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Summary of lectures and knowledge clips Food Ingrdient Functionality (FIF) FCH-30306 €5,49
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Summary of lectures and knowledge clips Food Ingrdient Functionality (FIF) FCH-30306

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This summary contains all lectures and knowledge clips. With a very nice overview of all the polysaccharides in a table, help me a lot with learning all the content.

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  • 24 januari 2022
  • 25
  • 2021/2022
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marlyverest
Summary FCH-30306 Knowledge clips and reader
Marly Verest


Summary FCH-30306 FIF
Knowledge clips and reader

Proteins
Introduction
Functionality of proteins

- Nutritional e.g. essential amino acids
o Affected by primary structure = amino acid sequence
- Physiological e.g. bio-active peptides, anti-nutritional factors
o Affected by primary structure = amino acid sequence
- Physical/technological e.g. texture in bread, beer foam
o Affected by tertiary structure = three-dimensional form

Why study proteins?

- Increase functionality
o New product formulations
o Avoid allergic responses
- Reduce variability between batches

Production of protein isolates
Isolation of proteins – general scheme First step = removal of other compounds

Use difference in:

- Solubility (precipitations)
- Size (filtration, size-exclusion
chromatography)
o Microfiltration, ultrafiltration,
nanofiltration, reverse
osmosis
- Charge (ion-exchange
chromatography)



Protein concentrates and isolates are heterogeneous

- Contain non-protein compounds
- Several different proteins
- ‘main’ protein can be present in different forms e.g. glycated, denatures, and aggregated




1

, Summary FCH-30306 Knowledge clips and reader
Marly Verest

Properties of hydrolysates
Characterization of proteins hydrolysates

- Degree of hydrolysis (DH)
o Solubility of hydrolysates affected by:
 Exposure hydrophobic groups
 Loss of single iso-electric point (pI)
o Gel properties: Changed electrostatic and hydrophobic interactions result in changed
aggregation and gel properties
o Foam and emulsions: Composition and properties of hydrolysates depend on DH as
well as enzyme and hydrolysis conditions (can have good techno-functional
properties until the peptides become too small)
- Concentration of intact protein
- Molecular weight distribution of peptides
- Identification of peptides
- Quantification of the peptides

Effect of heating and processing
Reasons to heat protein preparations

- Inactivation e.g. bacteria/spores, endogenous enzymes
- Product modification e.g. increased gelling properties

Effect of heat on protein preparations

- Chemical modifications e.g. Maillard reaction, cross-link reaction, dephosphorylation, …
- Physical changes
o Denaturation (globular protein)
o Dissociation (micellar proteins)
o Precipitation of Ca-phosphate (caseins)

Measuring protein unfolding

- Differential Scanning Calorimetry (DSC)
o Enthalpy of unfolding (peak area) can be used to quantify fraction of ‘native’ protein
- Precipitation at iso-electric point
o Amount of soluble protein at pI can be used to quantify ‘native’ whey proteins

Proteins do NOT always denature when heated  higher denaturation temperature in dry
conditions, so more protein unfolding during heating in solution (pasteurisation) than during spray
drying




2

, Summary FCH-30306 Knowledge clips and reader
Marly Verest

Structure function relation
Technological functionality (table chapter 2: Figure 2)




Challenge in making structure function relations

- Current understanding
o Rules of thumb for mechanisms
o Case-by-case observations
o Only a limited number of well-studied proteins
- Future understanding
o Systematic studies
o Better understanding of underlying mechanisms
o Quantitative predictions

Gel properties
Proteins have much less, or almost no effect on viscosity compared to polysaccharides due to the
small size

Gelatin gels

- Difference between sources of gelatin  melting temperature
- Gel strength of gelatin gels depend on the amount of helices formed

Globular protein gels

- Native, unfolded, aggregate, gel formation
- Effect of ionic strength
- pH=pI  high ionic strength  fractal/random aggregate

Changing the gel properties: disulfide bridges

- Increased permeability
- Increased turbidity
- Syneresis
- Spontaneous gel rupture




3

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