View in EDS

Protein bioaccessibility from mycoprotein hyphal structure: In vitro investigation of underlying mechanisms.

Saved in:
Bibliographic Details
Title: Protein bioaccessibility from mycoprotein hyphal structure: In vitro investigation of underlying mechanisms.
Authors: Colosimo, Raffaele1 (AUTHOR) raffaele.colosimo@quadram.ac.uk, Warren, Frederick J.1 (AUTHOR) fred.warren@quadram.ac.uk, Finnigan, Tim J.A.2 (AUTHOR), Wilde, Peter J.1 (AUTHOR) peter.wilde@quadram.ac.uk
Source: Food Chemistry. Nov2020, Vol. 330, pN.PAG-N.PAG. 1p.
Subjects: Proteins, Light scattering, Fungal cell walls, Filamentous fungi
Abstract: • Mycoprotein cell walls are highly resilient to mechanical/physical processing and digestion. • Intestinal proteases are the main factors controlling protein bioaccessibility from mycoprotein products. • Diffusion of proteases through the cell wall is the proposed mechanism which facilitates the high protein bioavailability. • An optimal ratio of mycoprotein to enzymes is crucial for protein release. Mycoprotein is a food ingredient from filamentous fungi rich in protein and fibre. This study investigated the protein bioaccessibility from the fungal cells by colourimetric assays in different mycoprotein formulations, following extraction methods and in vitro gastrointestinal digestion. The methods effects were further analysed by static laser light scattering, SDS-PAGE and optical-fluorescence microscopy. The extraction methods released a comparable proportion of protein (30 wt%) independent of sample concentration (10 wt% and 25 wt%), whereas the simulated digestions endpoints released a higher proportion of protein from the less concentrated (46 wt%). Furthermore, mechanical/physical processing had only a minor impact. Intestinal proteases promoted the most efficient protein release but without causing any apparent damage to the cell walls when viewed by microscopy. This suggested that the enzymes can diffuse through the cell walls, due to its porosity/permeability, and are the main factors responsible for the hydrolysis and bioaccessibility of protein from mycoprotein. [ABSTRACT FROM AUTHOR]
Copyright of Food Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
FullText Text:
  Availability: 0
Header DbId: egs
DbLabel: Engineering Source
An: 144671081
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: Protein bioaccessibility from mycoprotein hyphal structure: In vitro investigation of underlying mechanisms.
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AR" term="%22Colosimo%2C+Raffaele%22">Colosimo, Raffaele</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> raffaele.colosimo@quadram.ac.uk</i><br /><searchLink fieldCode="AR" term="%22Warren%2C+Frederick+J%2E%22">Warren, Frederick J.</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> fred.warren@quadram.ac.uk</i><br /><searchLink fieldCode="AR" term="%22Finnigan%2C+Tim+J%2EA%2E%22">Finnigan, Tim J.A.</searchLink><relatesTo>2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Wilde%2C+Peter+J%2E%22">Wilde, Peter J.</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> peter.wilde@quadram.ac.uk</i>
– Name: TitleSource
  Label: Source
  Group: Src
  Data: <searchLink fieldCode="JN" term="%22Food+Chemistry%22">Food Chemistry</searchLink>. Nov2020, Vol. 330, pN.PAG-N.PAG. 1p.
– Name: Subject
  Label: Subjects
  Group: Su
  Data: <searchLink fieldCode="DE" term="%22Proteins%22">Proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Light+scattering%22">Light scattering</searchLink><br /><searchLink fieldCode="DE" term="%22Fungal+cell+walls%22">Fungal cell walls</searchLink><br /><searchLink fieldCode="DE" term="%22Filamentous+fungi%22">Filamentous fungi</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: • Mycoprotein cell walls are highly resilient to mechanical/physical processing and digestion. • Intestinal proteases are the main factors controlling protein bioaccessibility from mycoprotein products. • Diffusion of proteases through the cell wall is the proposed mechanism which facilitates the high protein bioavailability. • An optimal ratio of mycoprotein to enzymes is crucial for protein release. Mycoprotein is a food ingredient from filamentous fungi rich in protein and fibre. This study investigated the protein bioaccessibility from the fungal cells by colourimetric assays in different mycoprotein formulations, following extraction methods and in vitro gastrointestinal digestion. The methods effects were further analysed by static laser light scattering, SDS-PAGE and optical-fluorescence microscopy. The extraction methods released a comparable proportion of protein (30 wt%) independent of sample concentration (10 wt% and 25 wt%), whereas the simulated digestions endpoints released a higher proportion of protein from the less concentrated (46 wt%). Furthermore, mechanical/physical processing had only a minor impact. Intestinal proteases promoted the most efficient protein release but without causing any apparent damage to the cell walls when viewed by microscopy. This suggested that the enzymes can diffuse through the cell walls, due to its porosity/permeability, and are the main factors responsible for the hydrolysis and bioaccessibility of protein from mycoprotein. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Food Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=egs&AN=144671081
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1016/j.foodchem.2020.127252
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 1
        StartPage: N.PAG
    Subjects:
      – SubjectFull: Proteins
        Type: general
      – SubjectFull: Light scattering
        Type: general
      – SubjectFull: Fungal cell walls
        Type: general
      – SubjectFull: Filamentous fungi
        Type: general
    Titles:
      – TitleFull: Protein bioaccessibility from mycoprotein hyphal structure: In vitro investigation of underlying mechanisms.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Colosimo, Raffaele
      – PersonEntity:
          Name:
            NameFull: Warren, Frederick J.
      – PersonEntity:
          Name:
            NameFull: Finnigan, Tim J.A.
      – PersonEntity:
          Name:
            NameFull: Wilde, Peter J.
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 15
              M: 11
              Text: Nov2020
              Type: published
              Y: 2020
          Identifiers:
            – Type: issn-print
              Value: 03088146
          Numbering:
            – Type: volume
              Value: 330
          Titles:
            – TitleFull: Food Chemistry
              Type: main
ResultId 1