Effect of digestive enzymes on antimicrobial, radical scavenging and angiotensin I-converting enzyme inhibitory activities of camel colostrum and milk proteins

Jrad, Zeineb; Hatmi, Halima El; Adt, Isabelle; Girardet, Jean‐Michel; Cakir-Kiefer, Céline; Jardin, Julien; Degraeve, Pascal; Khorchani, Touhami; Oulahal, Nadia

doi:10.1007/s13594-013-0154-1

Cited by 67 publications

(61 citation statements)

References 44 publications

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“…Salami et al (2008) reported higher extent of hydrolysis of camel caseins than that of bovine caseins upon treatment with pancreatic enzymes. Antimicrobial, radical-scavenging and angiotensin lconverting enzyme inhibitory activities of camel milk have also been studied by Jrad et al (2014), after hydrolysis by pepsin and pancreatin. Despite that, recent studies suggested that camel milk could have significant therapeutic attributes such as anti-cancer and anti-diabetic properties (Agrawal et al 2003;Magjeed 2005), search for milk-based bioactive peptides has been focused until now mainly on bovine and to smaller extent on ovine and caprine milk proteins.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic hydrolysis of camel milk casein and its antioxidant properties

Kumar

Chatli

Singh

et al. 2016

Dairy Sci. & Technol.

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The aim of this work was to investigate the enzymatic hydrolysis of whole casein from camel milk with proteolytic enzymes, viz. alcalase, α-chymotrypsin and papain, and to assess the antioxidant activity of hydrolysates. Casein powder was reconstituted (5% TS) and the selected enzymes were added at 1:100 (enzyme/substrate). Hydrolysis was carried out for 6 h at 55°C for alcalase and papain and 37°C for α-chymotrypsin, and samples were drawn at 2-h interval. The hydrolysates were analysed for pH, degree of hydrolysis (DH) and antioxidant activities, viz. 2, 2′-azinobis (3-ethylbenzthiazoline-6-sulphonic acid) (ABTS), 2, 2′-diphenyl-1-picrylhydrazyl (DPPH) and ferric reducing antioxidant power (FRAP) assay. The decrease in pH of the hydrolysates was observed with the progress of hydrolysis time, and as compared to alcalase, the rate of pH decrease was higher for α-chymotrypsin and papain. The DH increased significantly (P<0.05) up to 6 h on hydrolysis with alcalase and papain, whereas with chymotrypsinolysis, DH increased significantly (P<0.05) up to 4 h; thereafter, a non-significant increase was observed. The antioxidant activity assessed by ABTS, DPPH and FRAP assay increased significantly (P<0.05) with the increase in hydrolysis time as well as the degree of hydrolysis. The chymotrypsinolysis exhibited higher antioxidant activity as compared to alcalase and papain. The results obtained in this study suggested that camel milk casein could be used as an ingredient in nutraceuticals or health-oriented foods.

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Section: Introductionmentioning

confidence: 99%

Enzymatic hydrolysis of camel milk casein and its antioxidant properties

Kumar

Chatli

Singh

et al. 2016

Dairy Sci. & Technol.

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“…Only few studies have been reported that camel colostrum is rich in bioactives molecules such as antioxydant and antihypertensif peptides released after enzymatic hydrolysis or fermentation of milk (Jrad et al, 2014). Among the bioactive fragments, antimicrobial peptides (AMP) attract the attention of many researchers because the resistance of many pathogenic bacteria to conventional antibiotics.…”

Section: Introductionmentioning

confidence: 99%

Camel colostrum: Nutritional composition and improvement of the antimicrobial activity after enzymatic hydrolysis

Jrad

Oulahal

Adt

et al. 2015

Emir. J. Food Agric

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Camel colostrum collected within 24 h after parturition was analyzed for physicochemical and microbiological composition. The average contents of fats, dry matter, mineral matter and proteins were 1.71±0. 51, 199.55±16.93, 9.75±0.5 and 143.42±36.42 gL -1 , respectively. Microbiological analysis of colostrum samples showed richness in yeasts and Lactic acid bacteria and absence of coliforms. The good microbial quality of camel colostrum is due to a number of antimicrobial molecules such as immunoglobulins and lactoferrin. The antimicrobial activity was evaluated against the pathogens Bacillus cereus, Staphylococcus aureus, Enterococcus faecium and Pseudomonas aeruginosa. At concentration of 20 g L -1 , colostrum caused an important inhibition of growth of all tested bacteria. It therefore seemed interesting to assess whether the compounds inhibit the growth of tested strains present in camel colostrum are resisting to the action of digestive enzymes. An in vitro hydrolysis by pepsin and pancreatin was then conducted. Hydrolyzed camel colostrum was still active against all pathogenic strains with inhibition rate ranging from 15.8% to 24.18%. This finding highlights the presence of antimicrobial fragments/peptides released during proteolytic hydrolysis that may contribute to the antimicrobial activity in camel colostrum and play a significant role in the host defence system.

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“…It has been elucidated that many peptide sequences in milk proteins have angiotensin-converting enzyme (ACE)-inhibitory activity (Jrad et al 2014;Otte et al 2007). The angiotensin I-converting enzyme (ACE, EC 3.4.15.1) is a dipeptidyl carboxypeptidase which regulates the blood pressure (Hooper 1991).…”

Section: Introductionmentioning

confidence: 99%

“…Although the bioactivity of the milk-derived peptides from different sources has been extensively studied, only few attempts have been made to investigate the peptides from camel milk proteins (Jrad et al 2014;Moslehishad et al 2013;Salami et al 2011). Jrad et al (2014) hydrolyzed the camel milk protein by pepsin and pancreatin and evaluated the antioxidant and ACE-inhibitory activities of resulting peptides.…”

Section: Introductionmentioning

confidence: 99%

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ACE- inhibitory and radical scavenging activities of bioactive peptides obtained from camel milk casein hydrolysis with proteinase K

Rahimi

Ghaffari

Salami

et al. 2016

Dairy Sci. & Technol.

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The aim of this study was to evaluate the effects of enzymatic hydrolysis of camel whole casein on their antioxidant and angiotensin-converting enzyme (ACE)-inhibitory properties. Whole camel casein was hydrolyzed by proteinase K (PK), and the hydrolysates were fractionized by ultrafiltration membranes into three fractions. Semi-preparative reversed-phase high-performance liquid chromatography (RP-HPLC) was used to differentiate the mixture of peptides in the 3 kDa permeate fractions. A fraction (F4) with potentials of ACE-inhibitory activity (IC50 = 73 μg.mL −1 ) and radical scavenging activity (IC50 = 6.8 μg.mL −1 ) was selected for further purification and fractionation. The fraction F4C obtained from a second step purification of F4 showed strong ACE-inhibitory activity (IC 50 = 36 μg.mL −1 ) as well as radical scavenging activity (IC 50 = 3.3 μg.mL −1 ). The results of this study suggest that whole camel casein can be considered as a promising source for the production of peptides with potential of ACE-inhibitory and antioxidant activities.

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Effect of digestive enzymes on antimicrobial, radical scavenging and angiotensin I-converting enzyme inhibitory activities of camel colostrum and milk proteins

Cited by 67 publications

References 44 publications

Enzymatic hydrolysis of camel milk casein and its antioxidant properties

Enzymatic hydrolysis of camel milk casein and its antioxidant properties

Camel colostrum: Nutritional composition and improvement of the antimicrobial activity after enzymatic hydrolysis

ACE- inhibitory and radical scavenging activities of bioactive peptides obtained from camel milk casein hydrolysis with proteinase K

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