Hostname: page-component-586b7cd67f-tf8b9 Total loading time: 0 Render date: 2024-11-24T07:47:32.779Z Has data issue: false hasContentIssue false
  • English
  • Français

Biological activity of camel milk casein following enzymatic digestion

Published online by Cambridge University Press:  13 September 2011

Maryam Salami ,
Ali Akbar Moosavi-Movahedi ,
Faezeh Moosavi-Movahedi ,
Mohammad Reza Ehsani ,
Reza Yousefi ,
Mohammad Farhadi ,
Amir Niasari-Naslaji ,
Ali Akbar Saboury ,
Jean-Marc Chobert  and
Thomas Haertlé
Maryam Salami
Affiliation:
Institute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran, Iran
Ali Akbar Moosavi-Movahedi*
Affiliation:
Institute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran, Iran Center of Excellence in Biothermodynamics, IBB, University of Tehran, Tehran, Iran
Faezeh Moosavi-Movahedi
Affiliation:
Institute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran, Iran
Mohammad Reza Ehsani
Affiliation:
Department of Food Science and Engineering, College of Agriculture and Natural Resources, University of Tehran, Karaj, Iran
Reza Yousefi
Affiliation:
Protein Chemistry Laboratory (PCL), Department of Biology, College of Sciences, Shiraz University, Shiraz, Iran
Mohammad Farhadi
Affiliation:
ENT-HNS Research Center and Department, Tehran University of Medical Science, Tehran, Iran
Amir Niasari-Naslaji
Affiliation:
Department of Clinical Sciences, Faculty of Veterinary Medicine, University of Tehran, Tehran, Iran
Ali Akbar Saboury
Affiliation:
Institute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran, Iran Center of Excellence in Biothermodynamics, IBB, University of Tehran, Tehran, Iran
Jean-Marc Chobert
Affiliation:
UR 1268 Biopolymères Interactions Assemblages, INRA, équipe Fonctions et Interactions des Protéines, B.P. 71627, 44316 Nantes, Cedex 3, France
Thomas Haertlé
Affiliation:
UR 1268 Biopolymères Interactions Assemblages, INRA, équipe Fonctions et Interactions des Protéines, B.P. 71627, 44316 Nantes, Cedex 3, France
*
*For correspondence; e-mail: [email protected]
Get access Rights & Permissions [Opens in a new window]

Abstract

The aim of this study was to investigate the effects of enzymatic hydrolysis with digestive enzymes of camel whole casein and beta-casein (β-CN) on their antioxidant and Angiotensin Converting Enzyme (ACE)-inhibitory properties. Peptides in each hydrolysate were fractionated with ultra-filtration membranes. The antioxidant activity was determined using a Trolox equivalent antioxidant capacity (TEAC) scale. After enzymatic hydrolysis, both antioxidant and ACE-inhibitory activities of camel whole casein and camel β-CN were enhanced. Camel whole casein and β-CN showed significant ACE-inhibitory activities after hydrolysis with pepsin alone and after pepsinolysis followed by trypsinolysis and chymotrypsinolysis. Camel β-CN showed high antioxidant activity after hydrolysis with chymotrypsin. The results of this study suggest that when camel milk is consumed and digested, the produced peptides start to act as natural antioxidants and ACE-inhibitors.

Keywords

Camel milkcaseinproteolysisACEantioxidant
Type
Research Article
Information
Journal of Dairy Research , Volume 78 , Issue 4 , November 2011 , pp. 471 - 478
Copyright
Copyright © Proprietors of Journal of Dairy Research 2011

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Abd El-Salam, MH, El-Shibiny, S & Buchheim, W 1996 Characteristics and potential uses of the casein macropeptide. International Dairy Journal 6 327–341Google Scholar
Abuja, PM & Albertini, R 2001 Methods for monitoring oxidative stress, lipid peroxidation and oxidation resistance of lipoproteins. Clinica Chimica Acta 306 1–17Google Scholar
Agrawal, RP, Swami, SC, Beniwal, R, Kochar, DK, Sahani, MS, Tuteja, FC & Ghouri, SK 2003 Effect of camel milk on glycemic control, risk factors and diabetes quality of life in type-1 diabetes: a randomised prospective controlled study. Journal of Camel Practice and Research 10 45–50Google Scholar
Aimutis, WR 2004 Bioactive properties of milk proteins with particular focus on anticariogenesis. Journal of Nutrition 134 S989–S995Google Scholar
Arcan, I & Yemenicioğlu, A 2007 Antioxidant activity of protein extracts from heat-treated or thermally processed chickpeas and white beans. Food Chemistry 103 301–312CrossRefGoogle Scholar
Barzegar, A, Yousefi, R, Sharifzadeh, A, Dalgalarrondo, M, Chobert, JM, Ganjali, MR, Norouzi, P, Ehsani, MR, Niasari-Naslaji, A, Saboury, AA, Haertlé, T & Moosavi-Movahedi, AA 2008 Chaperone activities of bovine and camel β-caseins: importance of their surface hydrophobicity in protection against alcohol dehydrogenase aggregation. International Journal of Biological Macromolecules 42 392–399CrossRefGoogle ScholarPubMed
Cheung, HS, Wang, FL, Ondetti, MA, Sabo, EF & Cushman, DW 1980 Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence. Journal of Biological Chemistry 255 401–407Google Scholar
Clare, DA & Swaisgood, HE 2000 Bioactive milk peptides: a prospectus. Journal of Dairy Science 83 1187–1195CrossRefGoogle ScholarPubMed
Collins, AR 2005 Antioxidant intervention as a route to cancer prevention. European Journal of Cancer 41 1923–1930Google Scholar
El-Hatmi, H, Girardet, JM, Gaillard, JL, Yahyaoui, MH & Attia, H 2007 Characterisation of whey proteins of camel (Camelus dromedarius) milk and colostrum. Small Ruminant Research 70 267–271CrossRefGoogle Scholar
Elias, RJ, Kellerby, SS & Decker, EA 2008 Antioxidant activity of proteins and peptides. Critical Reviews in Food Science and Nutrition 48 430–441CrossRefGoogle ScholarPubMed
Elias, RJ, McClements, DJ & Decker, EA 2005 Antioxidant activity of cysteine, tryptophan, and methionine residues in continuous phase β-lactoglobulin in oil-in-water emulsions. Journal of Agricultural and Food Chemistry 53 10248–10253CrossRefGoogle ScholarPubMed
Fiat, AM, Migliore-Samour, D, Jollès, P, Drouet, L, Sollier, CB & Caen, J 1993 Biologically active peptides from milk proteins with emphasis on two examples concerning antithrombotic and immunomodulating activities. Journal of Dairy Science 76 301–310Google Scholar
Gómez-Ruiz, JA, Ramos, M & Recio, I 2004 Angiotensin converting enzyme-inhibitory activity of peptides isolated from Manchego cheese. Stability under simulated gastrointestinal digestion. International Dairy Journal 14 1075–1080CrossRefGoogle Scholar
Halliwell, B 2001 Role of free radicals in the neurodegenerative diseases: therapeutic implications for antioxidant treatment. Drugs and Aging 18 685–716CrossRefGoogle ScholarPubMed
Harjanne, A 1984 Automated kinetic determination of angiotensin-converting enzyme in serum. Clinical Chemistry 30 901–902CrossRefGoogle ScholarPubMed
Holt, C 1997 The milk salts and their interaction with casein. In: Advanced Dairy Chemistry, 2nd Edition (Ed. Fox, PF). London, UK: Chapman & HallGoogle Scholar
Huth, PJ, Layman, DK & Brown, PH 2004 The emerging role of dairy proteins and bioactive peptides in nutrition and health: foreword. Journal of Nutrition 134 961SCrossRefGoogle Scholar
Imondi, AR & Stradley, RP 1974 Utilization of enzymatically hydrolyzed soybean protein and crystalline amino acid diets by rats with exocrine pancreatic insufficiency. Journal of Nutrition 104 793–801CrossRefGoogle ScholarPubMed
Jung, MY, Kim, SK & Kim, SY 1995 Riboflavin-sensitized photooxidation of ascorbic acid: kinetics and amino acid effects. Food Chemistry 53 397–403CrossRefGoogle Scholar
Kappeler, SR, Farah, Z & Puhan, Z 2003 5′-Flanking regions of camel milk genes are highly similar to homologue regions of other species and can be divided into two distinct groups. Journal of Dairy Science 86 498–508CrossRefGoogle ScholarPubMed
Kauf, ACW & Kensinger, RS 2002 Purification of porcine β-casein, N-terminal sequence, quantification in mastitic milk. Journal of Animal Science 80 1863–1870CrossRefGoogle ScholarPubMed
Liu, Q, Raina, AK, Smith, MA, Sayre, LM & Perry, G 2003 Hydroxynonenal, toxic carbonyls, and Alzheimer disease. Molecular Aspects of Medicine 24 305–313CrossRefGoogle ScholarPubMed
López-Expósito, I, Quirós, A, Amigo, L & Recio, I 2007 Casein hydrolysates as a source of antimicrobial, antioxidant and antihypertensive peptides. Lait 87 241–249Google Scholar
López-Fandiño, R, Otte, J & van Camp, J 2006 Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity. International Dairy Journal 16 1277–1293CrossRefGoogle Scholar
Magjeed, NA 2005 Corrective effect of camel milk on some cancer biomarkers in blood of rats intoxicated with aflatoxin B1. Journal of the Saudi Chemical Society 9 253–263Google Scholar
Marshall, T & Williams, KM 1993 Bradford protein assay and the transition from an insoluble to a soluble dye complex: effects of sodium dodecyl sulphate and other additives. Journal of Biochemical and Biophysical Methods 26 237–240Google Scholar
Maruyama, S 1982 A peptide inhibitor of angiotensin I- converting enzyme in the tryptic hydrolysate of casein. Agricultural and Biological Chemistry 46 1393–1394Google Scholar
McLachlan, CNS 2001 β-casein A1, ischaemic heart disease mortality, and other illnesses. Medical Hypotheses 56 262–272CrossRefGoogle ScholarPubMed
Meisel, H 1998 Overview on milk protein-derived peptides. International Dairy Journal 8 363–373CrossRefGoogle Scholar
Meisel, H 2004 Multifunctional peptides encrypted in milk proteins. BioFactors 21 55–61Google Scholar
Meisel, H 2005 Biochemical properties of peptides encrypted in bovine milk proteins. Current Medicinal Chemistry 12 1905–1919CrossRefGoogle ScholarPubMed
Minervini, F, Algaron, F, Rizzello, CG, Fox, PF, Monnet, V & Gobbetti, M 2003 Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species. Applied and Environmental Microbiology 69 5297–5305CrossRefGoogle ScholarPubMed
Okada, Y & Okada, M 1998 Scavenging effect of water soluble proteins in broad beans on free radicals and active oxygen species. Journal of Agricultural and Food Chemistry 46 401–406Google Scholar
Otte, J, Shalaby, SM, Zakora, M, Pripp, AH & El-Shabrawy, SA 2007 Angiotensin-converting enzyme inhibitory activity of milk protein hydrolysates: effect of substrate, enzyme and time of hydrolysis. International Dairy Journal 17 488–503Google Scholar
Pescuma, M, Hébert, EM, Rabesona, H, Drouet, M, Choiset, Y, Haertlé, T, Mozzi, F, Font de Valdez, G & Chobert, JM 2011 Proteolytic action/activity of Lactobacillus delbrueckii subsp. bulgaricus CRL 656 reduces antigenic response to bovine β-lactoglobulin. Food Chemistry 127 487–492Google Scholar
Pihlanto-Leppälä, A, Koskinen, P, Phlola, K, Tupasela, T & Korhonen, H 2000 Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides. Journal of Dairy Research 67 53–64CrossRefGoogle ScholarPubMed
Rasmussen, LK, Due, HA & Petersen, TE 1995 Human αS1-casein: purification and characterization. Comparative Biochemistry and Physiology – B Biochemistry and Molecular Biology 111 75–81CrossRefGoogle Scholar
Re, R, Pellegrini, N, Proteggente, A, Pannala, A, Yang, M & Rice-Evans, C 1999 Antioxidant activity applying an improved ABTS radical cation decolorization assay. Free Radical Biology and Medicine 26 1231–1237Google Scholar
Rival, SG, Fornaroli, S, Boeriu, CG & Wichers, HJ 2001 Caseins and casein hydrolysates. 1. Lipoxygenase inhibitory properties. Journal of Agricultural and Food Chemistry 49 287–294Google Scholar
Salami, M, Yousefi, R, Ehsani, MR, Dalgalarrondo, M, Chobert, J-M, Haertlé, T, Razavi, SH, Saboury, AA, Niasari-Naslaji, A & Moosavi-Movahedi, AA 2008 Kinetic characterization of hydrolysis of camel and bovine milk proteins by pancreatic enzymes. International Dairy Journal 18 1097–1102CrossRefGoogle Scholar
Salami, M, Yousefi, R, Ehsani, MR, Razavi, SH, Chobert, J-M, Haertlé, T, Saboury, AA, Atri, MS, Niasari-Naslaji, A, Ahmad, F & Moosavi-Movahedi, AA 2009 Enzymatic digestion and antioxidant activity of the native and molten globule states of camel α-lactalbumin: possible significance for use in infant formula. International Dairy Journal 19 518–523CrossRefGoogle Scholar
Silk, DBA, Marrs, TC & Addison, JM 1973 Absorption of amino acids from an amino acid mixture simulating casein and a tryptic hydrolysate of casein in man. Clinical Science 45 715–719CrossRefGoogle Scholar
Tauzin, J, Miclo, L & Gaillard, J-L 2002 Angiotensin-I-converting enzyme inhibitory peptides from tryptic hydrolysate of bovine αS2-casein. FEBS Letters 531 369–374CrossRefGoogle ScholarPubMed
Tirelli, A, de Noni, I & Resmini, P 1997 Bioactive peptides in milk products. Italian Journal of Food Science 9 91–98Google Scholar
Vermeirssen, V, Van Camp, J & Verstraete, W 2002 Optimisation and validation of an angiotensin-converting enzyme inhibition assay for the screening of bioactive peptides. Journal of Biochemical and Biophysical Methods 51 75–87CrossRefGoogle ScholarPubMed
Wong, PYY & Kitts, DD 2003 Chemistry of buttermilk solid antioxidant activity. Journal of Dairy Science 86 1541–1547Google Scholar