In vitro antioxidant and wound-healing activities of hydrolyzed collagen from defatted Asian sea bass skin as influenced by different enzyme types and hydrolysis processes

Hydrolyzed collagen (HC) from defatted Asian sea bass skin was prepared by different enzymatic hydrolysis processes. For one-enzyme hydrolysis, papain (0.3 unit per g dry matter, DM) at 40 degrees C for 90 min or Alcalase (0.2 or 0.3 unit per g DM) at 50 degrees C for 90 min were used. The two-enzyme hydrolysis was accomplished with papain at 0.3 unit per g DM (P0.3), followed by Alcalase hydrolysis at 0.2 or 0.3 units per g DM (A0.2 or A0.3, respectively). HC prepared using the P0.3 + A0.3 process showed higher peptide yield, recovery and imino acid content in addition to stronger ABTS, DPPH radical scavenging activities and ferric reducing antioxidant power than other hydrolysis processes. HC obtained from the P0.3 + A0.3 process (at 125-500 mu g mL(-1)) induced MRC-5 fibroblast proliferation and augmented migration and lamellipodia formation in the cells. Peptides with average molecular weight of 750 Da exhibited the highest ABTS radical scavenging activity while the 4652 Da fraction had the lowest. Thus, HC can be considered as a suitable ingredient to formulate functional products for skin nourishment and wound healing.

Automated summary

Research found that hydrolyzed collagen prepared by a two-enzyme hydrolysis process with papain and Alcalase showed higher peptide yield, stronger antioxidant activities, and enhanced cell migration, making it suitable for formulating functional products for skin nourishment and wound healing.