LU2 Proteins - Part 2

Gelation
 Protein gelation refers to transformation of a protein

from the ‘sol’ state to a ‘gel-like’ state.
 Protein gels are prepared by heating a moderately
concentrated protein solution
 In this mode of gelation :
denaturation Cool (ambient/refrigeration T)
Protein in a ‘sol’ state → ‘progel’ state → gel
Gelation
 Proteins form two types of gel.
1. Coagulum (Opaque) Gel
2. Translucent Gel
Proteins containing large amounts of non polar amino
acid residues undergo hydrophobic aggregation upon
denaturation.
 These insoluble aggregates randomly associate and set
into coagulum (Opaque) gel
 Rate of aggregation faster than rate of denaturation.
Readily set into gel network even while being heated.
 Coagulum (Opaque) gel are weak & prone to syneresis
Gelation
 Proteins containing small amounts of non polar amino
acid residues form soluble complexes upon
denaturation
 Rate of association of these soluble complexes is slower
than rate of denaturation
 They often do not set into gel until heating followed by
cooling has occurred.
 Upon cooling, the slow rate of association of the
soluble complexes facilitates formation of an ordered
tranlucent gel network.
 Tranlucent gels are less prone to syneresis
Two Types of Gels
Coagulum (Opaque) Gel
Proteins form two types of gel.
Aggregation
large amounts of non polar amino acid
heat Cooling
(PD)n
nPN nPD Translucent
Gel
small amounts of non polar amino acid
(soluble complexes)
PN is native state, PD is unfolded state & n is number of protein molecules
Protein Quality
 What is Protein Quality?
 Proteins with a relatively high content of essential amino acids are
called first class proteins or high quality proteins
 This type of proteins are quite expensive to produce
 Animal proteins usually contain much more of the essential amino acids
than do plant proteins
 Intermediate quality proteins are those derived from plant material
 Poor quality proteins are derived from cassava and other roots and tubers
Proteins undergo several chemical changes when processed at high T.
These changes include racemization, hydrolysis, desulfuration and
deamidation
Some of the reactions result in formation of modified amino acid
types that are potentially toxic
Racemization of amino acids in
alkali-treated food proteins
 Thermal processing of protein at alkaline pH leads to
recemization of L-amino acid residues to D-amino
acid
 Residues such as Asp, Ser, Cys, Glu, Phe, Asn and Thr
are racemized at faster rate than other amino acid
residues
 The rate of racemization is about 10 x faster in protein
than in free amino acids.
Racemization
 Biological effects of racemization
 Reduction in protein digestibility and protein quality
 D-amino acids are also less efficiently absorbed through

intestinal mucosa cells & even if absorbed, they cannot
be utilized in in vivo protein synthesis
 Some D-amino acids, for example D-proline, have been
found to be neurotoxic in chickens
Racemization
 When protein are heated > 200oC, amino acids
undergo decomposition/ pyrolysis.
 Several pyrolysis product from broiled & grilled meat
are highly mutagenic.
 The most carcinogenic & mutagenic product formed
from pyrolysis of Trp & Glu residues.
 Mutagenic compounds produced from meat at T =190-
200 oC known as IQ (imidazo quinolines compounds)
which are condensation products of sugars & certain
amino acids such as Gly, Thr, Ala & Lys.
Three most potent mutagens
Form in broiled fish
2-amino-3-methylimidazoquinoline (1)
2-amino-3, 4-dimethylimidazoquinoline (2)
2-amino-3, 8-dimethylimidazoquinoxaline (3)
1 2 3
Mechanism of racemization
Abstraction
of α-proton
from amino
acid residue
to give a
negatively
charged
carbanion
When a proton is
added back to
this optically
inactive
intermediate,
either a D- or L-
enantiomer may
be formed.
Protein Cross-linking
 Processing of food proteins, especially at alkaline pH
will induce cross-link formation.
 Resulting in formation of lysinoalanine.
 Lysinoalanine is the major cross-link commonly found
in alkali treated protein.
 Biological effects of protein-protein cross-links in alkali
treated protein
Chemical Modification of proteins
 To alter the chemical properties of protein
 To improve functional properties of protein
 Alkylation
 Acylation
Alkylation
 SH & amino groups can be alkylated by reacting with
iodoacetate or iodoacetamide
Alkylation
 Effectively block sulfhydryl group so disulfide induce
protein polymerization cannot occur
Alkylation
 sulfhydryl group also can be blocked by reaction with
N-Etylmaleimide
Alkylation
 Amino groups can be alkylated with aldehyde &
ketones or sugar in the presence of sodium
borohydride (NaBH4)
 Resulting glycoprotein as the end product
Acylation
 Amino groups can be acylated by reacting with several
acid anhydrides.
 Acylated proteins are more soluble than native

protein.
 The solubility of caseins or less soluble proteins can be

increased by acylation
Acylation

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Gelation

 Protein gelation refers to transformation of a protein

large amounts of non polar amino acid

 D-amino acids are also less efficiently absorbed through

 Acylated proteins are more soluble than native

 The solubility of caseins or less soluble proteins can be

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