Optimization of preparation technology of ovalbumin-peptide by complex enzyme and its antialcoholic effect

Abstract

Objective: This study aimed to verify the antialcoholic activity of ovalbumin peptide and improve the added value of egg products. Methods: Ovalbumin was hydrolyzed by alkaline protease and trypsin. The activity rate of alcohol dehydrogenase (ADH) was taken as index, and the enzymolysis process was optimized by response surface methodology. The total antioxidant activity, hydrolysis degree, amino acid composition and relative molecular weight of ovalbumin peptide were determined to evaluate the antialcoholic effect of ovalbumin peptide. Results: The optimum enzymatic hydrolysis conditions were as follows. Under the conditions of enzymatic hydrolysis time 5 h, dosage of complex enzyme 3 100 U/g, enzymatic hydrolysis temperature 50 ℃, ratio of solid to liquid movalbumin∶Vdistilled water=3.5∶25 (g/mL), the ADH activation rate of ovalbumin peptide was (22.71±0.15)%, and the total antioxidant capacity was (9.51±0.03) U/mL. The degree of hydrolysis was (29.28±0.16)%. Ovalbumin peptide was rich in amino acids such as glutamic acid (9.553 4%), alanine (3.863 3%), leucine (5.764 7%), which was beneficial to improve the activity of antialcoholic, and the content of small molecule peptide (＜1 000 Da) was more than 88.77%. Conclusion: The ovalbumin peptide prepared by complex enzymatic hydrolysis method has good antioxidant activity and antialcoholic effect.

Keywords

• ovalbumin peptide
• alcohol dehydrogenase activation rate
• enzymatic hydrolysis optimization
• antioxidation
• promote ethanol metabolism