| Abstract: | The heat stability of rapeseed 12S globulin (cruciferin) was examined using 8-anilinonaphthalene-1-sulphonic acid (ANS) as a fluorescence probe. Heating cruciferin (0·06–0·3 mg ml−1 in 10 mM glycyl–glycyl piperizine buffer, pH 7·0, with 0·1–1·0 M NaCl) for 20 min increased its hydrophobicity as monitored by ANS fluorescence measurements. The mid-point temperature for the heat effect (Tm) increased linearly with increasing solvent pH (Tm (°C)=4·16 pH+41 (μ=0.1)) or sodium chloride concentration (Tm (°C)=14·7 [NaCl]+71 (pH=7·0)). The range of Tm values for cruciferin was 45–96°C. At 20°C cruciferin was unstable at pH<3·0 but relatively stable under alkaline conditions (pH 8–10). Though possessing an oligomeric structure, cruciferin appears to heat denature in accordance with the two-stage deactivation model for simple globular proteins. |
