Step 1: Denaturation of proteins.
- Egg-white proteins (ovalbumin, conalbumin, etc.) are native (\(P_N\)) in raw egg.
- Upon heating (\(\Delta\)), they unfold → denatured state (\(P_D\)).
Step 2: Aggregation.
- Denatured proteins lose solubility and expose hydrophobic groups.
- Further heating causes aggregation (\(P_A\)).
Step 3: Gelation.
- Aggregated proteins crosslink via hydrophobic, hydrogen, and disulfide bonds.
- Leads to formation of a continuous 3D structure: the protein gel (\(P_G\)).
Step 4: Analyze options.
- (A) Shows reversible cooling steps → incorrect (denaturation is largely irreversible).
- (B) Correct: \(P_N \;\xrightarrow{\Delta}\; P_D \;\xrightarrow{\Delta}\; P_A \;\rightarrow\; P_G\).
- (C) Skips aggregation step → incomplete.
- (D) Jumps from native to aggregate without denaturation step → incorrect.
Final Answer:
\[
\boxed{\text{(B)}}
\]