Purification and identification of angiotensin I-converting enzyme-inhibitory peptides from apalbumin 2 during simulated gastrointestinal digestion

2014 ◽  
Vol 95 (5) ◽  
pp. 906-914 ◽  
Author(s):  
Xiang Xu ◽  
Yanxiang Gao
Keyword(s):  
Converting Enzyme ◽  
Angiotensin I ◽  
Gastrointestinal Digestion ◽  
Inhibitory Peptides ◽  
Simulated Gastrointestinal Digestion ◽  
Angiotensin I Converting Enzyme

Preparation and identification of novel inhibitory angiotensin-I-converting enzyme peptides from tilapia skin gelatin hydrolysates: inhibition kinetics and molecular docking

2018 ◽  
Vol 9 (10) ◽  
pp. 5251-5259 ◽  
Author(s):  
Yuan Ling ◽  
Sun Liping ◽  
Zhuang Yongliang
Keyword(s):  
Molecular Docking ◽  
Cell Monolayer ◽  
Converting Enzyme ◽  
Inhibition Kinetics ◽  
Angiotensin I ◽  
Gastrointestinal Digestion ◽  
Simulated Gastrointestinal Digestion ◽  
Angiotensin I Converting Enzyme

Tilapia skin gelatin was hydrolyzed by successive simulated gastrointestinal digestion, and the hydrolysates were further separated by transport across a Caco-2 cell monolayer.

Effect of simulated gastrointestinal digestion of bioactive peptide from pigeon pea (Cajanus cajan) tempe on angiotensin-I converting enzyme inhibitory activity

2020 ◽  
Vol ahead-of-print (ahead-of-print) ◽  
Author(s):  
Ismail Dwi Putra ◽  
Yustinus Marsono ◽  
Retno Indrati
Keyword(s):  
Small Intestine ◽  
Pigeon Pea ◽  
Bioactive Peptide ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Gastrointestinal Digestion ◽  
Content Type ◽  
Simulated Gastrointestinal Digestion ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Purpose The purpose of this paper is to understand the effect of hydrolysis by pepsin and pancreatin on the angiotensin-I-converting enzyme (ACE) inhibitory activity of bioactive peptide from pigeon pea tempe and the absorption of pigeon pea tempe peptide by using the everted gut sac method. Design/methodology/approach The tempe was prepared by inoculating Raprima (Rhizopus oligosporus) on hulled-cooked pigeon pea for 48 h. The extraction was performed using the ultrasonic method at 40 kHz frequency and 100% ultrasonic power for 10 min. The extracted protein was placed in simulated gastrointestinal digestion using consecutive pepsin–pancreatin for 240 min. The hydrolysates were fractionated using a dialysis tube, and its absorption was assessed using the everted Sprague–Dawley rat gut sac. Findings The tempe protein from the hydrolyzed pigeon pea exhibited higher ACE inhibitory (71.53%) activity than that from the boiled pigeon pea (53.04%) (p = 0.028). The bioactive peptide of the digested pigeon pea tempe consisted of low-molecular-weight peptides (<1 kDa). The fraction also showed the highest ACE inhibition activity among the others (IC50 = 0.61 mg/mL, p = 0.021). Bioactive peptides from pigeon pea tempe were absorbed well in the small intestine, mainly in the jejunum. The activity of the absorbed peptides did not change considerably. Originality/value The activity of bioactive peptide of pigeon pea tempe was comparatively stable during digestion. It exhibited activity even after absorption in the small intestine. Thus, pigeon pea tempe can serve as an antihypertensive peptide source and alternative food for maintaining/reducing blood pressure.

Goat whey fermentation by Kluyveromyces marxianus and Lactobacillus rhamnosus release tryptophan and tryptophan-lactokinin from a cryptic zone of alpha-lactalbumin

2009 ◽  
Vol 76 (3) ◽  
pp. 379-383 ◽  
Author(s):  
Vanessa Hamme ◽  
Frederic Sannier ◽  
Jean-Marie Piot ◽  
Stephanie Bordenave-Juchereau
Keyword(s):  
Affective Disorders ◽  
Kluyveromyces Marxianus ◽  
Fermentation Process ◽  
Lactobacillus Rhamnosus ◽  
Functional Health ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Gastrointestinal Digestion ◽  
Simulated Gastrointestinal Digestion ◽  
Angiotensin I Converting Enzyme

Angiotensin-I-Converting Enzyme (ACE) inhibitors peptides were produced from unsupplemented acid goat whey fermented aerobically for 168 h by Kluyveromyces marxianus and Lactobacillus rhamnosus. This yeast-lactobacillus association is GRAS. Two novel lactokinins were identified: NYW and W with IC50 of 20 and 0·86 μm respectively. They both were resistant toward simulated gastrointestinal digestion. In addition, WLAHK was found in the hydrolysate. These three sequences belong to f(99–110) of α-la which seems to be a lactokinin cryptic zone. W was the major molecule released by the fermentation process. Considering that W is the precursor of serotonin, the hydrolysate produced could be of interest for the generation of functional health ingredient involved in regulation of affective disorders and hypertension.

Sign in / Sign up

Export Citation Format

Share Document