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Identification and characterization of a novel angiotensin I-converting enzyme inhibitory peptide (ACEIP) from silkworm pupa

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Abstract

The angiotensin I-converting enzyme inhibitory peptide (ACEIP) was isolated and characterized from silkworm pupae and purified using Sephadex G-25 gel filtration. The structure and physicochemical properties of pupa ACEIP were analyzed. The α-P3 fraction exhibited the most potent ACE inhibitory activity. After purification via semi-preparative reverse-phase HPLC (RP-HPLC) and HPLC, the α-P3-6-b component was revealed to have the highest ACE inhibitory activity (IC50=28.3 μg/mL). Edman degradation revealed a Val-Glu-Ile-Ser amino acid sequence in which novel active sequences were identified. Physicochemical property testing showed that purified pupa ACEIP exhibits good solubility, heat resistance, and acid resistance that all indicate ACEIP derived from silkworm pupa is an excellent food-derived ACEIP.

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Authors and Affiliations

  1. College of Food Science, Southwest University, Chongqing, 400715, China

    Xiyu Li, Yong Li, Jiong Zheng, Fusheng Zhang & Jianquan Kan

  2. College of Biotechnology, Southwest University, Chongqing, 400715, China

    Xianzhi Huang

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  1. Xiyu Li
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  2. Yong Li
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Correspondence to Jianquan Kan.

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Li, X., Li, Y., Huang, X. et al. Identification and characterization of a novel angiotensin I-converting enzyme inhibitory peptide (ACEIP) from silkworm pupa. Food Sci Biotechnol 23, 1017–1023 (2014). https://doi.org/10.1007/s10068-014-0138-9

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  • DOI: https://doi.org/10.1007/s10068-014-0138-9

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