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| Characteristics of Proteins Isolated from Giant Salamander Muscle |
| YANG Hui, CHEN Dejing, CHEN Haitao, DONG Mengyao |
| 1.College of Biological Science and Engineering, Shaanxi University of Technology, Hanzhong 723001, China; 2.Shaanxi Provincial Bio-Resource Key Laboratory, Shaanxi University of Technology, Hanzhong 723001, China; 3.Hanzhong Longni Biological Engineering Co. Ltd., Hanzhong 723001, China |
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Abstract In this paper, the composition and characteristics of giant salamander muscle proteins were studied. Sarcoplasmic, myofibrillar and muscle matrix proteins were isolated from giant salamander muscle, and their protein content, amino acid composition, molecular mass, ultraviolet (UV) spectra and infrared (IR) spectra were determined, and protein microstructures were observed by scanning electron microscope (SEM). The results showed that the content of sarcoplasmic protein was 4.91%, with a molecular mass of 20–200 kDa; the content of myofibrillar protein was 9.03%, mainly including 200 kDa myosin heavy chain, 43 kDa actin and 36 kDa myosin; and the content of muscle matrix protein was 2.28%, with molecular mass distribution in the range of 29–40 and 160–200 kDa. All three proteins exhibited maximum UV absorption peaks at 280 nm. There were characteristic IR absorption peaks for myofibrillar protein in the amide A, B, Ⅰ, Ⅱ and Ⅲ regions, while the characteristic IR absorption peaks of sarcoplasmic protein and muscle matrix protein appeared only in the amide Ⅰ, Ⅱ and Ⅲ regions. The SEM images showed that the surface of sarcoplasmic protein was smooth, myofibrillar protein was a rod-shaped or granular polymer, and muscle matrix protein had a more intact fiber structure.
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2020, Vol. 34 
