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

Czubiński, Jarosław; Montowska, Magdalena; Pośpiech, E.; Lampart‐Szczapa, E.

doi:10.1002/jsfa.8436

Cited by 11 publications

(3 citation statements)

References 25 publications

(80 reference statements)

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“…The reasons for such result of mass spectrometry identification may be related to the lack of available sequence for L. albus LEA proteins and the fact of a very high degree of homology of protein within the two of the analyzed lupin species. The similar situation was noted while proteomic analysis was used for characterization of proteins from L. luteus seeds . In this case L. luteus proteins spots separated by two‐dimensional electrophoresis were identified as L. angustifolius proteins.…”

Section: Resultssupporting

confidence: 53%

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Lupin seeds storage protein composition and their interactions with native flavonoids

Czubiński

Feder

2019

J Sci Food Agric

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BACKGROUND Lupin‐based food, due to the high content of functional proteins and phenolic compounds, are widely used in human nutrition. Unfortunately, proteins and phenolic compounds can easily interact with each other which results in formation of complexes that affect properties of both components. Therefore, in this study, composition of the seeds storage proteins isolated from Lupinus albus and L. angustifolius and their interactions with native flavonoids were investigated. RESULTS Based on the chromatographic separations, six proteins fractions of lupin seeds storage proteins were identified. The results indicate that two dominant fractions, α‐conglutin and β‐conglutin, constitute up to 80% of all proteins present in the seeds. Three flavonoids interacting with the proteins were identified as apigenin C‐glycosides. The lowest flavonoids content was noted in the main storage proteins while in both lupin seeds species over 90% of flavonoids interacted with the proteins present in late‐embryogenesis abundant (LEA) protein fraction. CONCLUSIONS Protein–phenolic compound complexes can affect the digestibility of proteins and bioavailability of phenolic compounds, and thus the functional and nutritional properties of products derived from lupin seeds can be changed. Therefore, a better understanding of factors affecting the nutritional value of lupin seeds proteins and flavonoids is necessary to optimize the biological use of this plant for human nutrition. © 2019 Society of Chemical Industry

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Section: Resultssupporting

confidence: 53%

“…The similar situation was noted while proteomic analysis was used for characterization of proteins from L. luteus seeds. 30 In this case L. luteus proteins spots separated by two-dimensional electrophoresis were identified as L. angustifolius proteins.…”

Section: Lupin Seed Proteins Composition and Identificationmentioning

confidence: 96%

Lupin seeds storage protein composition and their interactions with native flavonoids

Czubiński

Feder

2019

J Sci Food Agric

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“…However, the influences of enzymatic hydrolysis on lupin proteins have only scarcely been investigated up to now. Few studies on lupin proteins targeted either change in their technofunctional properties after enzymatic treatment or the reduction of their allergenic potential (Czubinski, Montowska, Pospiech, & Lampart‐Szczapa, ; Lqari et al, ; Raymundo, Empis, & Sousa, ). Sormus de Castro Pinto, Neves, and Machado de Medeiros () estimated the decrease in antigenic activity of the globulins of lupin due to enzymatic hydrolysis with pepsin and trypsin, while Álvarez‐Álvarez et al () studied the allergen characterization of lupin seeds after different boiling treatments.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic hydrolysis of lupin protein isolates—Changes in the molecular weight distribution, technofunctional characteristics, and sensory attributes

Schlegel

Sontheimer

Hickisch

et al. 2019

Food Science & Nutrition

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Enzymatic hydrolysis of lupin protein isolates (LPI; Lupinus angustifolius L.) was performed with nine different protease preparations to investigate their effect on technofunctionality, sensory properties, and the integrity of the proteins to estimate the reduction of the immunoreactivity. Alcalase 2.4 L, papain, and pepsin were most effective in the degradation of the α‐ and β‐conglutin examined by SDS–PAGE analysis, although the degree of hydrolysis only slightly increased. The technofunctional properties of LPI—solubility, emulsifying, and foaming activity—were improved by most of the proteolytic enzymes with the most impressive increase from 980% foam activity for LPI up to 3,614% foam activity for pepsin hydrolysate. The formation of bitterness, most likely linked to generation of bitter peptides, was pronounced in the Alcalase hydrolysate, while the other hydrolysates did not show an extensive increase in bitterness compared to the LPI. Other sensory attributes of the hydrolysates—with the exception of Alcalase treatment—were also very similar to the LPI. The results of this study show the potential of enzymatic degradation of LPI to modify the IgE‐reacting polypeptides and to improve the technofunctionality of the isolates and therefore their use as food ingredients.

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Lupinus angustifolius L. lactofermentation and protein isolation: effects on phenolic compounds and genistein, antioxidant properties, trypsin inhibitor activity, and protein digestibility

Bartkienė

Šakienė

Bartkevičs

et al. 2018

Eur Food Res Technol

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

Cited by 11 publications

References 25 publications

Lupin seeds storage protein composition and their interactions with native flavonoids

Lupin seeds storage protein composition and their interactions with native flavonoids

Enzymatic hydrolysis of lupin protein isolates—Changes in the molecular weight distribution, technofunctional characteristics, and sensory attributes

Lupinus angustifolius L. lactofermentation and protein isolation: effects on phenolic compounds and genistein, antioxidant properties, trypsin inhibitor activity, and protein digestibility

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