Purification and molecular docking study of angiotensin I-converting enzyme (ACE) inhibitory peptides from hydrolysates of marine sponge Stylotella aurantium
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Title
- Purification and molecular docking study of angiotensin I-converting enzyme (ACE) inhibitory peptides from hydrolysates of marine sponge Stylotella aurantium
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Author(s)
- Ko, Seok-Chun; Jang, Jiyi; Ye, Bo-Ram; Kim, Min-Sun; Choi, Il-Whan; Park, Won-Sun; Heo, Soo-Jin; Jung, Won-Kyo
- KIOST Author(s)
- Heo, Soo Jin(허수진)
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Alternative Author(s)
- 예보람; 김민선; 허수진
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Publication Year
- 2017-03
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Abstract
- Angioteinsin I-converting enzyme (ACE) inhibitory peptide was isolated from marine sponge (Stylotella aurantium) hydrolysate prepared by various hydrolysis enzymes. The peptic hydrolysate exhibited highest ACE inhibitory activity among them and was fractionated into three ranges of molecular weight. The below 5 kDa fraction showed the highest ACE inhibitory activity and was used for subsequent purification steps. The amino acid sequences of the purified peptides were identified to be Tyr-Arg (337.2 Da), and Ile-Arg (287.2 Da). The purified peptides from marine sponge had an IC50 value of 237.2 mu M and 306.4 mu M, respectively. The molecular docking study revealed that ACE inhibitory activity of the purified peptides was mainly attributed to the hydrogen bond interactions and Pi interaction between the dipeptides and ACE. The results suggest that marine sponge, S. aurantium would be an attractive raw material for the manufacture of anti-hypertensive nutraceutical ingredients. (C) 2016 Elsevier Ltd. All rights reserved.
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ISSN
- 1359-5113
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URI
- https://sciwatch.kiost.ac.kr/handle/2020.kiost/2128
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DOI
- 10.1016/j.procbio.2016.12.023
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Bibliographic Citation
- PROCESS BIOCHEMISTRY, v.54, pp.180 - 187, 2017
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Publisher
- ELSEVIER SCI LTD
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Subject
- SPONTANEOUSLY HYPERTENSIVE-RATS; PROTEIN HYDROLYSATE; BIOCHEMICAL-CHARACTERIZATION; FRAME PROTEIN; SKIN; IDENTIFICATION
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Keywords
- Marine sponge; Stylotella aurantium; Angioteinsin I-converting enzyme (ACE); Molecular docking; Peptides
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Type
- Article
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Language
- English
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Document Type
- Article
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