Abstract:

In the present study, the preparation of DPPH radical scavenging peptides derived from enzymatic hydrolysates
of Monopterus albus bone by different proteases was optimized using combination of single factor method and response
surface methodology. The optimal hydrolysis conditions for Monopterus albus bone peptides were determined as follows:
papain was the most suitable enzyme for the hydrolysis of Monopterus albus bone; the hydrolysis was allowed to proceed at
59.2 ℃ for 4.1 h at an initial pH of 5.8 with a substrate concentration of 40 mg/mL at an enzyme dosage of 8 000 U/g. The
DPPH radical clearance rate of the resulting hydrolysate was 90.85%. In vitro antioxidant assays showed that Monopterus
albus bone peptides had excellent concentration-dependent antioxidant activity.

Key words: Monopterus albus bone, peptides, antioxidant activity