Angiotensin I converting enzyme (ACE) inhibitory activity and antihypertensive effect of fermented milk

Pihlanto, Anne; Virtanen, Tarja; Korhonen, Hannu J. T.

doi:10.1016/j.idairyj.2009.07.003

Cited by 159 publications

(104 citation statements)

References 34 publications

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“…Fermented milk products prepared using different strains of lactic acid bacteria have been found to exert antihypertensive and antioxidative activities [71,72]. Moreover, several antioxidative and ACE-inhibitory peptide sequences have been identified from fermented milk [73].…”

Section: Production Of Peptidesmentioning

confidence: 99%

Antihypertensive Properties of Plant Protein Derived Peptides

Pihlanto¹,

Mäkinen²

2013

Bioactive Food Peptides in Health and Disease

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Section: Production Of Peptidesmentioning

confidence: 99%

Antihypertensive Properties of Plant Protein Derived Peptides

Pihlanto¹,

Mäkinen²

2013

Bioactive Food Peptides in Health and Disease

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“…Proteolysis is known to be one of the most important biochemical process occuring during fermentation. In addition, it is accepted that strong proteolytic activity is required to produce ACE inhibitory and antihypertensive peptides (Pihlanto et al 2010). The greater inhibitory activity of yoghurts supplemented with WPC can be attributed to the proteolytic activity of L. delbrueckii subsp.…”

Section: Ace Inhibitory Activitymentioning

confidence: 99%

Antioxidant and angiotensin-converting enzyme inhibitory activity of yoghurt fortified with sodium calcium caseinate or whey protein concentrate

Ünal

Akalın

2012

Dairy Sci. & Technol.

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In this study, the effect of fortification of yoghurt with sodium calcium caseinate (SCC) and whey protein concentrate (WPC) on the antioxidant and angiotensin-converting enzyme (ACE) inhibitory activity was assessed. Milk was fortified with skim milk powder (SMP) as control, SCC, and WPC at 2% and 4% ratios. The antioxidant activity was determined using 2,2,-diphenyl-1-picrylhydrazyl (DPPH • ) radical scavenging, hydrogen peroxide (H 2 O 2 ) scavenging, and Fe 2+ chelating activity methods. Yoghurt fortified with 4% WPC had the highest DPPH• scavenging activity, whereas there were no significant differences between yoghurt samples containing SMP and SCC at both fortification levels. In the Fe 2+ chelating activity method, increase in incubation time (from 0 to 60 min, at room temperature) significantly improved the chelating effect of all yoghurt types. Yoghurts supplemented with WPC and 4% SMP showed higher Fe 2+ chelating activity than those fortified with SCC for all incubation times. Experimental yoghurts also possessed antioxidant activity towards H 2 O 2 except yoghurts fortified with WPC at a concentration of 0.2 g mL −1 . Yoghurt containing 4% WPC showed higher H 2 O 2 -scavenging activity than those supplemented with 4% SCC at 0.05 and 0.1 g mLconcentrations, at 0 and 40 min. Addition of SCC or WPC caused an increase in the ACE inhibitory activity of yoghurt when compared to supplementation with SMP. Fortification of yoghurt with WPC was more effective than that of with SCC in terms of ACE inhibitory activity.

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“…Milk proteins are particularly good sources of ACE-inhibitory peptides and had been widely studied in the past (da Costa et al 2007;López-Fandiño et al 2006;Miguel et al 2009;Ortiz-Chao et al 2009). To obtain the peptides with high ACE-inhibitory activity, a lot of works have been carried out by in vitro enzymatic hydrolysis ) or fermentation (Pihlanto et al 2010) of food proteins. For example, two powerful ACEinhibitory peptides, IPP and VPP with IC 50 values of 5 and 9 μmol⋅L −1 , respectively, were obtained from the commercial fermented milk products or milk protein hydrolysates Nakamura et al 1995).…”

Section: Introductionmentioning

confidence: 99%

Optimization of some conditions of Neutrase-catalyzed plastein reaction to mediate ACE-inhibitory activity in vitro of casein hydrolysate prepared by Neutrase

Kong

Zhao

2011

J Food Sci Technol

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Casein hydrolysate was prepared by hydrolyzing casein with Neutrase and then modified by a Neutrasecatalyzed plastein reaction. The prepared hydrolysate had a degree of hydrolysis of 13.0% and exhibited ACE inhibition in vitro with an IC 50 value of 40.4 μg⋅mL −1 . With the decreased amount of free amino groups of the modified hydrolysate as the response, some conditions of the plastein reaction including substrate concentration, enzyme to substrate ratio, reaction temperature and time were studied by single factor experiments and response surface methodology, and optimized finally as 62% (w/w), 3.0 kU⋅g −1 peptides, 30°C and 6.3 h, respectively. The maximum decreased amount of free amino groups of the modified hydrolysate prepared under these optimized conditions was 210.0 μmol⋅g −1 peptides, while corresponding IC 50 value was lowered to 14.7 μg⋅mL −1 . The present result indicates that Neutrase-catalyzed plastein reaction was capable of enhancing ACE-inhibitory activity in vitro of casein hydrolysate, and also highlights the importance of a forthcoming study to investigate the peptide compositions of the modified hydrolysate and the role of protease used in the plastein reaction.

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Angiotensin I converting enzyme (ACE) inhibitory activity and antihypertensive effect of fermented milk

Cited by 159 publications

References 34 publications

Antihypertensive Properties of Plant Protein Derived Peptides

Antihypertensive Properties of Plant Protein Derived Peptides

Antioxidant and angiotensin-converting enzyme inhibitory activity of yoghurt fortified with sodium calcium caseinate or whey protein concentrate

Optimization of some conditions of Neutrase-catalyzed plastein reaction to mediate ACE-inhibitory activity in vitro of casein hydrolysate prepared by Neutrase

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