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European Food Research and Technology

, Volume 244, Issue 9, pp 1615–1625 | Cite as

Isolation and identification of two potential antioxidant peptides from sheep abomasum protein hydrolysates

  • Bing Liu
  • Haji Akber Aisa
  • Abulimiti Yili
Original Paper
  • 146 Downloads

Abstract

The objective of this study was to obtain antioxidant peptides from sheep abomasum protein hydrolysates (SAPH). Sheep abomasum proteins were first hydrolyzed using alcalase, neutrase, or papain. Results from three enzyme tests revealed that the hydrolysis process of papain catalyst was most effective as SAPH generated by papain exhibited the highest degree of hydrolysis (DH), yield, and antioxidant activity. The effect of the conditions for hydrolysis with papain was further optimized using the response surface methodology. The highest DH and yield of SAPH (16.86 and 40.65%, respectively) were obtained under the following conditions: hydrolysis temperature, 46 °C; hydrolysis time, 3.8 h; and enzyme/substrate ratio, 1.5%. Two novel peptides with high antioxidant activity were purified from SAPH by ultrafiltration, ion exchange chromatography, gel filtration chromatography, and reverse-phase high-performance liquid chromatography. Peptide sequences were determined as Leu-Glu-Asp-Gly-Leu-Lys (LEDGLK, SAPHP-A) and Ile-Asp-Asp-Val-Leu-Lys (IDDVLK, SAPHP-B) with molecular weights of 674.37 and 703.41 Da, respectively. The results of the present study indicated that peptides purified from SAPH were natural antioxidants and could be used as food additives and pharmaceutical products.

Keywords

Antioxidant peptide Sheep abomasum Enzymatic hydrolysis Optimization Purification 

Notes

Acknowledgements

Thank for the Central Asia Drug Research and Development Center of the Chinese Academy of Sciences and the Training Project of Xinjiang Autonomous Region for Technological Innovation of Youth Talents for financial support.

Compliance with ethical standards

Conflict of interest

The authors declare no conflict of interest.

Compliance with ethics requirements

This article does not contain any studies with human participants or animals.

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Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Xinjiang Technical Institute of Physics and ChemistryChinese Academy of SciencesUrumqiChina
  2. 2.The Key Laboratory of Plant Resources and Chemistry of Arid Zone and State Key Laboratory Basis of Xinjiang Indigenous Medicinal Plants Resource UtilizationUrumqiChina
  3. 3.University of Chinese Academy of SciencesBeijingChina

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