Angiotensin I–converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects

LI, G; Le, Guo; Shi, Yonghui; Shrestha, Shankar Prasad

doi:10.1016/s0271-5317(04)00058-2

Cited by 374 publications

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“…Moreover, all identified ACE-inhibitory peptides were corresponding to β-casein of C. dromedarius milk and contain at least one proline (P) residue at the C-terminal position (Table 1). This property is favorable and more effective in ACE-inhibitory activity compared to other hydrophobic amino acids as reported by Li et al (2004) and López-Expósito et al (2006). On the other hand, tyrosine (Y) and arginine (R) were detected at the ultimate C-terminal position of camel milk fermented with S1 or S2 samples.…”

Section: Sequences Of Ace-inhibitory Precursor Peptidesmentioning

confidence: 59%

“…The oral ingestion of these low molecular peptides has neither side effect nor causes significant changes in the blood pressure of normotensive subjects (Meisel et al, 2006;Takano, 2002). It has been reported (Li, Le, Shi, Shrestha, 2004) that there is a relationship between structure-activity of ACEinhibitory peptide and ACE-inhibitory activity. Only ACE-inhibitory peptides that able to bind to the active site of ACE enzyme are that inhibit ACE activity.…”

Section: Introductionmentioning

confidence: 99%

“…ACE enzyme is only known to have weak binding to peptides having C-terminal dicarboxylic amino acids such as Glutamic acid (E) and Aspartic acid (D) (Cheung, Wang, Ondetti, Sabo, Cushman, 1980). On the other hand, amino acids having hydrophobic properties such as tryptophan (W), phenylalanine (F), tyrosine (Y) and especially proline (P) were found to be favorable and more effective when present at each of the three C-terminal positions (Li et al, 2004;López-Expósito et al, 2006). Moreover, ACE-inhibitory peptides with a positively charged amino acid at the ultimate C-terminal residue such as arginine (guanidine group) and lysine (ε-amino group) would appear to contribute substantially to inhibitory potency (Li et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

“…On the other hand, amino acids having hydrophobic properties such as tryptophan (W), phenylalanine (F), tyrosine (Y) and especially proline (P) were found to be favorable and more effective when present at each of the three C-terminal positions (Li et al, 2004;López-Expósito et al, 2006). Moreover, ACE-inhibitory peptides with a positively charged amino acid at the ultimate C-terminal residue such as arginine (guanidine group) and lysine (ε-amino group) would appear to contribute substantially to inhibitory potency (Li et al, 2004). The information about the ACEinhibitory sequence of peptides generated after hydrolysis of camel milk with L. helveticus or Lactobacillus acidophilus in the literature is not abundant.…”

Section: Introductionmentioning

confidence: 99%

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Identification of potential ACE-inhibitory peptides from dromedary fermented camel milk

Alhaj

2016

CyTA - Journal of Food

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To cite this article: Omar Amin Alhaj (2017) Identification of potential ACE-inhibitory peptides from dromedary fermented camel milk, CyTA -Journal of Food, 15:2, 191-195, DOI: 10.1080/19476337.2016 Camel milk is a good nutritional source for people living in the arid and urban areas. This study aim to identify ACE-inhibitory peptides from dromedary camel milk produced using Lactobacillus helveticus or Lactobacillus acidophilus. Ten ACE-inhibitory peptides were identified using HPLC-MALDI-TOF MS. L. helveticus strain was found superior in respect to production of ACE-inhibitory peptides, compared with L. acidophilus due to having high proteolytic activity. However, all identified amino acid sequences were corresponding to β-casein of camel milk (Camelus dromedarius). Furthermore, molecular mass of identified peptides were below 1200 Da. Some ACE-inhibitory peptides were found to remain stable for up to 15 d of storage.Identificación de los péptidos inhibidores de ACE potenciales en leche fermentada de dromedario RESUMEN La leche de camello se trata de una rica fuente nutricional para las personas que viven en áreas áridas y urbanas. Este estudio pretende identificar los péptidos inhibidores de ACE en la leche de dromedario producida utilizando Lactobacillus helveticus o Lactobacillus acidophilus. Se identificaron diez péptidos inhibidores de ACE utilizando HPLC-MALDI-TOF MS. Se encontró que la cepa de L. helveticus era superior respecto a la producción de péptidos inhibidores de ACE, en comparación con L. acidophilus, debido a su mayor actividad proteolítica. Sin embargo, todas las secuencias de aminoácidos que se identificaron se correspondieron a Caseína β de leche de camello (Camelus dromedarius). Además, la masa molecular de los péptidos identificados resultó por debajo de 1200 Da. Se encontró que algunos péptidos inhibidores de ACE se mantuvieron estables hasta 15 días de almacenamiento. ARTICLE HISTORY

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Section: Sequences Of Ace-inhibitory Precursor Peptidesmentioning

confidence: 59%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Identification of potential ACE-inhibitory peptides from dromedary fermented camel milk

Alhaj

2016

CyTA - Journal of Food

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“…In addition, oxidative damage plays a significant role in the number of age-specific diseases, such as atherosclerosis, diabetes, rheumatoid arthritis, Alzheimer’s disease and cancer (Halliwell, 2001; Hoelzl et al , 2005; Korhonen and Pihlanto-Leppälä et al , 2007b). Therefore antioxidant peptides can then be utilized as an excellent source of natural ingredients to develop functional foods that may enhance physiological and metabolic functions or condition of the body to benefit the host (Clare et al , 2003; FitzGerald and Meisel, 2003; Kitts and Weiler, 2003; Li et al , 2004). …”

Section: Introductionmentioning

confidence: 99%

Identification and Characterization of a Novel Antioxidant Peptide from Bovine Skim Milk Fermented by Lactococcus lactis SL6

Kim¹,

Lee²,

Balolong³

et al. 2017

Korean Journal for Food Science of Animal Resources

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A novel peptide having free radical scavenging activity was separated, using an on-line high-performance liquid chromatography (HPLC) - ABTS screening method, from bovine skim milk fermented by Lactococcus lactis SL6 (KCTC 11865BP). It was further purified using reverse phase-HPLC (RP-HPLC) and sequenced by RP-HPLC-tandem mass spectrometry. The amino acid sequence of the identified peptide was determined to be Phe-Ser-Asp-Ile-Pro-Asn-Pro-Ile-Gly-Ser-Glu-Asn-Ser-Glu-Lys-Thr-Thr-Met-Pro-Leu-Trp (2,362 Da), which is corresponding to the C-terminal fragment of bovine αs1-casein (f179-199). The hydroxyl radicals scavenging activity (IC50 28.25±0.96 μM) of the peptide chemically synthesized based on the MS/MS data showed a slightly lower than that of the natural antioxidant Trolox (IC50 15.37±0.52 μM). Furthermore, derivatives of the antioxidant peptide were synthesized. The antioxidative activity of the derivatives whose all three proline residues replaced by alanine significantly decreased, whereas replacement of two proline residues in N-terminal region did not affect its antioxidative activity, indicating that 3rd proline in C-terminal region is critical for the antioxidative activity of the peptide identified in this study. In addition, N-terminal region of the antioxidant peptide did not show its activity, whereas C-terminal region maintained antioxidative activity, suggesting that C-terminal region of the peptide is important for antioxidative activity.

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Bioactive Components in Goat Milk

Park

2009

Bioactive Components in Milk and Dairy Products

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Angiotensin I–converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects

Cited by 374 publications

References 0 publications

Identification of potential ACE-inhibitory peptides from dromedary fermented camel milk

Identification of potential ACE-inhibitory peptides from dromedary fermented camel milk

Identification and Characterization of a Novel Antioxidant Peptide from Bovine Skim Milk Fermented by Lactococcus lactis SL6

Bioactive Components in Goat Milk

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