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Introduction

• Protein  complex macromolecules which build

>50% of DB live cells
• It consists of C, H, O, N and S also Fe, Cu, P, Zn

• Classification of protein is based on their

molecular structure, solubility, other compound
within the molecule, degradation level and
Amino Acid – Protein (1) function.
Food Chemistry Course

Protein General characteristics of Amino acids

 Proteins are polymers of amino acids (polypeptide)
 Amino acids are the building blocks (monomers) of proteins.
 20 different amino acids are used to synthesize proteins.
 The shape and other properties of each protein is dictated by
the precise sequence of amino acids in it.
 Different proteins have different chemical properties
 Because of widely different secondary and tertiary structures
# R-side chain decides the characteristics of AA
# Amino acids can be divided into groups depending on
the side chain functionality
– Broadly there are hydrophilic and hydrophobic side chains,
- High levels of polar amino acid residues in a protein
increase water solubility
– these can be subdivided into acidic, basic, polar, aromatic and
aliphatic

Classification of Amino acids according to

Example of amino acid R-side polarity
1. AA with hydrophobic side
# ALA, ILE, LEU, MET, PHE, PRO, TRP, VAL
# Hydrophobicity   the longer the aliphatic side
chain (opened chain)

(Aliphatic side chain)

Alanine

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2. AA with hydrophilic side

# CYS  its polarity caused by thiol group (-SH)
# Neutral, polar, functional group  can build hydrogen bond with certain
molecule (i.e. Water)
When its oxidised  CYSTINE where thiol group forms
# SER, THR, TYR  its polarity is caused by the hydroxyl group (-OH)
disulfide bond.
# ASN, GLN  its polarity is caused by amide group (-CO-NH2) 
hydrolise by acid/base (aspartic & glumatic acid).

3. AA with positive charged side (at pH 7) 4. AA with negative charged side (at pH 7)

Basic acidic characteristics of AA:

ionisation

 Other isolated AA:  In low concentrated solution (pH 7)  AA acts as

zwitter ion.
- Hydroxyproline, 5-hydrixylysine  contained in
colagen  When AA is dissolved in water, it can presents as:

- Desmosine & isodesmosine  in elastin - Acidic AA

- Methylhistidine & methyllysine  in muscle protein - Basic AA

 In total, >150 AA was found in the cells of animal,  The acidic/basic of AA depends on pH  amphoter.
plant and microorganisms.  IP (isoelectric point)  pH where the total charge in AA
is zero.

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Stereochemistry of AA Spectrum Absorption:Fluoresence

 # Amino acids are chiral molecules (except glycine, where  TRP, TRY, PHE  an absorp UV light with max.
R = H)  they have optical rotation  their asymmetric C absorbance of 278, 274.5, 260 nm.
atoms d and l isomers.
 CYS  238 nm
Two enantiomers of
a generic amino acid
 Other AA in general: 210 nm.

 In protein hydrolisate of plant and animal tissues  only

presents as l-isomers.
 D-isomers  in certain microbial cells & polypeptides can
acts as antibiotics, i.e. Actinomycin D, Gramicidin.

Amino Acids Amino Acids

 When hydrolyzed by strong mineral acids or with the
 Simplest amino acid: Glycine, The “R”-group is H (Hydrogen)
aid of certain enzymes, proteins can be completely  Aliphatic monoaminomonocarboxylic amino acids
decomposed into their component amino acids  Glycine
 Alanine
 Valine
 Leucine
 Isoleucine
 Serine
 Threonine
 Proline
 Sulfur-containing amino acids
 Cysteine
 Cystine
 Methionine

Amino Acids Protein Classification

 Monoaminodicarboxylic amino acids
 Classification of Proteins
 Aspartic acid  Based mostly on the solubility of proteins in different
 Glutamic acid
solvents
 Basic amino acids  More recent criteria being used includes:
 Lysine  Behaviour in the centrifuge
 Arginine  Electrophoreticproperties
 Histidine
 Proteins are divided into the following main groups
 Aromatic amino acids
 Simple Proteins
 Phenylalanine
 Conjugated Proteins
 Tyrosine
 Derived Proteins
 Tryptophan

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Protein Classification Protein Classification

 Simple Proteins  Conjugated Proteins

 Yield only amino acids on hydrolysis and include  Contain an amino acid part combined with a non-
the following classes protein material such as a lipid, nucleic acid, or
 Albumins carbohydrate
 Globulins  Some of the major conjugated proteins are as follows:
 Glutelins  Phosphoproteins
 Prolamins  Lipoproteins
 Sclereproteins  Nucleoproteins
 Histones  Glycoproteins
 Protamines  Chromoproteins

Protein Classification Protein structure

 Derived Proteins
 These are compounds obtained by chemical or enzymatic
methods and are divided into primary and secondary derivatives
 Primary derivatives
 Slightly modified and are insoluble in water
 Ex. Rennet-coagulated casein
 Secondary derivatives
 Changed more extensively, include proteoses, peptones, and
petides
 Difference between these breakdown products is in size and
solubility
 All are soluble in water
 Not coagulated by heat
 Proteoses can be precipitated with saturated ammonium sulfate
solution
 Peptides contain two or more amino acid residues

ProteinStructures
 Proteins are macromolecules with different levels of
structural organization
 Primary Structure
 the peptide bonds between component amino acids
 and also the amino acid sequences in the molecule
 Secondary Structure
 Involves folding the primary structure
 Hydrogen bonds between amide nitrogen and carbonyl oxygen are
the major stabilizing force
 Bonds may be formed between different areas of the same
polypeptide chain, or adjacent chains
 The secondary structure may be either a-helix or sheet
 Helical structures are stabilized by intramolecular hydrogen bonds
 Sheet structures are stabilized by intermolecular hydrogen bonds

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ProteinStructures
 Tertiary Structure
 Involves a pattern of folding of the chains into a compact unit
 Stabilized by:
 hydrogen bonds
 van der Waals forces
 disulfide bridges
 hydrophobic interactions
 This structure results in the formation of a tightly packed unit with most
polar amino acid residues located on the outside and hydrated
 Internal part with most of the apolar side chains and virtually no hydration
 Large molecules of molecular weights above about 50 000 may form
quaternary structures by association of subunits
 These structures my be stabilized by hydrogen bonds, disulfide bridges and
hydrophobic interactions

Denaturation

 A major change in the native structure that does

not involve alteration of the amino acid sequence
Changes the molecular structure without breaking
any peptide bonds of a protein
 Effect of heat usually involves a change in the tertiary structure,
leading to a less ordered arrangement of the polypeptide chains
 The temperature range in which denaturation and coagulation of
most proteins takes place is about 55 to 75C
 Casein and gelatin are examples of proteins that can be boiled
without apparent change in stability

Denaturation
 This process is peculiar to proteins and affects
different proteins to different degrees, depending on
the structure of a protein
 Denaturation can be brought about by various agents:
 Heat (most important), causes the destruction of enzyme activity
 pH
 Salts
 Surface effects
 Denaturation usually involves loss of biological
activity&significant changes in some physical or
functional properties, such as solubility
 Usually non-reversible
Denaturation
 Heat denaturation is sometimes desirable
 The denaturation of whey proteins for the production of milk powder used
in baking
 Proteins of egg white are readily denatured by heat and by surface forces
when egg white is whipped to a foam
 Meat proteins are denatured in the temperature range 57 to 75C, which has
a profound effect on texture, water holding capacity and shrinkage
 Denaturation may result in flocculation of globular proteins and
may lead to the formation of gels
 Protein denaturation and coagulation are aspects of heat stability
that can be related to the amino acid composition and sequence
of the protein

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Why do eggs look different cooked?
Eggs are a protein food and so are made up of
amino acid chains.
When eggs are cooked they become firmer.This is
because cooking eggs changes the shape of the amino
acid chains. This is called denaturing.
Changing the shape of the protein also changes its
properties. The protein becomes easier to digest and
more useful to the cells of the human body.
Meat is also made up of amino acids and reacts to
cooking in a similar way.
Figure.
Dough making
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Denaturation
 The exceptional Stability of Casein
 Makes it possible to boil, sterilize, and concentrate milk, without
coagulation
 In the first place:
 restricted formation of disulfide bonds due to low content of
cystine&cysteine results in increased stability
 Casein with its extremely low content of sulfurAAs are less likely to
become involved in the type of sulfhidrylagglomeration
 The heat stability of casein is also explained by the restraints
against forming a folded tertiary structure
 These restraints are due to the relatively high content of
proline&hydroxyproline in the heat stable proteins