Insights into enzymatic hydrolysis: Exploring effects on antioxidant and functional properties of bioactive peptides from Chlorella proteins

Abstract

Chlorella protein hydrolysate (CPH) is highly valued for its protein content, solubility, and functionality. Our main aim is to produce CPH via enzymatic hydrolysis using pepsin, alkaline, trypsin, and pancreatic enzymes and to analyze its amino acid composition, antioxidant activity, functional, and physiological properties. After the extraction and preparation of bioactive peptides (BAPs) derived from Chlorella protein, they were enzymatically hydrolyzed using the mentioned enzymes, and the degree of hydrolysis (DH) was evaluated. Our results showed that samples fabricated with trypsin and alkaline enzymes had the highest water-holding capacity (WHC) (3.8 g water/g dry matter) and oil-holding capacity (OHC) (5.7 g oil/g dry matter), respectively. Enzymatic hydrolysis with alkaline enzyme and trypsin showed the strongest radical scavenging activities of DPPH (83.2%) and ABTS (77.5%), respectively. Additionally, hydroxyl radical scavenging activity (HRSA) and reducing power of crude protein increased after enzymatic hydrolysis. Enzymatic hydrolysis also increased the metal-chelating activity. Based on these findings, it can be concluded that CPH has the best potential in improving the nutritional and functional properties of food ingredients and products.

Keywords

• Antioxidants activities
• Enzymatic hydrolysis
• Functional properties
• Chlorella proteins hydrolysate
• Bioactive peptides