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

Korean Journal for Food Science of Animal Resources
Go Eun HaSeok-Geun Jeong

Abstract

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 αs1-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), PIGSENSEKT...Continue Reading

References

Jul 1, 1971·Biochemical Pharmacology·D W Cushman, H S Cheung
Jan 1, 1982·Medicinal Research Reviews·E W Petrillo, M A Ondetti
May 8, 1999·The American Journal of Clinical Nutrition·M D Collins, G R Gibson
May 3, 2000·Journal of Dairy Science·R H DavidsonJ W Boling
Jun 13, 2002·Critical Reviews in Food Science and Nutrition·M GobbettiR Di Cagno
Jan 30, 2004·The American Journal of Clinical Nutrition·Jose M SaavedraRobert H Yolken
May 27, 2005·Journal of Applied Microbiology·S C LeahyD van Sinderen
Mar 17, 2009·Applied and Environmental Microbiology·M GenayS Lortal
Jun 9, 2009·International Journal of Food Microbiology·Lorena RuizAbelardo Margolles
Mar 1, 2011·International Journal of Food Microbiology·Leila Sadat-MekmeneValérie Gagnaire
Jul 12, 2011·Journal of Bacteriology·Jun-Sang HamHeebal Kim
Oct 19, 2013·International Journal of Food Microbiology·Cid Gonzalez-GonzalezPaula Jauregi
Jul 23, 2014·Asian-Australasian Journal of Animal Sciences·M A IslamG E Vegarud

❮ Previous
Next ❯

Citations

Oct 21, 2017·Journal of Food Science and Technology·Katarzyna SkrzypczakAdam Waśko
Mar 9, 2018·Analytical and Bioanalytical Chemistry·Dominic AgyeiChibuike C Udenigwe
Jul 28, 2017·Korean Journal for Food Science of Animal Resources·Sang Hoon KimDae-Kyung Kang
Nov 30, 2018·Food Science and Biotechnology·Eric Banan-Mwine DaliriDeog-Hwan Oh
Jun 13, 2017·Critical Reviews in Food Science and Nutrition·Eric Banan-Mwine DaliriDeog H Oh
Nov 26, 2020·International Journal of Molecular Sciences·Akanksha TyagiDeog-Hwan Oh
Dec 19, 2020·Comprehensive Reviews in Food Science and Food Safety·Kong Fei ChaiWei Ning Chen
Mar 12, 2020·Journal of Agricultural and Food Chemistry·Fidel ToldráLeticia Mora

❮ Previous
Next ❯

Methods Mentioned

BETA
MDS

Software Mentioned

Analyst QS

Related Concepts

Related Feeds

Antihypertensive Agents: Mechanisms of Action

Antihypertensive drugs are used to treat hypertension (high blood pressure) which aims to prevent the complications of high blood pressure, such as stroke and myocardial infarction. Discover the latest research on antihypertensive drugs and their mechanism of action here.

Barrel cortex

Here is the latest research on barrel cortex, a region of somatosensory and motor corticies in the brain, which are used by animals that rely on whiskers for world exploration.