Effect of angiotensin I-converting enzyme (ACE) inhibitory peptide purified from enzymatic hydrolysates of <Emphasis Type="Italic">Styela plicata</Emphasis> |
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Authors: | Seok-Chun Ko Min Cheol Kang Jung-Kwon Lee Hee-Guk Byun Se-Kwon Kim Seung-Cheol Lee Byong-Tae Jeon Pyo-Jam Park Won-Kyo Jung You-Jin Jeon |
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Affiliation: | (1) Department of Marine Life Science, Jeju National University, Jeju, 690-756, Republic of Korea;(2) Faculty of Marine Bioscience and Technology, Kangnung-Wonju National University, Gangneung, 210-720, Republic of Korea;(3) Department of Chemistry, Pukyoung National University, Busan, 608-737, Republic of Korea;(4) Division of Food Science and Technology, Kyungnam University, Masan, 631-701, Republic of Korea;(5) Korean Nokyong Research Center, College of Medicine, Konkuk University, Chungju, 380-701, Republic of Korea;(6) Department of Biotechnology, College of Medicine, Konkuk University, Chungju, 380-701, Republic of Korea;(7) Department of Marine Life Science, Marine Life Research Center, Chosun University, Gwangju, 501-759, Republic of Korea |
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Abstract: | Angiotensin I-converting enzyme (ACE) inhibitory peptide was isolated from Styela plicata. The S. plicata was hydrolyzed with various proteases including Protamex, Kojizyme, Neutrase, Flavourzyme, Alcalase, trypsin, α-chymotrypsin,
pepsin, and papain. The hydrolysate prepared with Protamex had the highest ACE inhibitory activity compared to the other hydrolysates.
We attempted to isolate ACE inhibitory peptides from hydrolysate prepared with Protamex using ultra-filtration, gel filtration
on a Sephadex G-25 column and reversed-phase high-performance liquid chromatography (RP-HPLC) on an ODS column. IC50 value of the purified ACE inhibitory peptide was 24.7 μM, and Lineweaver–Burk plots suggest that the purified peptide from
S. plicata acts as mixed-type inhibitor against ACE. Amino acid sequence of the purified peptide was identified as Met-Leu-Leu-Cys-Ser,
with a molecular weight 566.4 Da. The results of this study suggest that peptides derived from S. plicata may be beneficial as anti-hypertension compounds in functional foods resource. |
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