Bioactivity and Functional Properties of Protein Hydrolysate from Muscle and Visceral Waste of Ribbon Fish (Lepturacanthus savala) Extracted by Three Different Proteolytic Enzymes

Abstract

The study focuses on utilization of solid visceral waste from ribbon fish in preparation of protein hydrolysates, possessing bioactive properties. Three different proteolytic enzymes (alcalase 2.4 U/g, flavourzyme 500 U/g, and papain 1 U/mL) were used to standardize the preparation of visceral waste protein hydrolysates (VPH) in comparison to muscle protein hydrolysate (MPH). Based on the preliminary studies, the hydrolysis process was standardized to 4 h at 1.5 % (w/v) enzyme concentration. MPH and VPH form all the enzymes were taken to study the bioactive (ACE-1 and antioxidant activity) and functional properties. MPH and VPH extracted from alcalase (IC₅₀ = 0.835 and 0.902 mg/mL) showed higher angiotensin converting enzyme-1 (ACE-1) inhibitory activity than flavourzyme (IC₅₀ = 1.602 and 1.323 mg/mL) and papain (1.263 and 1.565 mg/mL). Similarly, alcalase extracted samples were showed higher levels of radical scavenging activity (IC₅₀ = 2.538 and 2.835 mg/mL) than papain (IC₅₀ = 8.382 and 9.389 mg/mL) and flavourzyme (IC₅₀ = 10.562 and 11.56 mg/mL). The present study proves that visceral waste, which is often discarded in a larger quantity, polluting the environment can be converted into a nutraceutical component with greater health benefits.

Keywords:

• Visceral waste
• fish protein hydrolysates
• MPH
• VPH
• Bioactive properties