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| Characteristics of Peptides Derived from Muscle Matrix Proteins of Andrias davidianus by Collagenase and Elastase |
| ZENG Yunhao, CHEN Dejing, DONG Mengyao, DANG Xinxin |
| 1.College of Biological Sciences and Engineering, Shaanxi University of Technology, Hanzhong 723001, China; 2.Shaanxi Key Laboratory of Resource Biology, Shaanxi University of Technology, Hanzhong 723001, China |
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Abstract The spectral characteristics, amino acid compositions, molecular masses, physical properties and in vitro antioxidant activity of peptides produced by enzymatic hydrolysis of muscle matrix protein of giant salamander with collagenase or elastase were investigated. The results showed that the yields of peptides with collagenase and elastase were 45.11% and 37.36%, respectively. The resulting peptides exhibited maximum absorption peaks at 210–230 and 200–220 nm in the ultraviolet (UV) spectra. The infrared spectra showed absorption peaks in the amide A, B and II bands for both peptides and absorption peaks in the amide III band only for the collagen peptide. Each of the peptides contained seven essential amino acids; the content of hydrophobic amino acids was higher, and the content of aromatic amino acids was lower. The peptides exhibited no electrophoretic bands with molecular mass in the marker range of 13–150 kDa. Both peptides had viscosity. The results of scanning electron microscopy (SEM) showed that the structure of the collagen peptide was spongy and was composed of large lamellas, while the structure of the elastin peptide was composed of flakes of different sizes and loose. Both peptides had antioxidant activity in a concentration-dependent manner.
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2022, Vol. 36 
