Resource Utilization of Bovine Neck Ligament: Enzymatic Preparation of Elastin Peptide and Its Antioxidant Activity.

Abstract

Elastin is considered an excellent resource for obtaining antioxidant peptides due to unique amino acid composition. However, it is hardly soluble in water or in dilute acid or alkali; most of the elastases have low yields for preparing elastin peptides, making it difficult to meet industrial applications. To address above problems, enzymes capable of hydrolyzing elastin into soluble peptides were preferred from typical commercial protease preparations. The optimal enzymatic hydrolysis process conditions for elastin peptides were obtained by response surface optimization design. The molecular weight, amino acid composition, and antioxidant activity of the enzymatic hydrolysis products were determined. The results show that the alkaline protease NUE has a strong hydrolysis effect. The optimized enzymatic hydrolysis conditions are as follows: substrate concentration is 5%, enzyme concentration is 650 U/mL, pH is 10.0, temperature is 60°C, time is 6h. The degree of hydrolysis of elastic protein peptides obtained through this method is 14.42%. The distribution of molecular weight is 200-6500Da, more than 85% of the component molecular amount is greater than 800Da; the amino acid content related to antioxidant activity has reached 68mg/100mg, so it has extremely high free radical clearance. Compared with acid and alkali methods, the anti-oxidation capacity of enzyme-based peptide is better, the reaction conditions are milder, the yield is higher, and by-products and pollutants are fewer. It provides an effective way to industrialized production of elastin peptides with high antioxidant activity and a basis for its widespread application in the food and pharmaceutical industries.