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Related Concept Videos

Protein Folding01:25

Protein Folding

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
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Protein Denaturation01:28

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The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
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Bacterial Protein Maturation01:26

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Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
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Molecular Chaperones and Protein Folding03:00

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Meat analogs: Protein restructuring during thermomechanical processing.

Akashdeep Singh Beniwal1,2, Jaspreet Singh1,2, Lovedeep Kaur1,2

  • 1School of Food and Advanced Technology, Massey University, Palmerston North, New Zealand.

Comprehensive Reviews in Food Science and Food Safety
|February 16, 2021
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Summary
This summary is machine-generated.

Developing sustainable meat alternatives requires understanding how protein ingredients interact during processing. This review explores how raw materials and processing parameters create fibrous, meat-like textures in plant-based analogs for improved food security.

Keywords:
functional propertiesmeat analogsprotein interactionsthermomechanical processing

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Species Determination and Quantitation in Mixtures Using MRM Mass Spectrometry of Peptides Applied to Meat Authentication
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Area of Science:

  • Food Science and Technology
  • Biomaterials Engineering
  • Sustainable Food Systems

Background:

  • Growing concerns about inefficient meat production and its impact on global food security necessitate sustainable alternatives.
  • Meat's desirable sensory qualities stem from its unique molecular composition and fibrous structure.
  • Advancements in food structuring science allow the use of alternative proteins to mimic meat's texture.

Purpose of the Study:

  • To review the structure-function-process relationships in creating meat analogs from concentrated protein systems.
  • To elucidate how raw materials and processing parameters influence the texture and sensory attributes of meat alternatives.
  • To provide insights for developing concept-based meat analogs with controlled structural properties.

Main Methods:

  • Analysis of physicochemical and structural changes in concentrated protein systems during thermomechanical processing.
  • Examination of phase transitions influenced by protein-protein, protein-polysaccharide, protein-lipid, and protein-water interactions.
  • Review of the impact of raw material composition (moisture, protein, lipids, polysaccharides, air) and processing parameters (temperature, pH, shear).

Main Results:

  • Thermomechanical processing induces physicochemical and structural changes, yielding fibrous or layered meat-like textures.
  • Interactions between components (proteins, polysaccharides, lipids, water) and processing conditions significantly affect texture and sensory outcomes.
  • Controlling raw material properties and processing parameters is key to achieving desired structural attributes in meat analogs.

Conclusions:

  • Understanding the interplay between ingredients and processing is crucial for manufacturing high-quality meat analogs.
  • This knowledge aids in developing plant-based meat alternatives that meet consumer expectations for texture and sensory appeal.
  • Successful development of meat analogs contributes to sustainable food systems and enhanced global food security.