Zobraziť v EDS

Unravelling the dominant role of phosphorylation degree in governing the functionality of reassembled casein micelles: Implications for future dairy production through precision fermentation

Uložené v:
Podrobná bibliografia
Názov: Unravelling the dominant role of phosphorylation degree in governing the functionality of reassembled casein micelles: Implications for future dairy production through precision fermentation
Autori: Che, Jing, Fan, Zekun, Bijl, Etske, Thomsen, Julia Prangchat Stub, Mijakovic, Ivan, 1975, Hettinga, Kasper, Poulsen, Nina Aagaard, Larsen, Lotte Bach
Zdroj: Är Bacillus subtilis PtkA reglerad som ett "cyclin-dependant" kinas? Food Hydrocolloids. 159
Predmety: Acid-induced gelation, TEM, Calcium-binding ability, Reassembled casein micelles, Dephosphorylation
Popis: This study investigated the effect of bovine casein (CN) phosphorylation degree on micelle reassembly, stability, calcium-binding, and acid-induced gelation or precipitation, with the aim of assessing the feasibility of utilising microbial CNs in future dairy production. The four CNs (αS1-, αS2-, β-, and κ-CN) were purified from bovine milk and subjected to enzymatic dephosphorylation, resulting in three pools – fully and partially phosphorylated and fully dephosphorylated. Nine reassembled CN micelle solutions (RCMS) were investigated, consisting of three systems (two of four-CN, and one of β/κ-CN) and three phosphorylation degrees of the corresponding CNs. The distribution of different components (protein, calcium, and phosphorus) into micellar, serum, and insoluble fractions after two centrifugation steps was studied. The pH stability relative to acid-gelation or precipitation of the formed RCMS was further investigated. Results showed that the micelle reassembly ability of RCMS containing all four CNs was proportional to the phosphorylation degree; CNs with higher phosphorylation degrees contained a higher proportion of micelles and exhibited greater calcium-binding ability, whereas fully dephosphorylated CNs hardly formed CN micelle structures. The gelation pH of RCMS increased with decreasing phosphorylation degree, whereas the fully dephosphorylated CNs completely failed in gelation but precipitated when reaching their isoelectric point at pH 5.5. Moreover, RCMS containing only β/κ-CN at their native full phosphorylation were unstable at the salt concentrations applied, with more than half of the CNs self-associating to flocculate. Our study confirms the essential role of phosphorylation degree in micelle reassembly and stability, providing important information for potential future applications of microbial CNs that are expected to exhibit non-native phosphorylation levels.
Popis súboru: electronic
Prístupová URL adresa: https://research.chalmers.se/publication/542841
https://research.chalmers.se/publication/542841/file/542841_Fulltext.pdf
Databáza: SwePub
FullText Text:
  Availability: 0
CustomLinks:
  – Url: https://research.chalmers.se/publication/542841#
    Name: EDS - SwePub (s4221598)
    Category: fullText
    Text: View record in SwePub
  – Url: https://resolver.ebscohost.com/openurl?sid=EBSCO:edsswe&genre=article&issn=0268005X&ISBN=&volume=159&issue=&date=20250101&spage=&pages=&title=Är Bacillus subtilis PtkA reglerad som ett "cyclin-dependant" kinas? Food Hydrocolloids&atitle=Unravelling%20the%20dominant%20role%20of%20phosphorylation%20degree%20in%20governing%20the%20functionality%20of%20reassembled%20casein%20micelles%3A%20Implications%20for%20future%20dairy%20production%20through%20precision%20fermentation&aulast=Che%2C%20Jing&id=DOI:10.1016/j.foodhyd.2024.110615
    Name: Full Text Finder
    Category: fullText
    Text: Full Text Finder
    Icon: https://imageserver.ebscohost.com/branding/images/FTF.gif
    MouseOverText: Full Text Finder
  – Url: https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=EBSCO&SrcAuth=EBSCO&DestApp=WOS&ServiceName=TransferToWoS&DestLinkType=GeneralSearchSummary&Func=Links&author=Che%20J
    Name: ISI
    Category: fullText
    Text: Nájsť tento článok vo Web of Science
    Icon: https://imagesrvr.epnet.com/ls/20docs.gif
    MouseOverText: Nájsť tento článok vo Web of Science
Header DbId: edsswe
DbLabel: SwePub
An: edsswe.oai.research.chalmers.se.8c8cf127.11da.4184.b047.863642a23cde
RelevancyScore: 1065
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 1064.736328125
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: Unravelling the dominant role of phosphorylation degree in governing the functionality of reassembled casein micelles: Implications for future dairy production through precision fermentation
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AR" term="%22Che%2C+Jing%22">Che, Jing</searchLink><br /><searchLink fieldCode="AR" term="%22Fan%2C+Zekun%22">Fan, Zekun</searchLink><br /><searchLink fieldCode="AR" term="%22Bijl%2C+Etske%22">Bijl, Etske</searchLink><br /><searchLink fieldCode="AR" term="%22Thomsen%2C+Julia+Prangchat+Stub%22">Thomsen, Julia Prangchat Stub</searchLink><br /><searchLink fieldCode="AR" term="%22Mijakovic%2C+Ivan%22">Mijakovic, Ivan</searchLink>, 1975<br /><searchLink fieldCode="AR" term="%22Hettinga%2C+Kasper%22">Hettinga, Kasper</searchLink><br /><searchLink fieldCode="AR" term="%22Poulsen%2C+Nina+Aagaard%22">Poulsen, Nina Aagaard</searchLink><br /><searchLink fieldCode="AR" term="%22Larsen%2C+Lotte+Bach%22">Larsen, Lotte Bach</searchLink>
– Name: TitleSource
  Label: Source
  Group: Src
  Data: <i>Är Bacillus subtilis PtkA reglerad som ett "cyclin-dependant" kinas? Food Hydrocolloids</i>. 159
– Name: Subject
  Label: Subject Terms
  Group: Su
  Data: <searchLink fieldCode="DE" term="%22Acid-induced+gelation%22">Acid-induced gelation</searchLink><br /><searchLink fieldCode="DE" term="%22TEM%22">TEM</searchLink><br /><searchLink fieldCode="DE" term="%22Calcium-binding+ability%22">Calcium-binding ability</searchLink><br /><searchLink fieldCode="DE" term="%22Reassembled+casein+micelles%22">Reassembled casein micelles</searchLink><br /><searchLink fieldCode="DE" term="%22Dephosphorylation%22">Dephosphorylation</searchLink>
– Name: Abstract
  Label: Description
  Group: Ab
  Data: This study investigated the effect of bovine casein (CN) phosphorylation degree on micelle reassembly, stability, calcium-binding, and acid-induced gelation or precipitation, with the aim of assessing the feasibility of utilising microbial CNs in future dairy production. The four CNs (αS1-, αS2-, β-, and κ-CN) were purified from bovine milk and subjected to enzymatic dephosphorylation, resulting in three pools – fully and partially phosphorylated and fully dephosphorylated. Nine reassembled CN micelle solutions (RCMS) were investigated, consisting of three systems (two of four-CN, and one of β/κ-CN) and three phosphorylation degrees of the corresponding CNs. The distribution of different components (protein, calcium, and phosphorus) into micellar, serum, and insoluble fractions after two centrifugation steps was studied. The pH stability relative to acid-gelation or precipitation of the formed RCMS was further investigated. Results showed that the micelle reassembly ability of RCMS containing all four CNs was proportional to the phosphorylation degree; CNs with higher phosphorylation degrees contained a higher proportion of micelles and exhibited greater calcium-binding ability, whereas fully dephosphorylated CNs hardly formed CN micelle structures. The gelation pH of RCMS increased with decreasing phosphorylation degree, whereas the fully dephosphorylated CNs completely failed in gelation but precipitated when reaching their isoelectric point at pH 5.5. Moreover, RCMS containing only β/κ-CN at their native full phosphorylation were unstable at the salt concentrations applied, with more than half of the CNs self-associating to flocculate. Our study confirms the essential role of phosphorylation degree in micelle reassembly and stability, providing important information for potential future applications of microbial CNs that are expected to exhibit non-native phosphorylation levels.
– Name: Format
  Label: File Description
  Group: SrcInfo
  Data: electronic
– Name: URL
  Label: Access URL
  Group: URL
  Data: <link linkTarget="URL" linkTerm="https://research.chalmers.se/publication/542841" linkWindow="_blank">https://research.chalmers.se/publication/542841</link><br /><link linkTarget="URL" linkTerm="https://research.chalmers.se/publication/542841/file/542841_Fulltext.pdf" linkWindow="_blank">https://research.chalmers.se/publication/542841/file/542841_Fulltext.pdf</link>
PLink https://erproxy.cvtisr.sk/sfx/access?url=https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=edsswe&AN=edsswe.oai.research.chalmers.se.8c8cf127.11da.4184.b047.863642a23cde
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1016/j.foodhyd.2024.110615
    Languages:
      – Text: English
    Subjects:
      – SubjectFull: Acid-induced gelation
        Type: general
      – SubjectFull: TEM
        Type: general
      – SubjectFull: Calcium-binding ability
        Type: general
      – SubjectFull: Reassembled casein micelles
        Type: general
      – SubjectFull: Dephosphorylation
        Type: general
    Titles:
      – TitleFull: Unravelling the dominant role of phosphorylation degree in governing the functionality of reassembled casein micelles: Implications for future dairy production through precision fermentation
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Che, Jing
      – PersonEntity:
          Name:
            NameFull: Fan, Zekun
      – PersonEntity:
          Name:
            NameFull: Bijl, Etske
      – PersonEntity:
          Name:
            NameFull: Thomsen, Julia Prangchat Stub
      – PersonEntity:
          Name:
            NameFull: Mijakovic, Ivan
      – PersonEntity:
          Name:
            NameFull: Hettinga, Kasper
      – PersonEntity:
          Name:
            NameFull: Poulsen, Nina Aagaard
      – PersonEntity:
          Name:
            NameFull: Larsen, Lotte Bach
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 01
              M: 01
              Type: published
              Y: 2025
          Identifiers:
            – Type: issn-print
              Value: 0268005X
            – Type: issn-locals
              Value: SWEPUB_FREE
            – Type: issn-locals
              Value: CTH_SWEPUB
          Numbering:
            – Type: volume
              Value: 159
          Titles:
            – TitleFull: Är Bacillus subtilis PtkA reglerad som ett "cyclin-dependant" kinas? Food Hydrocolloids
              Type: main
ResultId 1