Abstract
Gelatine was extracted from deer antler base by the hot water method and hydrolyzed with trypsin. A comparison of the properties of gelatine before and after enzymatic hydrolysis showed a decline in the surface hydrophobicity, enhanced thermal stability, broadening of the particle size distribution, a zeta potential shift to a lower pH, reduced foaming and emulsifying properties, and enhanced antioxidant activity. Hydrolysis increased the gelatine antioxidant activity in DPPH and FRAP assays. These results indicate that the functional properties of deer antler base gelatine may be affected by trypsin modification.
Highlights
Deer (Cervidae) are animals mainly distributed in Eurasia, North America, South America and southwest Africa
Trypsin had a stronger effect on the enzymatic reaction of gelatine than pepsin and was selected for subsequent experiments
The foaming capacity (FC) has been correlated with peptide size; FIGURE 4 differential scanning calorimetry (DSC) curves of deer antler base gelatine and its hydrolysate
Summary
Deer (Cervidae) are animals mainly distributed in Eurasia, North America, South America and southwest Africa. The aim of this study was to evaluate the following functional properties of deer antler gelatine before and after enzyme hydrolysis: thermal properties, the zeta potential, the particle size distribution, the surface hydrophobicity, foaming properties, and emulsifying properties. TA B L E 1 Degree of hydrolysis, surface hydrophobicity, thermal stability, and zeta potential of deer antler base gelatine and its hydrolysate
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