Therefore, coevolution of an editing site and its cognate trans-factor was demonstrated biochemically in psbE mRNA editing between tobacco and pea plants.

Efficient in vitro import of a cytosolic heat shock protein into pea chloroplasts

Lubben, Thomas H.; Keegstra, Kenneth
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /08/1986 EN
Relevância na Pesquisa
26.48%
In order to further our understanding of the targeting of nuclear-encoded proteins into intracellular organelles, we have investigated the import of chimeric precursor proteins into pea chloroplasts. Two different chimeric precursor proteins were produced by in vitro expression of chimeric genes. One chimeric precursor contained the transit peptide of the small subunit of soybean ribulose 1,5-bisphosphate carboxylase and the mature peptide of the same protein from pea. The second contained the same transit peptide plus 13 amino acids of the pea mature peptide fused to a cytosolic heat shock protein. The extent of import and binding of the two chimeric proteins was examined by using quantitative assays and was compared to the import of pea small subunit precursor. Both precursor proteins imported well into pea chloroplasts, although the extent of import observed with the chimeric small-subunit-heat shock precursor was less than that observed with the soybean-pea small subunit precursor. The heat shock protein alone did not import into nor bind to chloroplasts. The binding of both the chimeric small-subunit-heat shock protein and the soybean-pea small subunit precursor to chloroplasts was physiologically significant, as shown by the fact that when chloroplasts with bound precursors were isolated...

Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD

Renganathan, Hemamalini; Vaidyanathan, Hema; Knapinska, Anna; Ramos, Joe W.
Fonte: Portland Press Ltd. Publicador: Portland Press Ltd.
Tipo: Artigo de Revista Científica
EN
Relevância na Pesquisa
26.42%
Cell signalling pathways that regulate proliferation and those that regulate programmed cell death (apoptosis) are co-ordinated. The proteins and mechanisms that mediate the integration of these pathways are not yet fully described. The phosphoprotein PEA-15 (phosphoprotein enriched in astrocytes) can regulate both the ERK (extracellular-signal-regulated kinase)/MAPK (mitogen-activated protein kinase) pathway and the death receptor-initiated apoptosis pathway. This is the result of PEA-15 binding to the ERK/MAPK or the proapoptotic protein FADD (Fas-activated death domain protein) respectively. The mechanism by which binding of PEA-15 to these proteins is controlled has not been elucidated. PEA-15 is a phosphoprotein containing a Ser-104 phosphorylated by protein kinase C and a Ser-116 phosphorylated by CamKII (calcium/calmodulin-dependent protein kinase II) or AKT. Phosphorylation of Ser-104 is implicated in the regulation of glucose metabolism, while phosphorylation at Ser-116 is required for PEA-15 recruitment to the DISC (death-initiation signalling complex). Moreover, PEA-15 must be phosphorylated at Ser-116 to inhibit apoptosis. In the present study, we report that phosphorylation at Ser-104 blocks ERK binding to PEA-15 in vitro and in vivo...

Extracellular Proteins in Pea Root Tip and Border Cell Exudates1[OA]

Wen, Fushi; VanEtten, Hans D.; Tsaprailis, George; Hawes, Martha C.
Fonte: American Society of Plant Biologists Publicador: American Society of Plant Biologists
Tipo: Artigo de Revista Científica
Publicado em /02/2007 EN
Relevância na Pesquisa
26.42%
Newly generated plant tissue is inherently sensitive to infection. Yet, when pea (Pisum sativum) roots are inoculated with the pea pathogen, Nectria haematococca, most newly generated root tips remain uninfected even though most roots develop lesions just behind the tip in the region of elongation. The resistance mechanism is unknown but is correlated spatially with the presence of border cells on the cap periphery. Previously, an array of >100 extracellular proteins was found to be released while border cell separation proceeds. Here we report that protein secretion from pea root caps is induced in correlation with border cell separation. When this root cap secretome was proteolytically degraded during inoculation of pea roots with N. haematococca, the percentage of infected root tips increased from 4% ± 3% to 100%. In control experiments, protease treatment of conidia or roots had no effect on growth and development of the fungus or the plant. A complex of >100 extracellular proteins was confirmed, by multidimensional protein identification technology, to comprise the root cap secretome. In addition to defense-related and signaling enzymes known to be present in the plant apoplast were ribosomal proteins, 14-3-3 proteins, and others typically associated with intracellular localization but recently shown to be extracellular components of microbial biofilms. We conclude that the root cap...

S-Nitrosylated proteins in pea (Pisum sativum L.) leaf peroxisomes: changes under abiotic stress

Ortega-Galisteo, Ana P.; Rodríguez-Serrano, María; Pazmiño, Diana M.; Gupta, Dharmendra K.; Sandalio, Luisa M.; Romero-Puertas, María C.
Fonte: Oxford University Press Publicador: Oxford University Press
Tipo: Artigo de Revista Científica
EN
Relevância na Pesquisa
26.38%
Peroxisomes, single-membrane-bounded organelles with essentially oxidative metabolism, are key in plant responses to abiotic and biotic stresses. Recently, the presence of nitric oxide (NO) described in peroxisomes opened the possibility of new cellular functions, as NO regulates diverse biological processes by directly modifying proteins. However, this mechanism has not yet been analysed in peroxisomes. This study assessed the presence of S-nitrosylation in pea-leaf peroxisomes, purified S-nitrosylated peroxisome proteins by immunoprecipitation, and identified the purified proteins by two different mass-spectrometry techniques (matrix-assisted laser desorption/ionization tandem time-of-flight and two-dimensional nano-liquid chromatography coupled to ion-trap tandem mass spectrometry). Six peroxisomal proteins were identified as putative targets of S-nitrosylation involved in photorespiration, β-oxidation, and reactive oxygen species detoxification. The activity of three of these proteins (catalase, glycolate oxidase, and malate dehydrogenase) is inhibited by NO donors. NO metabolism/S-nitrosylation and peroxisomes were analysed under two different types of abiotic stress, i.e. cadmium and 2,4-dichlorophenoxy acetic acid (2,4-D). Both types of stress reduced NO production in pea plants...

Effect of Arabinogalactan Proteins from the Root Caps of Pea and Brassica napus on Aphanomyces euteiches Zoospore Chemotaxis and Germination12[C][W]

Cannesan, Marc Antoine; Durand, Caroline; Burel, Carole; Gangneux, Christophe; Lerouge, Patrice; Ishii, Tadashi; Laval, Karine; Follet-Gueye, Marie-Laure; Driouich, Azeddine; Vicré-Gibouin, Maïté
Fonte: American Society of Plant Biologists Publicador: American Society of Plant Biologists
Tipo: Artigo de Revista Científica
EN
Relevância na Pesquisa
26.42%
Root tips of many plant species release a number of border, or border-like, cells that are thought to play a major role in the protection of root meristem. However, little is currently known on the structure and function of the cell wall components of such root cells. Here, we investigate the sugar composition of the cell wall of the root cap in two species: pea (Pisum sativum), which makes border cells, and Brassica napus, which makes border-like cells. We find that the cell walls are highly enriched in arabinose and galactose, two major residues of arabinogalactan proteins. We confirm the presence of arabinogalactan protein epitopes on root cap cell walls using immunofluorescence microscopy. We then focused on these proteoglycans by analyzing their carbohydrate moieties, linkages, and electrophoretic characteristics. The data reveal (1) significant structural differences between B. napus and pea root cap arabinogalactan proteins and (2) a cross-link between these proteoglycans and pectic polysaccharides. Finally, we assessed the impact of root cap arabinogalactan proteins on the behavior of zoospores of Aphanomyces euteiches, an oomycetous pathogen of pea roots. We find that although the arabinogalactan proteins of both species induce encystment and prevent germination...

Phosphoprotein enriched in astrocytes (PEA)-15: A potential therapeutic target in multiple disease states

Greig, Fiona H.; Nixon, Graeme F.
Fonte: Pergamon Press Publicador: Pergamon Press
Tipo: Artigo de Revista Científica
Publicado em /09/2014 EN
Relevância na Pesquisa
26.44%
Phosphoprotein enriched in astrocytes-15 (PEA-15) is a cytoplasmic protein that sits at an important junction in intracellular signalling and can regulate diverse cellular processes, such as proliferation and apoptosis, dependent upon stimulation. Regulation of these processes occurs by virtue of the unique interaction of PEA-15 with other signalling proteins. PEA-15 acts as a cytoplasmic tether for the mitogen-activated protein kinases, extracellular signal-regulated kinase 1/2 (ERK1/2) preventing nuclear localisation. In order to release ERK1/2, PEA-15 requires to be phosphorylated via several potential pathways. PEA-15 (and its phosphorylation state) therefore regulates many ERK1/2-dependent processes, including proliferation, via regulating ERK1/2 nuclear translocation. In addition, PEA-15 contains a death effector domain (DED) which allows interaction with other DED-containing proteins. PEA-15 can bind the DED-containing apoptotic adaptor molecule, Fas-associated death domain protein (FADD) which is also dependent on the phosphorylation status of PEA-15. PEA-15 binding of FADD can inhibit apoptosis as bound FADD cannot participate in the assembly of apoptotic signalling complexes. Through these protein–protein interactions, PEA-15-regulated cellular effects have now been investigated in a number of disease-related studies. Changes in PEA-15 expression and regulation have been observed in diabetes mellitus...

Eliminating Anti-Nutritional Plant Food Proteins: The Case of Seed Protease Inhibitors in Pea

Clemente, Alfonso; Arques, Maria C.; Dalmais, Marion; Le Signor, Christine; Chinoy, Catherine; Olias, Raquel; Rayner, Tracey; Isaac, Peter G.; Lawson, David M.; Bendahmane, Abdelhafid; Domoney, Claire
Fonte: Public Library of Science Publicador: Public Library of Science
Tipo: Artigo de Revista Científica
Publicado em 12/08/2015 EN
Relevância na Pesquisa
26.38%
Several classes of seed proteins limit the utilisation of plant proteins in human and farm animal diets, while plant foods have much to offer to the sustainable intensification of food/feed production and to human health. Reduction or removal of these proteins could greatly enhance seed protein quality and various strategies have been used to try to achieve this with limited success. We investigated whether seed protease inhibitor mutations could be exploited to enhance seed quality, availing of induced mutant and natural Pisum germplasm collections to identify mutants, whilst acquiring an understanding of the impact of mutations on activity. A mutant (TILLING) resource developed in Pisum sativum L. (pea) and a large germplasm collection representing Pisum diversity were investigated as sources of mutations that reduce or abolish the activity of the major protease inhibitor (Bowman-Birk) class of seed protein. Of three missense mutations, predicted to affect activity of the mature trypsin / chymotrypsin inhibitor TI1 protein, a C77Y substitution in the mature mutant inhibitor abolished inhibitor activity, consistent with an absolute requirement for the disulphide bond C77-C92 for function in the native inhibitor. Two further classes of mutation (S85F...

Vinyl sulfone silica: application of an open preactivated support to the study of transnitrosylation of plant proteins by S-nitrosoglutathione

Begar?? Morales, Juan Carlos; L??pez Jaramillo, Francisco Javier; S??nchez Calvo, Beatriz; Carreras Enga??a, Alfonso; Ortega Mu??oz, Mariano; Santoyo Gonz??lez, Francisco; Corpas Aguirre, Francisco Javier; Barroso, Juan B.
Fonte: Biomed Central Publicador: Biomed Central
Tipo: Artigo de Revista Científica
ENG
Relevância na Pesquisa
36.02%
Background S-nitrosylaton is implicated in the regulation of numerous signaling pathways with a diversity of regulatory roles. The high lability of the S-NO bond makes the study of proteins regulated by S-nitrosylation/denitrosylation a challenging task and most studies have focused on already S-nitrosylated proteins. We hypothesize that: i) S-nitrosoglutathione (GSNO) transnitrosylation is a feasible mechanism to account for the physiological S-nitrosylation of rather electropositive sulfur atoms from proteins, ii) affinity chromatography is a suitable approach to isolate proteins that are prone to undergo S-transnitrosylation and iii) vinyl sulfone silica is a suitable chromatographic bead.; Results The combination of vinyl sulfone silica with GSNO yielded an affinity resin that withstood high ionic strength without shrinking or deforming and that it was suitable to isolate potential GSNO transnitrosylation target candidates. Fractions eluted at 1500???mM NaCl resulted in a symmetrical peak for both, protein and S-nitrosothiols, supporting the idea of transnitrosylation by GSNO as a selective process that involves strong and specific interactions with the target protein. Proteomic analysis led to the identification of 22 physiological significant enzymes that differ with the tissue analyzed...

Pre-fractionation strategies to resolve pea (Pisum sativum) sub-proteomes

Meisrimler, Claudia-Nicole; Menckhoff, Ljiljana; Kukavica, Biljana M.; Lüthje, Sabine
Fonte: Frontiers Media S.A. Publicador: Frontiers Media S.A.
Tipo: Artigo de Revista Científica
Publicado em 19/10/2015 EN
Relevância na Pesquisa
26.41%
Legumes are important crop plants and pea (Pisum sativum L.) has been investigated as a model with respect to several physiological aspects. The sequencing of the pea genome has not been completed. Therefore, proteomic approaches are currently limited. Nevertheless, the increasing numbers of available EST-databases as well as the high homology of the pea and medicago genome (Medicago truncatula Gaertner) allow the successful identification of proteins. Due to the un-sequenced pea genome, pre-fractionation approaches have been used in pea proteomic surveys in the past. Aside from a number of selective proteome studies on crude extracts and the chloroplast, few studies have targeted other components such as the pea secretome, an important sub-proteome of interest due to its role in abiotic and biotic stress processes. The secretome itself can be further divided into different sub-proteomes (plasma membrane, apoplast, cell wall proteins). Cell fractionation in combination with different gel-electrophoresis, chromatography methods and protein identification by mass spectrometry are important partners to gain insight into pea sub-proteomes, post-translational modifications and protein functions. Overall, pea proteomics needs to link numerous existing physiological and biochemical data to gain further insight into adaptation processes...

Isoelectric-focusing properties and carbohydrate content of pea (Pisum sativum) legumin

Gatehouse, John A.; Croy, Ronald R. D.; Boulter, Donald
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em 01/02/1980 EN
Relevância na Pesquisa
35.99%
Legumin from pea (Pisum sativum) is a molecule made up of six pairs of subunits, each pair consisting of an `acidic' subunit (mol.wt. about 40000) and a `basic' subunit (mol.wt. about 20000) linked by one or more disulphide bonds. The heterogeneity of legumin has been investigated by isoelectric focusing; undissociated legumin could not be focused satisfactorily, but legumin subunits could be analysed under dissociating conditions. 8m-Urea was not found to be a satisfactory medium for isoelectric focusing of legumin, as the `basic' subunits showed a shift in pI with time of incubation in urea. A new dissociating medium for isoelectric focusing, namely 50% (v/v) formamide, was used for analysis of legumin, which gave pI values of 5.0–5.3 for the `acidic' subunits, and 8.3–8.7 for the `basic' subunits. Both types of subunits were shown to be heterogeneous in charge and molecular weight by two-dimensional analysis employing isoelectric focusing in the first dimension and sodium dodecyl sulphate/polyacrylamide gel electrophoresis in the second. The `basic' and `acidic' subunits of legumin were separated on the preparative scale by ion-exchange chromatography in 50% formamide. Carbohydrate attached to the protein was investigated as a possible cause of the heterogeneity of legumin subunits. However...

Increased capacity for sucrose uptake leads to earlier onset of protein accumulation in developing pea seeds

Rosche, Elke; Blackmore, Daniel; Offler, Christina E; Patrick, John W
Fonte: CSIRO Publishing Publicador: CSIRO Publishing
Tipo: Artigo de Revista Científica
Relevância na Pesquisa
36.09%
Pea (Pisum sativum L.) cotyledons, overexpressing a potato sucrose transporter (StSUT1), were used to explore the hypothesis that sucrose stimulates the onset of storage protein biosynthesis. The study focused on the transition between pre-storage and storage phases of seed development. During this period supply of sucrose and hexose to transgenic cotyledons was unaffected by StSUT1 expression. However, protoplasmic levels of sucrose but not hexoses were elevated in transgenic cotyledons. Total protein levels in cotyledons followed the same temporal trend as observed for sucrose and this was reflected in an earlier appearance of protein bodies. Protein levels in wild type and StSUT1 cotyledons were found to lie on the same sucrose dose-response curve and this could be reproduced in vitro when wild type cotyledons were cultured on media containing various sucrose concentrations. Rates of [14C] sucrose uptake and incorporation into polymeric forms were consistent with protoplasmic sucrose supplying a proportion of the carbon skeletons required for storage protein accumulation. In addition, vicilin gene expression was up-regulated earlier in StSUT1 cotyledons. We conclude that sucrose functions both as a signal and fuel to stimulate storage protein accumulation and assembly into protein bodies. An earlier stimulation of storage protein synthesis is considered to largely account for the 14% increase in protein levels of StSUT1 seeds at harvest.

Edible films and coatings for cheese; Filmes e revestimentos comestíveis para queijos

Orosa, Maria Inês Franco
Fonte: Universidade de Aveiro Publicador: Universidade de Aveiro
Tipo: Dissertação de Mestrado
ENG
Relevância na Pesquisa
36.27%
Over the last years there has been an increasing interest to replace synthetic materials by biodegradable ones, due to the ecological problems. Edible and biodegradable films can be produced using polysaccharides, lipids, proteins and composites, and act as a package without damaging the environment. By choosing a suitable coating composition it is possible to preserve several desired properties of a certain food product. Important properties should be considered, such as mechanical, functional and barrier properties. The main goal of this study was to evaluate edible films and coatings from plant proteins (pea, soy), with incorporated natural antimicrobial and antioxidant agents, to potentially protect cheese from physico-chemical and microbial deterioration and to preserve the organoleptic characteristics, especially of sliced cheeses. The work performed focused mainly on the preparation and characterization of pea protein films, with added chitooligosaccharides (COs) (0.5%, 1% and 2%) and two types of essential oils at 1%, bay and thyme oils. Films with 0.5% of COs showed the highest values of Young’s modulus, tensile strength and elongation. Regarding the barrier properties, the film with 1% of COs showed the lower permeability value. Addition of small amounts of COs may be advantageous to improve the mechanical properties of the PPI films...