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In vitro antioxidant and angiotensin I-converting enzyme inhibitory properties of peptides derived from corn gluten meal

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Abstract

Corn gluten meal (CGM) was hydrolyzed by Alcalase 2.4L and Protex 7L to obtain low-molecular-weight peptides. The antioxidant and angiotensin-I-converting enzyme (ACE) inhibitory activities of the peptides were determined by 2,2′-Azinobis-(3-ethylbenzthiazoline-6-sulphonate) (ABTS) free radical scavenging activity, the JHH7 cell oxidative stress model, and the ACE inhibition assay, respectively. Corn peptides (CPs) had strong antioxidant capacity to scavenge ABTS radicals (1.44 ± 0.11 mmol/g), and significantly reduced reactive oxygen species and malondialdehyde levels in oxidized JHH7 cells, increasing superoxide dismutase, catalase, and glutathione peroxidase activities by 26.20%, 147.52%, and 43.20%, respectively, at the concentration of 800 μg/mL. CPs had high ACE inhibitory activity, with an IC50 value of 0.27 ± 0.05 mg/mL. Next, the CPs were separated by reverse-phase high-performance liquid chromatography. Twelve fractions were collected, and their ABTS free radical scavenging and ACE inhibitory activities were determined. Fractions 1, 2, 3, 4, and 9 showed higher ABTS free radical scavenging and ACE inhibitory activities. Twelve peptides were identified from active fractions by liquid chromatography–tandem mass spectrometry (LC–MS/MS) as Leu-Ser-Pro-Tyr, Leu-Asn-Ser-Pro-Ala-Tyr, Tyr-Gly-Pro-Gln, Pro-Pro-Tyr, Ala-Tyr-Pro-Glu, Thr-Tyr-Ser-Gly-Pro-Lys, Ala-Tyr-Pro-Gly-Pro-Gln, Leu-Ala-Tyr-Pro-Gln, Ala-Tyr-Leu-Gln-Gln-Gln, Ser-Ala-Pro, Asn-Ala-Pro, and Val-Asn-Ala-Pro. These peptides exhibited good ABTS free radical scavenging and ACE inhibitory activities. Therefore, CPs may have potential applications in the food industry as functional material additives.

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Acknowledgements

This study was supported by grants from the National Key Research and Development Program of China (No. 2016YFD0400604), the General Program of the National Natural Science Foundation of China (No. 31671963), and Fund by Key Laboratory of Animal Protein Food Deep Processing Technology of Zhejiang Province (ZJAP-2019–01).

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  1. Wen-Ying Liu and Lei Fang have contributed equally to this work.

Authors and Affiliations

  1. Key Laboratory of Animal Protein Food Deep Processing Technology of Zhejiang Province, Zhejiang Province, Ningbo, 315832, People’s Republic of China

    Wen-Ying Liu

  2. Beijing Engineering Research Center of Protein and Functional Peptides, China National Research Institute of Food and Fermentation Industries Co., Ltd., Beijing, 100015, People’s Republic of China

    Wen-Ying Liu, Lei Fang, Xiao-Wen Feng, Guo-Ming Li & Rui-Zeng Gu

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  1. Wen-Ying Liu
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  2. Lei Fang
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Correspondence to Wen-Ying Liu.

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Liu, WY., Fang, L., Feng, XW. et al. In vitro antioxidant and angiotensin I-converting enzyme inhibitory properties of peptides derived from corn gluten meal. Eur Food Res Technol 246, 2017–2027 (2020). https://doi.org/10.1007/s00217-020-03552-6

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  • DOI: https://doi.org/10.1007/s00217-020-03552-6

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