Comparative proteome analysis of seed storage and allergenic proteins among four narrow-leafed lupin cultivars

Islam, Shahidul; Yan, Guijun; Appels, R.; Ma, Wujun

doi:10.1016/j.foodchem.2012.05.081

Cited by 16 publications

(12 citation statements)

References 42 publications

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“…Therefore, in our experiment we decided to carry out a preliminary fractionation of white lupin seed proteins before separating them by electrophoresis. In a study of narrow-leafed lupin seed proteome, published by Islam et al (2012) , the 2D-electrophorogram comprised mostly of polypeptides similar to β conglutin. On the other hand, in gels with yellow lupin seed proteins 205 β conglutin spots were found among a total of 341 seed protein spots ( Ogura et al, 2014 ).…”

Section: Discussionmentioning

confidence: 99%

Proteins in Relation to Vigor and Viability of White Lupin (Lupinus albus L.) Seed Stored for 26 Years

Dobiesz

Piotrowicz-Cieślak

2017

Front. Plant Sci.

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The aim of the study was to evaluate the vigor and viability as well as to determine and compare the contents of selected protein fractions of white lupin (Lupinus albus L.) seeds stored for 26 years at temperatures of -14°C and +20°C. The seeds stored at -14°C germinated in 86.3%, while the seeds stored at +20°C did not germinate at all. The viability evaluation was confirmed by the measuring electroconductivity of seed exudates. In seeds stored at -14°C the contents of γ, δ, and β conglutin were 14, 4 and 69 mg g-1 fresh mass, respectively, while in seed stored at +20°C they were 15.5, 3, 65 mg g-1 fresh mass, respectively. One-dimensional electrophoresis of γ and δ conglutin fractions indicated the presence of several intense polypeptide bands with molecular weights from 23.0 to 10.3 kDa. Polypeptide bands with a molecular weight of 22.4 and 19.8 kDa exhibited almost two times higher expression in the seeds stored at -14°C compared to the seeds stored at +20°C. Electrophoresis revealed 310 protein spots on the maps generated for seeds stored at -14°C, and 228 spots for seeds stored at +20°C. In seeds stored at +20°C most polypeptide subunits had a pI ranging from 4.5 to 7 and a molecular weight of 10–97 kDa. The greatest differences in the contents of polypeptides between the analyzed variants was observed within the range of 20–45 kDa (-14°C: 175, +20°C: 115 protein spots) and within the range of 65–97 kDa (-14°C: 103, +20°C: 75 protein spots). In seeds stored at +20°C, a clear decline in basic (8–10 pI) polypeptides was observed. The study demonstrated that the polypeptides identified as γ and δ conglutins are probably closely related to vigor and viability of seeds.

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Section: Discussionmentioning

confidence: 99%

Proteins in Relation to Vigor and Viability of White Lupin (Lupinus albus L.) Seed Stored for 26 Years

Dobiesz

Piotrowicz-Cieślak

2017

Front. Plant Sci.

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“…Islam et al 18 studied proteome of seed storage proteins among four L. angustifolius cultivars. The reported results indicate that the main proteins differentially expressed in studied seeds were identified as -conglutin, whereas most of -, -and -conglutins showed a similar expression pattern among the cultivars.…”

Section: Proteomic Analysis Of Lupin Seed Proteinsmentioning

confidence: 99%

“…The reported results indicate that the main proteins differentially expressed in studied seeds were identified as -conglutin, whereas most of -, -and -conglutins showed a similar expression pattern among the cultivars. 18 The lupin seed proteomic studies typically involved seeds other than those of the L. luteus. Recently, Ogura et al 19 carried out a detailed proteomic characterisation of L. luteus seeds proteins.…”

Section: Proteomic Analysis Of Lupin Seed Proteinsmentioning

confidence: 99%

Proteomic analysis of Lupinus angustifolius (var. Zeus and Bojar) and Lupinus luteus (var. Lord and Parys) seed proteins and their hydrolysates

et al. 2017

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The results of the present study provide insight into the nature of the digestion process that may take place after lupin seed protein intake and highlight the important fact that some of the proteins are insensitive to digestive enzyme activity. Moreover, evaluation of digestion activity of trypsin towards lupin seed proteins may be used for the development of specific processes with respect to hypoallergenic food production. © 2017 Society of Chemical Industry.

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“…The digests, which were then treated or not with N-glycosidase PNGase A or PNGase F, before being analyzed by LC-Orbitrap MS, where MS survey scans were followed by "data-dependent" MS2 or targeted MSn mode. Of the two partially "overlapping" potential N-glycosylation sites in γconglutin, Asn 131 and Asn 132→36 , the N-glycan was proven to reside on Asn 131 , which corresponded to the glycosylation site that was predicted using ANTHEPROT software (Table 1; Yorrel) distributed in different groups, and performed a comprehensive proteome analysis of mature seeds using 2D IEF/SDS-PAGE followed by mass spectrometric peptide sequencing [113]. They reported differences in abundance between cultivars for 24.3% of the spots, among which 20.6%…”

Section: Seed Proteomics Of Lupin Domestic Speciesmentioning

confidence: 99%

Proteomics for exploiting diversity of lupin seed storage proteins and their use as nutraceuticals for health and welfare

Cabello‐Hurtado

Keller

Ley

et al. 2016

Journal of Proteomics

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Some important topics concerning storage proteins from lupin seeds are presented and analyzed in an integrated way in this review. Proteomic approaches have been essential in characterizing lupin seed protein diversity, which goes far beyond gene diversity since the protein level adds to the latter differential proteolytic cleavage of conglutin pro-proteins and a diverse array of glycosylation forms and sites. Proteomics has also proved helpful for screening and studying Lupinus germplasm with the future aim of exploiting and improving food production, quality, and nutritional values.

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Comparative proteome analysis of seed storage and allergenic proteins among four narrow-leafed lupin cultivars

Cited by 16 publications

References 42 publications

Proteins in Relation to Vigor and Viability of White Lupin (Lupinus albus L.) Seed Stored for 26 Years

Proteins in Relation to Vigor and Viability of White Lupin (Lupinus albus L.) Seed Stored for 26 Years

Proteomic analysis of Lupinus angustifolius (var. Zeus and Bojar) and Lupinus luteus (var. Lord and Parys) seed proteins and their hydrolysates

Proteomics for exploiting diversity of lupin seed storage proteins and their use as nutraceuticals for health and welfare

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