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

Raffaele Colosimo1, Frederick J Warren1, Tim J A Finnigan2

  • 1Quadram Institute Bioscience, Norwich Research Park, Norwich, Norfolk NR4 7UQ, UK.

Food Chemistry
|June 26, 2020
PubMed

Insights

This study shows that protein bioaccessibility from mycoprotein is enhanced by lower concentrations and intestinal proteases, which effectively hydrolyze fungal cell walls without causing damage. This highlights key factors for optimizing mycoprotein as a protein source.

Area of Science:

  • Food Science
  • Biotechnology
  • Mycology

Background:

  • Mycoprotein, derived from filamentous fungi, is a valuable source of protein and fiber.
  • Understanding protein bioaccessibility is crucial for optimizing its nutritional value.

Purpose of the Study:

  • To investigate factors influencing protein bioaccessibility from mycoprotein.
  • To analyze the effects of extraction methods, sample concentration, and in vitro digestion on protein release.

Main Methods:

  • Colorimetric assays for protein quantification.
  • Static laser light scattering, SDS-PAGE, and optical-fluorescence microscopy for structural analysis.
  • In vitro gastrointestinal digestion models.

Main Results:

  • Extraction methods released approximately 30% protein, irrespective of concentration (10% and 25% wt%).
  • Simulated digestion released more protein (46% wt%) from lower concentration mycoprotein.
  • Intestinal proteases were most effective for protein release, penetrating porous fungal cell walls without apparent damage.

Conclusions:

  • Mycoprotein concentration significantly impacts protein bioaccessibility during simulated digestion.
  • Enzymatic hydrolysis by intestinal proteases is the primary driver of protein release, facilitated by fungal cell wall permeability.
  • Mechanical/physical processing has a minimal effect on protein bioaccessibility.

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