Abstract
This study focused on the preparation method of antioxidant peptides by enzymatic hydrolysis of bone collagen after microwave assisted acid pre-treatment and nitrogen protection. Phosphoric acid showed the highest ability of hydrolysis among the four other acids tested (hydrochloric acid, sulfuric acid and/or citric acid). The highest degree of hydrolysis (DH) was 9.5% using 4 mol/L phosphoric acid with a ratio of 1:6 under a microwave intensity of 510 W for 240 s. Neutral proteinase gave higher DH among the four protease tested (Acid protease, neutral protease, Alcalase and papain), with an optimum condition of: (1) ratio of enzyme and substrate, 4760 U/g; (2) concentration of substrate, 4%; (3) reaction temperature, 55 °C and (4) pH 7.0. At 4 h, DH increased significantly (P < 0.01) under nitrogen protection compared with normal microwave assisted acid pre-treatment hydrolysis conditions. The antioxidant ability of the hydrolysate increased and reached its maximum value at 3 h; however DH decreased dramatically after 3 h. Microwave assisted acid pre-treatment and nitrogen protection could be a quick preparatory method for hydrolyzing bone collagen.
Highlights
Collagen is one of the longest fibrous structural proteins
We found that when the reaction is completed, degree of hydrolysis (DH) does not change, and the antioxidant activity of hydrolysate decreased significantly; it might be due to antioxidant peptides that react with environmental oxygen
This research showed that the swine bone collagen hydrolysate has high antioxidant activity under the optimum conditions of neutrase hydrolysis
Summary
Collagen is one of the longest fibrous structural proteins. Collage is an extracellular matrix protein, which plays an important role in many animal tissues within the skeletal, muscular and cardiovascular network tissues [1]. Native collagen is very hard to digest; their functions are quite different from those of globular proteins such as enzymes. Tough bundles of collagen called collagen fibers are a major component of the extracellular matrix that supports most tissues and gives cells structure from the outside, but collagen is found inside certain cells. As raw materials in medicine and food industries, collagen peptides are used as important active components because of their excellent bioactivity, good biocompatibility, good penetrability and non-irritation of the body [3]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
