Food proteins. Nutritive function of proteins.

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Lecture 5.
Food proteins. Nutritive function of proteins.
Quality evaluation.
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Proteins: a major food macro-component.
Food is the major source providing proteins to
human body:
 
food with animal origin
 
food with plant origin
Food proteins: General overview. 
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Why do we need proteins?
Food proteins
Amino acid mixture
Digestion
New proteins
Biologically 
Active
Compounds
Hormones: insulin,
serotonin and melatonin
(tryptophan derived)
Energy
(May provide up to 10-15%
of body’s energy need. )
Glycogen
Lipids
(re-synthesis)
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The amount of protein needed depends on:
Individual physiological features:
Sex
Age
Physical activity
Health status
Protein quality:
Amino acid composition/ratio
Protein digestibility
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Protein quality: Amino acid composition
20 common amino acids composing proteins.
Non-essential
 amino acids (NE): body 
can
 synthesize them.
Essential
 amino acids (E): body 
can not 
synthesize them. 
Must
be supplied by diet.
Conditionally essential 
amino acids: nonessential amino acids
that become essential under certain conditions.  For example Tyr
(NE) is synthesized by Phe (E). If diet is low in Phe then Tyr
becomes conditionally essential.
The quality 
of a dietary protein is a measure of
its ability to provide the essential amino acids
required for tissue maintenance.
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Essential amino acids
Valine
Leucine
Isoleucine
Lysine
Methionine
Phenylalanine
Threonine
Tryptophan
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Complete proteins: contain an adequate
proportion of all the essential amino acids that
should be incorporated into a diet.
Proteins from animal sources (meat, poultry, milk, and fish) have a
high quality because they contain all the essential amino acids in
proportions similar to those required for synthesis of human
tissue proteins
[Note: Gelatin prepared from animal collagen is an exception; it
has a low biological value as a result of deficiencies in several
essential amino acids.]
 
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Incomplete proteins: 
lack one or more essential
amino acids or contain them in inadequate
proportions necessary for human metabolism.
 Proteins from plant sources (wheat, corn, rice, and
beans) have a lower quality (except soy protein) than do
animal proteins. They are considered incomplete.
 
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Incomplete proteins 
from different plant
sources may 
be combined 
in such a way
that the result is equivalent in nutritional
value to animal protein.
Complementary proteins
Complementary proteins
 
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Methods for evaluation of protein quality
Amino acid scoring 
provides a way to predict how
efficiently protein will meet person’s amino acid
needs.
This concept assumes that tissue protein
synthesis is limited unless all required amino acids
are available at the same time and in appropriate
amounts at the site of tissue protein synthesis.
Amino Acid Scoring (AAS)
Chemical methods
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Ration 
of the amount of each essential amino acid (g/100g protein)
in a test protein and the amount of the respective essential amino
acid (g/100g protein) in an “ideal protein” as defined by FAO/WHO.
Proposed “ideal protein” :
Whole egg protein
Milk protein
Amino acid score calculation
 
For example, 
if the lysine content of a whole-wheat flour protein is 2.6% and
the value for lysine in an “ideal protein” is 5.1%,  AAS is calculated as
2.6/5.1
x
100=51.
The essential amino acid with the lowest AAS for certain protein
is called limiting amino acid.
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Drawbacks
AAS is determined after acid hydrolyses of
proteins which results in total amino acid content.
Some of the amino acids in the total pool are not
bioavailable.
The degree of error varies depending on food:
o
highly processed food has impaired
digestibility
o
proteins with plant origin have lower
digestibility
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Amino acid scoring does not take protein
digestibility into account. It is useful for
comparing animal products and refined foods that
are not excessively heated.
Plant foods are not completely digested, it is
necessary to make a correction to the calculation
of AAS.
Protein digestibility-corrected
amino acid score (PDCAAS)
PDCAAS = 
Protein digestibility x Amino acid score
J. Nutr.  2000, vol. 130  no. 7  1865S-1867S
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Protein digestibility
A measure of efficient utilization of a protein
 
Calculations:
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Factors affecting protein digestibility
Indigenous anti-nutritional factors:
Glucosinolates (mustard and rapeseed)
Trypsin inhibitors and hemagglutinins (legumes)
Tannins (legumes and cereals)
Phytates  (cereals and oilseeds)
Gossypol (cottonseed protein products.)
Effects of antinutritional factors on protein digestibility
and amino acid availability in foods 
J AOAC Int.
 2005
May-Jun;88(3):967-87.
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Oxidized forms of sulfur amino acids,
D-amino acids,
Lysinoalanine (LAL – cross-linkage
between polypeptides).
Maillard compounds,
Anti-nutritional factors formed
during heat/alkaline processing of
protein containing food.
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Biological Value (BV)
Biological Value (BV) is a measure of
the proportion of the absorbed protein
from food which becomes incorporated
into the proteins of the organism's body.
B.V. = (N retained/N-absorbed) x 100
Egg and human milk have BV = 90-100;
Meat and fish have BV = 75–80;
Wheat protein - 50;
Biological  methods:  Animal assays
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Apparent Net Protein Utilization (NPU)
Defined as the percentage of ingested protein
which is deposited as tissue protein
Pb - the total body protein at the end of the feeding trial,
Pa - the total body protein at the beginning of the feeding
trial,
Pi  - the amount of protein consumed over the feeding trial.
In this calculation no allowance is made for endogenous
protein losses.
Representative sample of animals should be sacrificed at the
beginning and end of the feeding trial for carcass protein
analysis.
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Protein Efficiency Ratio (PER) is the gain in
weight of growing animals per gram of protein
eaten.
Protein Efficiency Ratio (PER) 
With this method no allowance is made for
maintenance: ie. method assumes that all
protein is used for growth
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Biological  methods: Microbial assays
For determination of:
Total amino acids (after chemical hydrolysis)
Bioavailable amino acids
Microorganisms used:
Tetrahymena pyriformis
Streptococcus zymogenes
Escherichia coli
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Streptococcus zymogenes:
It does not require lysine and therefore, this amino acid (neither
total nor bioavailable) can not be determined.
Can hydrolyze protein with own enzymes but slowly. Protein
could be pre-treated with enzymes.
Tetrahymena pyriformis
It requires all essential amino acids for growth
Own extracellular enzymes to hydrolyze proteins
Assay takes 2-3 days
Escherichia coli
Auxotrophs for specific amino acids are used
Use own extracellular enzymes to digest food ingredients
Assay can be completed in 6 to 8 hours
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Advantages of microbial assays
Compared to animal assays:
Simple
Fast
Cheaper
Do not require elaborate equipment
 
Do not require vast working space 
Overall cost effective
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Food proteins are essential for various functions in the body, including digestion, energy provision, and synthesis of new proteins. The quality of proteins depends on factors like amino acid composition and digestibility, with animal sources typically containing all essential amino acids. Learn about complete and incomplete proteins, essential amino acids, and how protein quality impacts overall health.

  • Food Proteins
  • Nutritive Functions
  • Protein Quality
  • Essential Amino Acids
  • Complete Proteins

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  1. Lecture 5. Food proteins. Nutritive function of proteins. Quality evaluation.

  2. Food proteins: General overview. Proteins: a major food macro-component. Food is the major source providing proteins to human body: food with animal origin food with plant origin

  3. Why do we need proteins? Food proteins Digestion Amino acid mixture Glycogen Lipids (re-synthesis) New proteins Biologically Active Compounds Hormones: insulin, serotonin and melatonin (tryptophan derived) Energy (May provide up to 10-15% of body s energy need. )

  4. The amount of protein needed depends on: Individual physiological features: Protein quality: Sex Age Physical activity Health status Amino acid composition/ratio Protein digestibility

  5. Protein quality: Amino acid composition 20 common amino acids composing proteins. Non-essential amino acids (NE): body can synthesize them. Essential amino acids (E): body can not synthesize them. Must be supplied by diet. Conditionally essential amino acids: nonessential amino acids that become essential under certain conditions. For example Tyr (NE) is synthesized by Phe (E). If diet is low in Phe then Tyr becomes conditionally essential. The quality of a dietary protein is a measure of its ability to provide the essential amino acids required for tissue maintenance.

  6. Essential amino acids Valine Leucine Isoleucine Lysine Methionine Phenylalanine Threonine Tryptophan

  7. Complete proteins: contain an adequate proportion of all the essential amino acids that should be incorporated into a diet. Proteins from animal sources (meat, poultry, milk, and fish) have a high quality because they contain all the essential amino acids in proportions similar to those required for synthesis of human tissue proteins [Note: Gelatin prepared from animal collagen is an exception; it has a low biological value as a result of deficiencies in several essential amino acids.]

  8. Incomplete proteins: lack one or more essential amino acids or contain them in inadequate proportions necessary for human metabolism. Proteins from plant sources (wheat, corn, rice, and beans) have a lower quality (except soy protein) than do animal proteins. They are considered incomplete.

  9. Complementary proteins Incomplete proteins from different plant sources may be combined in such a way that the result is equivalent in nutritional value to animal protein. Ile, Leu Lys Met Trp Legumes x x Cereals x x Combined

  10. Methods for evaluation of protein quality Chemical methods Amino Acid Scoring (AAS) Amino acid scoring provides a way to predict how efficiently protein will meet person s amino acid needs. This concept assumes that tissue protein synthesis is limited unless all required amino acids are available at the same time and in appropriate amounts at the site of tissue protein synthesis.

  11. Amino acid score calculation Ration of the amount of each essential amino acid (g/100g protein) in a test protein and the amount of the respective essential amino acid (g/100g protein) in an ideal protein as defined by FAO/WHO. http://docsdrive.com/images/ansinet/ja/2007/image2-2k7-286-293.gif Proposed ideal protein : Whole egg protein Milk protein For example, if the lysine content of a whole-wheat flour protein is 2.6% and the value for lysine in an ideal protein is 5.1%, AAS is calculated as 2.6/5.1x100=51. The essential amino acid with the lowest AAS for certain protein is called limiting amino acid.

  12. Drawbacks AAS is determined after acid hydrolyses of proteins which results in total amino acid content. Some of the amino acids in the total pool are not bioavailable. The degree of error varies depending on food: o highly processed food has impaired digestibility o proteins with plant origin have lower digestibility

  13. Protein digestibility-corrected amino acid score (PDCAAS) Amino acid scoring does not take protein digestibility into account. It is useful for comparing animal products and refined foods that are not excessively heated. Plant foods are not completely digested, it is necessary to make a correction to the calculation of AAS. PDCAAS = Protein digestibility x Amino acid score J. Nutr. 2000, vol. 130 no. 7 1865S-1867S

  14. Protein digestibility A measure of efficient utilization of a protein Calculations: where I = nitrogen intake F = fecal nitrogen output on the test diet Fk = fecal nitrogen output on a non-protein diet.

  15. Factors affecting protein digestibility Indigenous anti-nutritional factors: Glucosinolates (mustard and rapeseed) Trypsin inhibitors and hemagglutinins (legumes) Tannins (legumes and cereals) Phytates (cereals and oilseeds) Gossypol (cottonseed protein products.) Effects of antinutritional factors on protein digestibility and amino acid availability in foods J AOAC Int. 2005 May-Jun;88(3):967-87.

  16. Anti-nutritional factors formed during heat/alkaline processing of protein containing food. Oxidized forms of sulfur amino acids, D-amino acids, Lysinoalanine (LAL cross-linkage between polypeptides). Maillard compounds,

  17. Biological methods: Animal assays Biological Value (BV) Biological Value (BV) is a measure of the proportion of the absorbed protein from food which becomes incorporated into the proteins of the organism's body. B.V. = (N retained/N-absorbed) x 100 Egg and human milk have BV = 90-100; Meat and fish have BV = 75 80; Wheat protein - 50;

  18. Apparent Net Protein Utilization (NPU) Defined as the percentage of ingested protein which is deposited as tissue protein Pb - the total body protein at the end of the feeding trial, Pa - the total body protein at the beginning of the feeding trial, Pi - the amount of protein consumed over the feeding trial. In this calculation no allowance is made for endogenous protein losses. Representative sample of animals should be sacrificed at the beginning and end of the feeding trial for carcass protein analysis.

  19. Protein Efficiency Ratio (PER) Protein Efficiency Ratio (PER) is the gain in weight of growing animals per gram of protein eaten. With this method no allowance is made for maintenance: ie. method assumes that all protein is used for growth

  20. Biological methods: Microbial assays For determination of: http://i.cbc.ca/1.1527823.1409966010!/httpImage/image.jpg_gen/derivatives/16x9_620/hi-nb-e-coli-fredericton-8col.jpg Total amino acids (after chemical hydrolysis) Bioavailable amino acids Microorganisms used: Escherichia coli http://www.oxoid.com/omd/library/fullsize/CM0701.jpg Tetrahymena pyriformis Streptococcus zymogenes

  21. Streptococcus zymogenes: It does not require lysine and therefore, this amino acid (neither total nor bioavailable) can not be determined. Can hydrolyze protein with own enzymes but slowly. Protein could be pre-treated with enzymes. Tetrahymena pyriformis It requires all essential amino acids for growth Own extracellular enzymes to hydrolyze proteins Assay takes 2-3 days Escherichia coli Auxotrophs for specific amino acids are used Use own extracellular enzymes to digest food ingredients Assay can be completed in 6 to 8 hours

  22. Advantages of microbial assays Compared to animal assays: Simple Fast Cheaper Do not require elaborate equipment Do not require vast working space Overall cost effective

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