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Successive digestion of tilapia collagen by serine proteinase and proline specific endopeptidase to produce novel angiotensin I-converting enzyme inhibitory peptides

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Abstract

Serine proteinase, purified from the hepatopancreas of Pacific white shrimp (Litopenaeus vannamei), was used to hydrolyze acid solubilized collagen (ASC) isolated from Nile tilapia (Oreochromis sp.) skin to produce angiotensin I-converting enzyme (ACE) inhibitory peptides (ACEIPs). A series of column chromatography assays were used to separate the ACEIPs. A peptide, NPARTCR, was isolated as it exhibited high ACE inhibition potential. Further digestion of this peptide by a proline specific endopeptidase (PSEP), produced a pentapeptide ARTCR with ACE inhibitory activity (IC50) of 77.0 μmol/L. Both NPARTCR and ARTCR inhibited ACE in a non-competitive manner. An in vivo study in rats demonstrated that ARTCR has ACE inhibitory activity via lowering systolic blood pressure in spontaneously hypertensive rats (SHRs). These results suggest that processing by-products from shrimp and tilapia are ideal raw materials for the production of serine proteinase and collagen, respectively. Serine proteinase and collagen are both ideal raw materials that can be used to derive ACE inhibitory active peptides against hypertension.

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Abbreviations

ACEIP:

ACE inhibitory peptide

PSEP:

Proline specific endopeptidase

SHRs:

Spontaneously hypertensive rats

SBP:

Systolic blood pressure

HBP:

High blood pressure

NPARCTR:

Crude peptide isolate

ARTCR:

N-terminal cleavage pentapeptide

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Acknowledgements

This work was sponsored by the National Key R&D Program of China (2018YFD0901004), the National Natural Scientific Foundations of China (31471640, 31702372).

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Authors and Affiliations

  1. College of Food and Biological Engineering, Jimei University, Xiamen, 361021, China

    Xin Hua, Lechang Sun, Chan Zhong, Panpan Xiao, Guangming Liu & Minjie Cao

  2. Collaborative Innovation Center of Marine Food Deep Processing, Dalian Polytechnic University, Dalian, 116034, China

    Lechang Sun & Minjie Cao

  3. Department of Biological and Chemical Engineering, Shaoyang University, Shaoyang, 422000, China

    Qiang Wu

  4. Faculty of Fisheries, Nagasaki University, Nagasaki, 852-8521, Japan

    Asami Yoshida

Authors
  1. Xin Hua
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  2. Lechang Sun
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  3. Chan Zhong
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  4. Qiang Wu
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  5. Panpan Xiao
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  6. Asami Yoshida
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  7. Guangming Liu
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  8. Minjie Cao
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Contributions

XH contributed to the presented idea and design. LS implemented the computational and statistical analysis and took the lead in writing the manuscript. CZ and AY assisted with data analysis. MC and GL supervised the findings of this work. All authors provided critical feedback and helped to conduct the research, analysis, and preparation of the manuscript.

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Correspondence to Minjie Cao.

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The authors declare that they have no conflict of interest.

Animal and human rights statement

This article does not include results from any study involving human subjects performed by any of the authors. All study procedures that involved animals were in accordance with the ethical standards of the institution or practice where the study was conducted.

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Edited by Xin Yu.

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Hua, X., Sun, L., Zhong, C. et al. Successive digestion of tilapia collagen by serine proteinase and proline specific endopeptidase to produce novel angiotensin I-converting enzyme inhibitory peptides. Mar Life Sci Technol 2, 268–278 (2020). https://doi.org/10.1007/s42995-020-00038-y

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  • DOI: https://doi.org/10.1007/s42995-020-00038-y

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