Restricted proteolysis of legumin of broad beans: Effect on thermodynamic properties of aqueous solutions and interaction with ficoll

Danilenko, A. N.; Vetrov, V. Yu.; Dmitrochenko, A. P.; Leontiev, A.L.; Braudo, E. E.; Tolstoguzov, V. B.

doi:10.1002/food.19920360202

Cited by 12 publications

(3 citation statements)

References 12 publications

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“…Limited tryptic hydrolysis of 11 S globulins results in the splitting of the surface-exposed regions of a-chains, while the b-chains located in the inner part of the protein molecules remains intact [60][61][62]. The loss of hydrophilic peptides leads to the reduction of the molecular mass from 350-360 kDa to 230 kDa in soybean glycinin [63], 240-250 kDa in faba bean legumin [64,65] and 260-270 kDa in pea legumin [66].…”

Section: Modification Of the 11 S Globulins By Limited Proteolysismentioning

confidence: 99%

Reflections about the functional potential of legume proteins A Review

Schwenke¹

2001

Nahrung

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The term "functional potential" was introduced to better approach to the understanding of the relationships between the structure and the functional properties of food proteins. Although in practice the complex of structural features of a protein contributes to its functionality, it is very useful to regard the functional potential of the protein surface on the one side and to look on special effects of protein conformation (role of compact or unfolded state) on the functionality on the other side. This point of view may help to design the best strategy of modification of the protein structure and functionality. The special situation of the oligomeric legume storage protein, i.e. legumin-like 11 S globulins and vicilin-like 7 S globulin, and the structural and functional modification of 11 S globulin by limited tryptic hydrolysis and by acylation are discussed in this paper.

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Section: Modification Of the 11 S Globulins By Limited Proteolysismentioning

confidence: 99%

Reflections about the functional potential of legume proteins A Review

Schwenke¹

2001

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“…1 confirms our finding that the tryptic modified legumin is more hydrophobic than the parent protein [l 1, 281. However, the finding of another group [9] that tryptically nicked legumin had an increased hydrophilicity, which was concluded from its higher affinity to ficoll in aqueous solution, demands more profound reflections about the term "hydrophobicity".…”

Section: Discussionmentioning

confidence: 92%

Legumin‐T from faba bean legumin: Isolation, partial characterization and surface functional properties

Schwenke

Staatz

Dudek

et al. 1995

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SummaryLegumin-T was prepared by limited tryptic hydrolysis of legumin from faba beans (Viciu faba L.) and was chromatographically purified. It is composed of two principle subunits consisting each of an intact P-polypeptide chain and a nicked a-chain of legumin besides minor polypeptides. The molecular mass was (250 f 11) kDa estimated by gel chromatography. Amino acid analysis showed that the transformation of legumin to legumin-T resulted in a loss of polar amino acids and an increase of non-polar hydrophobic amino acids. The time-dependent surface tension and the surface compressions isotherms showed a rather similar behavior of legumin and legumin-T. The calculated ratio of the surface areas A / A o revealed, however, difference between both proteins (legumin: A / A , = 1, legurnin-T: A / A o < 1) pointing to an irreversible desorption of legumin-T from the surface due to compression. The emulsifying activity of legumin-T was higher than that of the parent legumin. ZusamrnenfassungLegumin-T aus Ackerbohnen: Isolierung, teilweise Charakterisierung und Grenzflachenfunktionalitlt Legurnin-T wurde durch begrenzte tryptische Hydrolyse von Legumin aus Ackerbohnen (Viciafaba L.) gewonnen und gelchromatographisch gereinigt. Es besteht aus zwei verschiedenen UntereinheitenTypen, die aus je einem Fragment der Legumin-a-Ketten und einer intakten P-Kette sowie tryptischen Spaltpeptiden zusammengesetzt sind. Die gelchrornatographisch bestimmte Molmasse betragt (250 1 I ) kDa. Die Aniinosaurezusammensetzung des Legumin-T ist durch eine Erniedrigung des Anteils polarer und eine Erhohung des Anteils uupolarer hydrophober Aminosluren gekennzeichnet. Beide Proteine ergaben iihnliche Werte bei der Messung des zeitlichen Verlaufs der Grenzflachenspannung und der Aufnahme der Kompressionsisothermen. Der fur Legumin-T erhaltene geringere Wert fur das Verhaltnis der bedeckten Grenzflachen A / A , (Legumin = 1, Legumin-T < I ) weist jedoch auf irreversible Desorptionsprozesse der Molekiile des modifizierten Proteins an der GrenzflIche hin. Die Emulgieraktivitat von Legumin-T war hoher als diejenige des nativen Legumins.

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“…This was shown by limited trypsin proteolysis of the 11S broad bean globulin in concentrated biphasic mixtures with Ficoll. After a short (10‐min) incubation the biphasic mixed solution is converted into a single‐phase state due to a modification of the protein, where the molecule loses the least ordered segment, preserves conformational stability and becomes more compact and hydrophilic [10, 17]. This could contribute to activation of protoenzymes by cleavage, like that of inactive forms of many enzymes, e.g.…”

Section: Compatibility Control In Biological Systemsmentioning

confidence: 99%

Origins of globular structure in proteins

Tolstoguzov

1999

FEBS Letters

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Thermodynamic incompatibility of polymers in a common solvent is possibly a driving force for formation and evolution of globular protein structures. Folding of polypeptide chains leads to a decrease in both excluded volume of molecules and chemical differences between surfaces of globular molecules with chemical information hidden in the hydrophobic interior. Folding of polypeptide chains results in`molecular or thermodynamic mimicry' of globular proteins and in at least more than 10-fold higher phase separation threshold values of mixed protein solutions compared to those of classical polymers. Unusually high co-solubility might be necessary for efficient biological functioning of proteins, e.g. enzymes, enzyme inhibitors, etc.z 1999 Federation of European Biochemical Societies.

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Restricted proteolysis of legumin of broad beans: Effect on thermodynamic properties of aqueous solutions and interaction with ficoll

Cited by 12 publications

References 12 publications

Reflections about the functional potential of legume proteins A Review

Reflections about the functional potential of legume proteins A Review

Legumin‐T from faba bean legumin: Isolation, partial characterization and surface functional properties

Origins of globular structure in proteins

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