Safflower Protein Hydrolysates: Physicochemical, Functional Properties and Antioxidant Activities

Area of Science:

• Food Science
• Biochemistry
• Protein Chemistry

Background:

• Safflower protein isolate (SPI) is a valuable source of plant-based protein.
• Understanding the impact of enzymatic hydrolysis on SPI properties is crucial for its application.

Purpose of the Study:

• To investigate the effects of enzymatic hydrolysis using Alcalase and Flavourzyme on SPI.
• To evaluate the changes in physicochemical, functional, and antioxidant properties of SPI hydrolysates.

Main Methods:

• Safflower protein isolate was hydrolyzed with Alcalase and Flavourzyme at varying degrees of hydrolysis (2–10%).
• Physicochemical properties (color, cohesiveness, flowability, hydrophobicity, solubility) were assessed.
• Functional properties (oil binding, water holding, foaming, emulsion capacities/stability) were measured.
• Antioxidant activities (ABTS, DPPH radical scavenging) were determined.

Main Results:

• Hydrolysis resulted in lighter color, reduced redness, lower cohesiveness, and improved flowability of SPI.
• Surface hydrophobicity decreased significantly, while solubility increased, particularly at pH 4–7.
• Alcalase hydrolysates exhibited higher oil binding, foaming, and emulsion capacities compared to Flavourzyme.
• Optimal foaming and emulsion capacities were observed with Alcalase at 8% hydrolysis, though stability was reduced.
• Safflower protein hydrolysates displayed enhanced ABTS and DPPH radical scavenging activities.

Conclusions:

• Enzymatic hydrolysis significantly enhances the physicochemical, functional, and antioxidant properties of safflower protein isolate.
• The choice of enzyme and degree of hydrolysis critically influences the resulting hydrolysate characteristics.
• Safflower protein hydrolysates offer improved potential for various food applications.