Matches in SemOpenAlex for { <https://semopenalex.org/work/W1982546593> ?p ?o ?g. }
Showing items 1 to 93 of
93
with 100 items per page.
- W1982546593 endingPage "283" @default.
- W1982546593 startingPage "283" @default.
- W1982546593 abstract "Study of heat denaturation of major whey proteins (beta-lactoglobulin or alpha-lactalbumin) either in separated purified forms, or in forms present in fresh industrial whey or in recomposed mixture respecting whey proportions, indicated significant differences in their denaturation depending on pH, temperature of heating, presence or absence of other codenaturation partner, and of existence of a previous thermal pretreatment (industrial whey). alpha-Lactalbumin, usually resistant to tryptic hydrolysis, aggregated after heating at > or = 85 degrees C. After its denaturation, alpha-lactalbumin was susceptible to tryptic hydrolysis probably because of exposure of its previously hidden tryptic cleavage sites (Lys-X and Arg-X bonds). Heating over 85 degrees C of beta-lactoglobulin increased its aggregation and exposure of its peptic cleavage sites. The co-denaturation of alpha-lactalbumin with beta-lactoglobulin increased their aggregation and resulted in complete exposure of beta-lactoglobulin peptic cleavage sites and partial unveiling of alpha-lactalbumin tryptic cleavage sites. The exposure of alpha-lactalbumin tryptic cleavage sites was slightly enhanced when the alpha-lactalbumin/beta-lactoglobulin mixture was heated at pH 7.5. Co-denaturation of fresh whey by heating at 95 degrees C and pH 4.5 and above produced aggregates stabilized mostly by covalent disulfide bonds easily reduced by beta-mercaptoethanol. The aggregates stabilized by covalent bonds other than disulfide arose from a same thermal treatment but performed at pH 3.5. Thermal treatment of whey at pH 7.5 considerably enhanced tryptic and peptic hydrolysis of both major proteins." @default.
- W1982546593 created "2016-06-24" @default.
- W1982546593 creator A5020091726 @default.
- W1982546593 creator A5038633972 @default.
- W1982546593 creator A5047512281 @default.
- W1982546593 creator A5075868496 @default.
- W1982546593 creator A5078884564 @default.
- W1982546593 date "2002-07-01" @default.
- W1982546593 modified "2023-10-17" @default.
- W1982546593 title "Thermal modifications of structure and codenaturation of α-lactalbumin and β-lactoglobulin induce changes of solubility and susceptibility to proteases" @default.
- W1982546593 doi "https://doi.org/10.1002/1521-3803(20020701)46:4<283::aid-food283>3.0.co;2-a" @default.
- W1982546593 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12224426" @default.
- W1982546593 hasPublicationYear "2002" @default.
- W1982546593 type Work @default.
- W1982546593 sameAs 1982546593 @default.
- W1982546593 citedByCount "54" @default.
- W1982546593 countsByYear W19825465932012 @default.
- W1982546593 countsByYear W19825465932013 @default.
- W1982546593 countsByYear W19825465932014 @default.
- W1982546593 countsByYear W19825465932015 @default.
- W1982546593 countsByYear W19825465932016 @default.
- W1982546593 countsByYear W19825465932017 @default.
- W1982546593 countsByYear W19825465932018 @default.
- W1982546593 countsByYear W19825465932020 @default.
- W1982546593 countsByYear W19825465932021 @default.
- W1982546593 countsByYear W19825465932022 @default.
- W1982546593 countsByYear W19825465932023 @default.
- W1982546593 crossrefType "journal-article" @default.
- W1982546593 hasAuthorship W1982546593A5020091726 @default.
- W1982546593 hasAuthorship W1982546593A5038633972 @default.
- W1982546593 hasAuthorship W1982546593A5047512281 @default.
- W1982546593 hasAuthorship W1982546593A5075868496 @default.
- W1982546593 hasAuthorship W1982546593A5078884564 @default.
- W1982546593 hasConcept C127413603 @default.
- W1982546593 hasConcept C13965031 @default.
- W1982546593 hasConcept C155574463 @default.
- W1982546593 hasConcept C175156509 @default.
- W1982546593 hasConcept C178617795 @default.
- W1982546593 hasConcept C178790620 @default.
- W1982546593 hasConcept C180577832 @default.
- W1982546593 hasConcept C181199279 @default.
- W1982546593 hasConcept C182220744 @default.
- W1982546593 hasConcept C185592680 @default.
- W1982546593 hasConcept C187320778 @default.
- W1982546593 hasConcept C2776923230 @default.
- W1982546593 hasConcept C2777897731 @default.
- W1982546593 hasConcept C2780124430 @default.
- W1982546593 hasConcept C43369102 @default.
- W1982546593 hasConcept C43617362 @default.
- W1982546593 hasConcept C55493867 @default.
- W1982546593 hasConcept C68863886 @default.
- W1982546593 hasConcept C94412978 @default.
- W1982546593 hasConceptScore W1982546593C127413603 @default.
- W1982546593 hasConceptScore W1982546593C13965031 @default.
- W1982546593 hasConceptScore W1982546593C155574463 @default.
- W1982546593 hasConceptScore W1982546593C175156509 @default.
- W1982546593 hasConceptScore W1982546593C178617795 @default.
- W1982546593 hasConceptScore W1982546593C178790620 @default.
- W1982546593 hasConceptScore W1982546593C180577832 @default.
- W1982546593 hasConceptScore W1982546593C181199279 @default.
- W1982546593 hasConceptScore W1982546593C182220744 @default.
- W1982546593 hasConceptScore W1982546593C185592680 @default.
- W1982546593 hasConceptScore W1982546593C187320778 @default.
- W1982546593 hasConceptScore W1982546593C2776923230 @default.
- W1982546593 hasConceptScore W1982546593C2777897731 @default.
- W1982546593 hasConceptScore W1982546593C2780124430 @default.
- W1982546593 hasConceptScore W1982546593C43369102 @default.
- W1982546593 hasConceptScore W1982546593C43617362 @default.
- W1982546593 hasConceptScore W1982546593C55493867 @default.
- W1982546593 hasConceptScore W1982546593C68863886 @default.
- W1982546593 hasConceptScore W1982546593C94412978 @default.
- W1982546593 hasIssue "4" @default.
- W1982546593 hasLocation W19825465931 @default.
- W1982546593 hasLocation W19825465932 @default.
- W1982546593 hasOpenAccess W1982546593 @default.
- W1982546593 hasPrimaryLocation W19825465931 @default.
- W1982546593 hasRelatedWork W1982546593 @default.
- W1982546593 hasRelatedWork W2016377423 @default.
- W1982546593 hasRelatedWork W2018366523 @default.
- W1982546593 hasRelatedWork W2026049228 @default.
- W1982546593 hasRelatedWork W2123456504 @default.
- W1982546593 hasRelatedWork W2405405747 @default.
- W1982546593 hasRelatedWork W2774452498 @default.
- W1982546593 hasRelatedWork W4385157041 @default.
- W1982546593 hasRelatedWork W2185699682 @default.
- W1982546593 hasRelatedWork W2254905552 @default.
- W1982546593 hasVolume "46" @default.
- W1982546593 isParatext "false" @default.
- W1982546593 isRetracted "false" @default.
- W1982546593 magId "1982546593" @default.
- W1982546593 workType "article" @default.