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

Li, Guanhong; Li, Guowei; Shi, Yonghui; Shrestha, Shankar Prasad

doi:10.1016/j.nutres.2003.10.014

Cited by 257 publications

(322 citation statements)

References 116 publications

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“…Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity ACE-inhibitory peptides are present in the primary structure of various food protein sources including milk proteins [50,69,80,81]. These peptides are also found in fermented camel milk [86].…”

Section: Protection Against Lead Contaminationmentioning

confidence: 99%

Camel Milk: An Important Natural Adjuvant

et al. 2017

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One humped camel (Camelus dromedarius) breeds, indigenous to India, have been shown to have good genetic potential to produce milk. Camel milk not only is cost-effective in terms of feed conversion but also has additional advantage of longer lactation period and unique adaptation mechanisms for warm arid and semiarid regions. The key features of camel milk in comparison with other milk are low fat with high content of unsaturated and long-chain fatty acid. The proteins are rich in lactoferrin and lysozymes, but deficient in b-lactoglobulin. It has higher percentage of total salts, free calcium, protective proteins and vitamin C, and some of the microminerals, viz iron, copper and zinc. Physicochemical properties of camel milk are also unique and useful for food processing. The shelf life of raw camel milk is 8-9 h, which can be extended up to 18-20 h through activation of camel lactoperoxidase system. Heat stability of camel milk is shown to be highest at pH 6.8, and it ferments relatively slowly compared to the cattle milk. The camel milk is successfully processed for producing a variety of products, such as fermented milk ('lassi'), soft cheese, flavored milk and 'kulfee' (a kind of ice cream). Camel milk has been traditionally used in different regions of the world as natural adjuvant for managing a variety of human diseases.

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Section: Protection Against Lead Contaminationmentioning

confidence: 99%

Camel Milk: An Important Natural Adjuvant

et al. 2017

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“…So it could be assumed that among the released terminal amino acids, Arg and Lys were involved in the ACE inhibition. It has been reported that positively charged amino acids at the ultimate C-terminal position such as Arg (guanidine group) and Lys (ε-amino group) appear to effectively inhibit ACE (Li et al [24]). Chobert et al [25] found that the ACE-inhibiting activity of tryptic hydrolysates of ovine β-lactoglobulin increased with the degree of hydrolysis.…”

Section: Ace-inhibiting Activity Of Crude Hydrolysates Formed By Trypsinmentioning

confidence: 99%

Hypocholesterolemic and Angiotensin I Converting Enzyme-Inhibiting Activity of Trypsin-Hydrolysed Bovine Casein

Oa¹,

Irshad²,

Ad³

2016

JNHFE

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Bovine casein solution was hydrolysed by trypsin for 4 h at a ratio of 1:100. Throughout the experiment, the solution temperature and pH were maintained at 37°C and 7.5, respectively. AbstractNowadays, the need for new dietary containing some bioactive peptides with specific amino acid sequences increased to express biological functions. We investigated the hypocholesterolemic effect and ACE-inhibiting activity of bovine casein hydrolysates with different molecular weights. The bovine casein was hydrolysed with trypsin for different amounts of time to release bioactive peptides from the casein. Then, crude casein hydrolysate was ultrafiltered using membranes with two different molecular-weight cut offs (1 kDa and 10k Da) to determine the hypocholesterolemic effects and ACE-inhibiting activities of peptides with different molecular weights. The results showed that a higher level of hydrolysis (more active bioactive peptides) was associated with greater hypocholesterolemic and ACE-inhibiting effects in all the tested samples. The unhydrolysed crude casein reduced the cholesterol level in orthophthaldialdehyde (OPA) assays by 39.5%, while the 10 kDa and 1 kDa permeates of casein hydrolysed with trypsin for 4 h reduced the cholesterol level by 50.7 and 69.6%, respectively. The unhydrolysed crude casein and the 10 kDa and 1 kDa permeates of casein hydrolysed by trypsin for 4 h inhibited ACE activity by 18.9%, 29.7%, and 51.4%, respectively.

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“…ACE-inhibition of the peptides is correlated with their primary peptide structure, as the peptides will bind to the active site of ACE (Li et al 2004). It seems that amino acids (esp.…”

Section: Plastein Reaction Of Casein Hydrolysate and Its Impact On Acmentioning

confidence: 99%

“…TCH1-4) thus would contain some new peptides generated from the plastein reaction with different amino acid sequences from their parent peptides, and thus would have higher inhibition towards ACE. ACE-inhibitory peptides usually contain 2-12 amino acid residues (Li et al 2004). When the plastein reaction was carried out for a too long time, the peptides in the treated hydrolysate were too much condensed (i.e.…”

Section: Plastein Reaction Of Casein Hydrolysate and Its Impact On Acmentioning

confidence: 99%

“…Angiotensin I-converting enzyme (ACE, EC 3.4.15.1) converts inactive decapeptide angiotensin I by cleaving a dipeptide from C-terminal into octapeptide angiotensin II, which has a tendency to increase the blood pressure (Li et al 2004). Food protein-derived peptides are suggested as potential alternatives to ACE inhibitor drugs (Ni et al 2012), and now are well-known as so-called ACE-inhibitory peptides.…”

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confidence: 99%

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Properties of casein hydrolysate as affected by plastein reaction in ethanol-water medium

Zhang¹,

Zhao²

2013

Czech J. Food Sci.

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Zhang Y., Zhao X.-H. (2013): Properties of casein hydrolysate as affected by plastein reaction in ethanol-water medium. Czech J. Food Sci., 31: 559-567.Casein hydrolysate with in vitro ACE-inhibitory activity of 44.4% at 0.3 mg/ml was generated from casein by Alcalase and modified by the Alcalase-catalysed plastein reaction in an ethanol-water medium. Eight treated hydrolysates were prepared using the reaction time of 1-8 h under ethanol or substrate concentration, Alcalase addition and reaction temperature of 56.8% (v/v) or 56.8% (w/v), 8.4 kU/g peptides and 37.5°C, respectively. Most of the treated hydrolysates showed enhanced ACE-inhibition compared to casein hydrolysate, and a reaction time of 4 h brought about the highest ACE-inhibition. All treated hydrolysates had lower zinc-or calcium-chelation but slightly higher iron(II)-chelation than casein hydrolysate, and a reaction time of 4 or 2 h could grant the treated hydrolysates the highest zinc-or calcium-chelation. Kinetic evaluation indicated that casein hydrolysate and two treated hydrolysates were competitive inhibitors to ACE. ACE-inhibition of these evaluated hydrolysates originated from themselves but was uncorrelated with their zinc-chelation, while their CaCO 3 precipitation inhibition was clearly correlated with their measured calcium-chelation (P < 0.05).

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

Cited by 257 publications

References 116 publications

Camel Milk: An Important Natural Adjuvant

Camel Milk: An Important Natural Adjuvant

Hypocholesterolemic and Angiotensin I Converting Enzyme-Inhibiting Activity of Trypsin-Hydrolysed Bovine Casein

Properties of casein hydrolysate as affected by plastein reaction in ethanol-water medium

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