FND 100 Lecture Notes - Lecture 3: Trypsin Inhibitor, Rennet, Egg White
30 Apr 2018
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• Digestibility
o Structure - folding of proteins
o Inhibitors - trypsin inhibitors that would inactivate to get full biological value
• Coagulation
o Is not a negative term, typically involves denaturation of PRO, taking a native
PRO, a PRO in its original structure, usually soluble (eg. egg white proteins- high
liquid high moisture compound, easily soluble)
o Native protein (soluble) >>(heat)>> gel (insoluble)
o H2O holding capacity
• Original native folded protein
• Polar AA towards outside, hydrophobic in inside
• Denature through heat (Chemical denaturing: or acid? Physically denaturing: Or through
beater/whisk (egg whites) ) >>> Unfolding it and therefore exposing AA side chains +
peptide bonds
• Got the protein folded in original Shape, hydrophobic on the inside and hydrophilic on
the outside
• Quite a bit of PRO that are denaturing in the sauce pans, casein is more difficult to
denature, components that make up the skin on the surface (the skin from heated milk)
• Custard making (based on heat) or cheese making
o Slightly different mechanisms
o Custard = heat
o Cheese making (rennet) = the enzyme activity
• Coagulation - formation of a semi-solid gel
• Moisture that separates is the whey
Eggs:
Koal X 4168 - kjoules (kJ)
One grade A large egg (50 g) provides:
E =75 kJ
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