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Updated: Jan 31, 2026

Preparation and Characterization of Nanoliposomes for the Entrapment of Bioactive Hydrophilic Globular Proteins
Published on: August 31, 2019
Insight into the effect of glycerol on stability of globular proteins in high protein model system
Xiaoxia Chen1, Bhesh Bhandari2, Peng Zhou1
1State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu Province 214122, China; International Joint Research Laboratory for Functional Dairy Protein Ingredients, U.S. China Dairy Innovation Center, Jiangnan University, Wuxi, Jiangsu Province 214122, China.
Abstract:
A model system was established to investigate the effect of glycerol on stability of globular proteins. To study whether protective effect of glycerol is dependent on the nature of protein, four kinds of globular protein were used including α-lactalbumin, β-lactoglobulin, native lactoferrin and lysozyme. Differential scanning calorimetry (DSC) was used to study the thermal stability of the proteins with glycerol aqueous (0-80% v/v). The results showed that the stability of β-lactoglobulin and lysozyme (hydrophobicity-dominated proteins) increased with glycerol concentration. However, that of α-lactalbumin and lactoferrin (metalloproteins), regardless of the ion-binding state, initially increased and then decreased. Different protective effects were observed beyond 50% (v/v) glycerol concentrations in liquid phase. The secondary structure and tryptophan exposure remained unchanged. In conclusion, the protection of glycerol on protein stability was highly dependent on the nature of proteins.
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