Related Experiment Video
Updated: Mar 18, 2026

05:55
High-throughput, Microscale Protocol for the Analysis of Processing Parameters and Nutritional Qualities in Maize Zea mays L.
Published on: June 16, 2018
7.6K
Protein structural changes during processing of vegetable feed ingredients used in swine diets: implications for
S Salazar-Villanea1, W H Hendriks2, E M A M Bruininx2
11Wageningen UR Livestock Research,Wageningen,The Netherlands.
Nutrition Research Reviews
|July 1, 2016
Summary
Protein structure, particularly beta-sheets, impacts enzyme accessibility and digestibility. Processing can alter protein structures, with outcomes depending on conditions and protein type, affecting nutritional value.
Area of Science:
- Food Science and Technology
- Protein Chemistry
- Nutritional Biochemistry
Background:
- Protein digestibility is crucial for nutritional value and is influenced by protein structure.
- Intramolecular beta-sheets in native proteins are associated with reduced digestibility.
- Processing can induce simultaneous positive (denaturation) and negative (aggregation) structural changes affecting digestibility.
Purpose of the Study:
- To explore the mechanisms by which processing affects protein digestibility.
- To understand how different processing parameters influence protein structural changes.
- To clarify the relationship between protein structure modifications and nutritional outcomes.
Main Methods:
- Review of literature on protein processing and its effects on digestibility.
- Analysis of the impact of processing parameters like heat, moisture, and shear.
- Investigation of protein structural changes, including denaturation, random coil formation, aggregation, and Maillard reactions.
Main Results:
- Processing-induced structural changes have a counterbalancing effect on protein digestibility.
- Heat is a primary driver of protein structural modification during processing.
- The correlation between denaturation enthalpy and digestibility varies by protein source.
Conclusions:
- Understanding the mechanisms of processing-induced structural changes is key to predicting nutritional consequences.
- Processing conditions and protein type are critical determinants of digestibility outcomes.
- Further research is needed to disentangle the effects of multifactorial processing technologies.
Related Concept Videos
Protein and Protein Structure
91.6K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
A protein's shape is critical to its function. For example, an enzyme...
91.6K
Protein Digestion
113.2K
Protein digestion begins in the stomach, where the highly acidic environment can easily disrupt protein structure by exposing the peptide bonds of polypeptide chains. After polypeptide chains are broken into individual amino acids by a series of digestive enzymes, the amino acids are transported to the liver via the bloodstream to produce energy.
113.2K
Protein Folding
12.1K
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
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
12.1K
Protein Folding
129.9K
Overview
129.9K
Bacterial Protein Maturation
674
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...
674
Protein Denaturation
10.5K
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...
10.5K

