Identification of Antihypertensive Peptides Derived from Low Molecular Weight Casein Hydrolysates Generated during Fermentation by Bifidobacterium longum KACC 91563

Ha, Go Eun; Chang, Oun Ki; Jo, Su-Mi; Han, Gi-Sung; Park, Beom-Young; Ham, Jun-Sang; Jeong, Seok-Geun

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자료유형: 학술저널

저자정보: Ha, Go Eun (Animal Products Research and Development Division, National Institute of Animal Science, RDA) Chang, Oun Ki (Animal Products Research and Development Division, National Institute of Animal Science, RDA) Jo, Su-Mi (Animal Products Research and Development Division, National Institute of Animal Science, RDA) Han, Gi-Sung (Animal Products Research and Development Division, National Institute of Animal Science, RDA) Park, Beom-Young (Animal Products Research and Development Division, National Institute of Animal Science, RDA) Ham, Jun-Sang (Animal Products Research and Development Division, National Institute of Animal Science, RDA) Jeong, Seok-Geun (Animal Products Research and Development Division, National Institute of Animal Science, RDA)

저널정보: 한국축산식품학회 한국축산식품학회지 한국축산식품학회지 제35권 제6호

발행연도: 2015.1

수록면: 738 - 747 (10page)

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Angiotensin-converting enzyme (ACE) inhibitory activity was evaluated for the low-molecular-weight fraction (<3 kDa) obtained from milk fermentation by Bifidobacterium longum KACC91563. The ACE inhibitory activity in this fraction was 62.3%. The peptides generated from the <3 kDa fraction were identified by liquid chromatography-electrospray ionization quantitative time-of-flight mass spectrometry analysis. Of the 28 peptides identified, 11 and 16 were identified as β-casein (CN) and α<sub>s1</sub>-CN, respectively. One peptide was identified as κ-CN. Three peptides, YQEPVLGPVRGPFPIIV, QEPVLGPVRGPFPIIV, and GPVRGPFPIIV, from β-CN corresponded to known antihypertensive peptides. We also found 15 peptides that were identified as potential antihypertensive peptides because they included a known antihypertensive peptide fragment. These peptides were as follows: RELEELNVPGEIVE (f1-14), YQEPVLGPVRGPFP (f193-206), EPVLGPVRGPFPIIV (f195-206), PVLGPVRGPFPIIV (f196-206), VLGPVRGPFPIIV (f197-206), and LGPVRGPFPIIV (f198-206) for β-CN; and APSFSDIPNPIGSENSEKTTMPLW (f176-199), SFSDIPNPIGSENSEKT- TMPLW (f178-199), FSDIPNPIGSENSEKTTMPLW (f179-199), SDIPNPIGSENSEKTTMPLW (f180-199), DIPNPIGSENSEKTTMPLW (f181-199), IPNPIGSENSEKTTMPLW (f182-199), PIGSENSEKTTMPLW (f185-199), IGSENSEKTTMPLW (f186-199), and SENSEKTTMPLW (f188-199) for α<sub>s1</sub>-CN. From these results, B. longum could be used as a starter culture in combination with other lactic acid bacteria in the dairy industry, and/or these peptides could be used in functional food manufacturing as additives for the development of a product with beneficial effects for human health.

#B #longum #antihypertensive peptide #angiotensin converting enzyme

참고문헌 (48)

참고문헌 신청

Arunachalam, K. D. / 1999 / Role of bifidobacteria in nutrition, medicine and technology / Nutr. Res 19:1559~1597

Chang, O. K. / 2014 / Use of a free form of the Streptococcus thermophilus cell envelope protease PrtS as a tool to produce bioactive peptides / Int. Dairy J 38:104~115

Chang, O. K. / 2013 / Casein hydrolysis by Bifidobacterium longum KACC91563 and antioxidant activities of peptides derived therefrom / J. Dairy Sci 96:5544~5555

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Cushman, D. W. / 1971 / Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung / Biochem. Pharmacol 20:1637~1648

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