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FREE Notes Food Chemistry - Knowledge clips Proteins

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Free document that contains notes about the knowledge clips about Proteins.

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Notes knowledge clips – Proteins
Introduction to proteins
 Animal proteins  milk, egg, blood, gelatin
 Plant proteins  soy, lupine, sunflower
 New proteins  potato, algae, leaf proteins
 Nutrition: essential amino acids
 Structure: for instance collagen contains gelatin
 Metabolism: for instance anti-bodies
 Taste: for instance by Maillard reaction
 Build-up of amino acids (amino group and carboxylic acid group). Linked to
central carbon atom. The differences between amino acids are determined by
the side group R.





 Peptides: linking carboxylic group of one amino acid with the amino group of
another amino acid. This is done by a peptide bond.
 Oligo-peptides: 2-100 amino acids
 Protein: 100-300 amino acids  adopts a structure
 Properties of proteins depends on amino acids, total folding state of protein
 Peptides can be formed by hydrolysing proteins
 Meat (muscle) proteins: not soluble so they can give structure to the body
 Milk proteins: should be soluble so the calf can drink the milk and the proteins
are dissolved in the milk.

Amino acids
 Amino group (NH2) and carboxylic group (COOH) are linked to central carbon
atom (alpha carbon atom).
 Also a R group (side chain) is connected to the alpha carbon atom.
 4th place is taken by an H.
 So all places of the carbon are full  you can get stereoisomers .
 Proteins: only 20 different amino acids (only alpha-L)
 You can have L or D stereoisomer. L means that the amino group is on the
left. D means the amino group is on the right. D-amino acids are not
digestible.
 Alpha and beta amino acids. Alpha: amino group is attached to the alpha
carbon atom (the central one). Beta: amino group is attached to one carbon
atom lower (the beta carbon)
 Aromatic amino acids: for instance tryptophan: contains a benzene ring
(aromatic group). Does not dissolve very well in water because no polar
group.
 Aliphatic amino acids: only carbon-hydrocarbon chains (leucine). Does not
dissolve very well in water because no polar group.

,  Polar amino acids: for instance asparagine, has an amide function: C double
bonded O and NH2.
 Classification of amino acids
o Non-polar & non-charged: hydrophobic, low solubility in water, are
positioned in inside of protein.
 Side chains are aliphatic group, aromatic group, imino acid (thio-
ether)
o Polar & non-charged: hydrophilic, high solubility, on outside of
proteins, reactive
 Side chains are hydroxyl groups, sulfhydryl groups, amide
groups (can be reactive under certain conditions)
o Polar & charged: very well soluble, outside of protein, can be
reactive, charge depends on pH!!
 Side chains are carboxyl group and amino groups
 Low pH: carboxylic group is protonated and neutral, amino group
is protonated and thus positively charged.
 High pH: carboxylic group is deprotonated and thus negative
charge. Becomes deprotonated and is neutrally charged.
 Classification on nutritional value
o Essential  not produced by body (should be taken up by diet)
o Conditionally essential  certain people should eat more of them
o Non-essential  can be produced by the body
o The reactive amino acids are distributed over all these classes. If you
have a lot of reactions (high reactivity), you can loose nutritional value.
 Leucine: non polar side groups so non-polar, non-charged
 Glutamic acid: contains an additional COOH group = polar, charged
 Tyrosine: contains aromatic ring and hydroxylic group (polar)  polar, non-
charged amino acid.

Peptides
 More reactive than intact proteins  sometimes not convenient
 Have taste  not always desired because sometimes bitter
 Taken up more easily by the body
 Can have anti-oxidant, blood-pressure properties
 Combination of amino-acids (carboxyl group with amino group)  peptide
bond. One water molecule is released! Weight of dipeptide is smaller than two
amino acids together.
 Tripeptides, or even longer can be formed from this.
 Nomenclature: N-terminal side should always be on the left (the amino acid
where the amino group is still free and not bound). Right side: C-terminal
side with free carboxylic group. Cysteine and glutamic acid are bound at alpha
carbon.
 However, if you would have glutathione, the amino acids are bound at the
gamma carbon. You then call it: gamma-glutamyl-cysteinyl-glycine. YL
because these amino acids are bound to next amino acid. Between Cys and
Gly – and between glu and cys = corned line. Because glutamic acid is not
linked by alpha but gamma carboxylic group. Difference in digestibility and
functionality

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