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ACE inhibitory and antihypertensive properties of apricot almond meal hydrolysate

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Abstract

Apricot almond meal was hydrolyzed simultaneously with Neutrase and N120P proteases. The hydrolysate almond peptide (AP) was fractionated into three ranges of molecular weight (AP-I, >5 kDa; AP-II, 1–5 kDa; AP-III, <1 kDa) using an ultrafiltration membrane bioreactor system. The AP-III brought about a high angiotensin-I-converting enzyme (ACE) inhibitory activity with IC50 value of 0.138 mg mL−1 and the content of hydrophobic amino acid of AP-III was 50.08%. Lineweaver–Burk plots suggested that AP-III acts as a non-competitive inhibitor to inhibit ACE. And we evaluated the stability and in vivo antihypertensive activity of AP-III. Multiple dose oral administration (100 mg kg−1 body weight (BW), 400, 800 mg kg−1 BW) to spontaneously hypertensive rats led to a significant decrease in blood pressure for AP-III. Additionally, the gel filtration and RP-HPLC were used to separate ACE inhibitory peptides from the hydrolysate. The results suggested that the peptide derived from apricot almond protein may have potential applications as functional food.

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Acknowledgments

This research was funded by Major Special Project of the Xinjiang Uygur Autonomous Region (200831108).

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Authors and Affiliations

  1. Institute of Agro-food Science and Technology, The Key Laboratory of Agro-Food Process and Quality Control, Ministry of Agriculture, Chinese Academy of Agriculture Science, 2 Yuanmingyuan west road, Beijing, 100193, China

    Chunyan Wang, Jinqiang Tian & Qiang Wang

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  1. Chunyan Wang
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  2. Jinqiang Tian
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  3. Qiang Wang
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Correspondence to Qiang Wang.

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Wang, C., Tian, J. & Wang, Q. ACE inhibitory and antihypertensive properties of apricot almond meal hydrolysate. Eur Food Res Technol 232, 549–556 (2011). https://doi.org/10.1007/s00217-010-1411-7

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  • DOI: https://doi.org/10.1007/s00217-010-1411-7

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