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Pigments and colour in foods
• Flavonoids
– These are phenolic compounds with at least 3
phenyl groups and a sugar residue
– Anthocyanins
– Anthoxanthins
Pigments and colour in foods
– Anthocyanins
• These are flavonoids which contribute to several colours:
Red, purple, violet, and deep blue .
• Examples of food whose colours are due to anthocyanins
include strawberries, grapes, egg plants, peach skin,
plums, radish, apple etc
• Anthocyanins have three phenyl rings designated as A, B
& C rings
• They have a sugar residue attached to carbon 3 of the A
ring.
• The sugar can be glucose or arabinose, rhamnose
• Have a characteristic C6C3C6 carbon skeleton –
the basic structure of the flavonoids.
• The structure of all anthocyanins is based on
the flavan structure.
Flavan – Flavylium cation.
O
Flavan nucleus
A
B
1
2
3
4
5
6
7
8 1'
2'
3'
4'
5'
6'
+
O
General structure of anthocyanidins
The flavylium cation (at low pH)
A
B
5
7
3'
4'
5'
HO
OH
OH
R'
OH
R''
3
R` and R`` = H, OH
or OCH3
• The are:
R` R``
pelargonidin H H
cyanidin OH H
peonidin OCH3 H
delphinidin OH OH
petunidin OCH3 OH
malvidin OCH3 OCH3
Anthocyanins commonly found in
foods
Pigments and colour in foods
• Characteristics of anthocyanins
– They are water soluble
– They undergo colour change due to change in pH
• pH 7- Purple
• <pH 7 (acidic) – Red
• > pH 7 (alkaline) – Navy blue
– Colour intensity is reduced by
• Phenolase which removes the sugar
• Oxidation
• Meat colour from oxidation state of myoglobin,
ligands bound and state of the globin protein.
• Oxidation – the Fe in the haem can exist as the
reduced Fe2+ (Mb) or oxidised Fe3+ (MMb).
• Oxygenation – binding of molecular oxygen to
the sixth ligand site on the Fe2+.
• Both Mb and Hb transport oxygen bound to this
sixth ligand site – oxymyoglobin (MbO2)
Myoglobin
• Myoglobin (deoxymyoglobin) is purplish-red
• Binding O2 to oxymyoglobin gives the
customary bright red of meat.
• Both Mb and MbO2 can have oxidation, the Fe2+
being oxidised to Fe3+ - undesirable brownish
red in colour.
• Conditions in muscle determine the ratios of
Mb, MMb and MbO2. Inter-conversion of these
occurs readily in muscle not in meat.
Myoglobin
• Heat denatures myoglobin.
• Myoglobin decreases rate of haem oxidation –
so denaturation leads to easier oxidation of
Mb to MMb.
• Also easier oxidation at lower pH.
• In cured meats have stable pink colour – due
to reaction with nitrite compounds at 6th co-
ordination site.
Myoglobin
General structure of myoglobin:
Pigments and colour in foods
• Myoglobin
– This is the pigment responsible for the colour of muscle.
– Myoglobin is composed of a heme unit and globin protein
molecule
– The colour of myoglobin depends on
• The presence of oxygen: Red vs purplish red
• Heat: Denatured, brown colour
• Presence of oxidising agents: brownish
• Spoilage: Greenish colour due to the presence of sulfur
Meat color – chemical state of myoglobin:
Browning reactions in foods,
and acrylamide formation:

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Food Chemistry - Color and pigments in Food_Part 3.pptx

  • 1. Pigments and colour in foods • Flavonoids – These are phenolic compounds with at least 3 phenyl groups and a sugar residue – Anthocyanins – Anthoxanthins
  • 2. Pigments and colour in foods – Anthocyanins • These are flavonoids which contribute to several colours: Red, purple, violet, and deep blue . • Examples of food whose colours are due to anthocyanins include strawberries, grapes, egg plants, peach skin, plums, radish, apple etc • Anthocyanins have three phenyl rings designated as A, B & C rings • They have a sugar residue attached to carbon 3 of the A ring. • The sugar can be glucose or arabinose, rhamnose
  • 3. • Have a characteristic C6C3C6 carbon skeleton – the basic structure of the flavonoids. • The structure of all anthocyanins is based on the flavan structure.
  • 4. Flavan – Flavylium cation. O Flavan nucleus A B 1 2 3 4 5 6 7 8 1' 2' 3' 4' 5' 6' + O General structure of anthocyanidins The flavylium cation (at low pH) A B 5 7 3' 4' 5' HO OH OH R' OH R'' 3 R` and R`` = H, OH or OCH3
  • 5. • The are: R` R`` pelargonidin H H cyanidin OH H peonidin OCH3 H delphinidin OH OH petunidin OCH3 OH malvidin OCH3 OCH3 Anthocyanins commonly found in foods
  • 6. Pigments and colour in foods • Characteristics of anthocyanins – They are water soluble – They undergo colour change due to change in pH • pH 7- Purple • <pH 7 (acidic) – Red • > pH 7 (alkaline) – Navy blue – Colour intensity is reduced by • Phenolase which removes the sugar • Oxidation
  • 7. • Meat colour from oxidation state of myoglobin, ligands bound and state of the globin protein. • Oxidation – the Fe in the haem can exist as the reduced Fe2+ (Mb) or oxidised Fe3+ (MMb). • Oxygenation – binding of molecular oxygen to the sixth ligand site on the Fe2+. • Both Mb and Hb transport oxygen bound to this sixth ligand site – oxymyoglobin (MbO2) Myoglobin
  • 8. • Myoglobin (deoxymyoglobin) is purplish-red • Binding O2 to oxymyoglobin gives the customary bright red of meat. • Both Mb and MbO2 can have oxidation, the Fe2+ being oxidised to Fe3+ - undesirable brownish red in colour. • Conditions in muscle determine the ratios of Mb, MMb and MbO2. Inter-conversion of these occurs readily in muscle not in meat. Myoglobin
  • 9. • Heat denatures myoglobin. • Myoglobin decreases rate of haem oxidation – so denaturation leads to easier oxidation of Mb to MMb. • Also easier oxidation at lower pH. • In cured meats have stable pink colour – due to reaction with nitrite compounds at 6th co- ordination site. Myoglobin
  • 10. General structure of myoglobin:
  • 11. Pigments and colour in foods • Myoglobin – This is the pigment responsible for the colour of muscle. – Myoglobin is composed of a heme unit and globin protein molecule – The colour of myoglobin depends on • The presence of oxygen: Red vs purplish red • Heat: Denatured, brown colour • Presence of oxidising agents: brownish • Spoilage: Greenish colour due to the presence of sulfur
  • 12. Meat color – chemical state of myoglobin:
  • 13.
  • 14. Browning reactions in foods, and acrylamide formation: