NDLI: Purification of Angiotensin I-Converting Enzyme Inhibitory Peptide from Squid Todarodes pacificus Skin

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Purification of Angiotensin I-Converting Enzyme Inhibitory Peptide from Squid Todarodes pacificus Skin

Content Provider	Semantic Scholar
Author	Lee, Jung Kwon Jeon, Joong-Kyun Byun, Hee-Guk
Copyright Year	2011
Abstract	In this study, an angiotensin I-converting enzyme (ACE) inhibitor from squid skin was purified and characterized. Squid (Todarodes pacificus) skin protein isolates were hydrolyzed using six commercial proteases: alcalase, -chymotrypsin, neutrase, papain, pepsin, and trypsin. The peptic hydrolysate had the highest ACE inhibitory activity. The ACE inhibitory peptide was purified using Sephadex G-25 column chromatography and reverse phase high-performance liquid chromatography (HPLC) with a column. The purified ACE inhibitory peptide was identified and sequenced, and found to consist of seven amino acid residues: Ser-Ala-Gly-Ser-Leu-Val-Pro (657Da). The value of the purified ACE inhibitory peptide was 766.2 , and Lineweaver-Burk plots suggested that the purified peptide acts as a noncompetitive ACE inhibitor. These results suggest that the ACE inhibitory peptide purified from the peptic hydrolysate of squid skin may be of benefit in developing antihypertensive drugs and functional foods.
Starting Page	118
Ending Page	125
Page Count	8
File Format	PDF HTM / HTML
DOI	10.5657/kfas.2011.44.2.118
Volume Number	44
Alternate Webpage(s)	http://ocean.kisti.re.kr/downfile/volume/kofis/KSSHBC/2011/v44n2/KSSHBC_2011_v44n2_118.pdf
Alternate Webpage(s)	https://doi.org/10.5657/kfas.2011.44.2.118
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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