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Separation and Purification of Antioxidant Peptides from Enzymatically Prepared Scorpion (Buthus martensii Karsch) Protein Hydrolysates

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Abstract

The purpose of this study was to separate and purify antioxidant peptides from the scorpion (Buthus martensii Karsch) protein hydrolysates (SPHs). Scorpion protein (SP) was first hydrolyzed by trypsin, papain, and alcalase, respectively. Results from hydrolysis tests revealed that peptides hydrolyzed with papain showed the highest degree of hydrolysis (DH), yield and antioxidant activity. The effect of papain hydrolysis on scorpion protein was optimized using the response surface methodology. The highest DH (31.31%) and yield (52.02%) of SPHs were obtained under the following conditions: hydrolysis time, 4.0 h; hydrolysis temperature, 50 °C; and enzyme/substrate ratio, 2.43%. Ultrafiltration, gel filtration and reversed-phase high-performance liquid chromatography was used and two novel antioxidant peptides were obtained. The sequences of the peptides determined by MALDI–TOF–MS/MS were LPTETLH (MW: 810.43 Da, P4-1) and IEEDLER (MW: 903.44 Da, P4-2), respectively. The results revealed SPHs as a potential valuable bioresource for production of antioxidant peptides in the food system.

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Acknowledgements

This work was supported by the Program for National Science and Technology Major Project of China (No. 2017ZX09301045), and we thank Central Asian Drug Research and Development Center of Chinese Academy of Sciences.

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Correspondence to Abulimiti Yili.

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Wali, A., Wubulikasimu, A., yanhua, G. et al. Separation and Purification of Antioxidant Peptides from Enzymatically Prepared Scorpion (Buthus martensii Karsch) Protein Hydrolysates. Int J Pept Res Ther 26, 1803–1818 (2020). https://doi.org/10.1007/s10989-019-09976-3

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