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Characterization of Caseins from Mongolian Yak, Khainak, and Bactrian Camel B Ochirkhuyag, Jm Chobert, M Dalgalarrondo, Y Choiset, T Haertlé

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Characterization of Caseins from Mongolian Yak, Khainak, and Bactrian Camel B Ochirkhuyag, Jm Chobert, M Dalgalarrondo, Y Choiset, T Haertlé Characterization of caseins from Mongolian yak, khainak, and bactrian camel B Ochirkhuyag, Jm Chobert, M Dalgalarrondo, Y Choiset, T Haertlé To cite this version: B Ochirkhuyag, Jm Chobert, M Dalgalarrondo, Y Choiset, T Haertlé. Characterization of caseins from Mongolian yak, khainak, and bactrian camel. Le Lait, INRA Editions, 1997, 77 (5), pp.601-613. hal-00929550 HAL Id: hal-00929550 https://hal.archives-ouvertes.fr/hal-00929550 Submitted on 1 Jan 1997 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Lait (1997) 77, 601-613 601 © Eisevier/Inra Original article Characterization of caseins from Mongolian yak, khainak, and bactrian cam el B Ochirkhuyag 2, lM Chobert 1*, M Dalgalarrondo 1, Y Choiset 1, T Haertlé ' 1 Laboratoire d'étude des interactions des molécules alimentaires, Inra, rue de la Géraudière, BP 71627, 44316 Nantes cedex 03, France; 2 Institute of Chemistry, Academy of Sciences, Vlan Bator, Mongolia (Received 25 November 1996; accepted 5 May 1997) Summary - The composition of acid-precipitated caseins from ruminant Mongolian domestic ani- maIs was analyzed and a comparative study between camel (Camelus bactrianus) and dromedary (Camelus dromedarius) was realized. Acid-precipitated whole caseins were analyzed for ami no acid composition, separated by anion exchange chromatography and identified by alkaline urea-PAGE. Elution profiles and electrophoretic mobilities of the main components of yak and khainak caseins were nearly identical to their cow counterparts. However, the main part of a:;l-casein of yak was eluted in lower molarity in NaCI. Characterization by PAGE, ami no acid composition and N-terminal sequence of individual caseins from camel (Camelus bactrianus) indicated that milk of this ruminant con- tains dominantly aS1-' aS2-' and ~-casein and small amounts of x-casein as is the case for the milk of dromedary (Camelus dromedarius). caseins / yak / khainak / camel Résumé - Caractérisation des caséines de ruminants de Mongolie: yak, khainak et chameau bactrien, La composition en acides aminés des caséines totales de deux ruminants de Mongolie (yak, khainak) a été déterminée. Les différentes caséines ont été séparées par chromatographie sur échangeur d'ions et analysées par électrophorèse en milieu urée et à pH alcalin. Les caséines des deux espèces étudiées ont un comportement voisin, proche de celui des caséines de vache. La seule différence notable réside dans le fait que chez le yak, la caséine aSI est éluée à une molarité inférieure à celle utilisée lors de la séparation des caséines de vache et de khainak. Une étude comparative a été réalisée entre le chameau (Camelus bactrianus) et le dromadaire (Camelus dromedarius). Ces deux espèces renferment principalement les caséines aS l' aS2 et B, dont la séquence N-terminale a été déterminée. La caséine K n'est que faiblement représentée. caséines / yak / khainak / camélidés * Correspondence and reprints 602 B Ochirkhuyag et al INTRODUCTION sent a more systematic description of the major milk proteins of principal Mongol Many populations of Central Asia, and Mon- stock animais and to compensate for this gols in particular, have thousands of years of gap. This paper describes the separation of old traditions of using milk and milk prod- the caseins from Mongolian cow, yak, ucts for nutritional purposes. Sometimes, khainak, and Camelus bactrianus by dif- they use also particular dairy products as ferent ion exchange chromatographies and curative agents (Kadirova, 1985). The first their further purification by reversed-phase European written mentions of the use of HPLC. For comparison, the caseins from milk as main staple of nomadic tribes origi- Camelus dromedarius (Arabi an dromedary) nating from Asia by ancient Greeks are due were separated using the same set of purifi- to Homer (-800 BC), Herodot (-500 BC) cation methods. The major casein compo- and Strabo (-100 BC) in their descriptions nents were characterized by urea and SDS of barbarian populations termed ya.Àa.K- polyacrylamide gel electrophoresis, and by 'tO<\>a.yot (galactophagi). Antique Greeks determination of their amino acid compo- attributed to this type of diet the particular sition and N-terminal sequence. strength and fierceness of described nomads. The earliest conserved written Chine se records of the mare' s milk use for prepara- MATERIALS AND METHODS tion of koumys can be traced to almost 2000 BC, to the descriptions of northem nomadic Preparation of milk sampi es tribes by Han historian Ssu-ma Ch'ien (sum- marizing ail preexisting information around Milk was collected from weil identified single the 1st century BC) and to conserved runic Mongolian domestic animais. The milk was and Ouigur petroglyphs on still existing stel- Iyophilized in the Food Industry Research Insti- lae. Nowadays, dairy products derived from tute of Ulan Bator, Mongolia. The lyophilized samples were kept frozen at -4 "C until further milk of animais herded on the Mongolian processing. The dromedary milk was a kind gift steps and deserts constitute still a major ele- of Professor Mahmoud Sitohy and was also pre- ment of indigenous diet. In 1995, Mongolia, pared from the single dromedary from Egyptian counting about 2.5 millions inhabitants, had desert animal stock. 416 000 cows, 708 000 yaks and 58 000 khainaks (hybrid between cow and yak), and had also 367 000 bactrian camels. Preparation and separation of caseins Unfortunately, despite the studies of Grosc1aude et al (1982), despite long ali- The whole casein was obtained from skim milk mentary practice, information about milk by precipitation at the isoelectric point (pH 4.6) proteins of Mongolian domestic animais is using 1 N hydrochloric acid. The precipitate was rather fragmentary. Moreover, available washed with distilled water, solubilised at pH 7 by addition of sodium hydroxide, precipitated information concerning dromedary milk again at pH 4.6 and washed three times with dis- (Farah and Farah-Riesen, 1985; Beg et al, tilled water. Finally, the whole casein was solu- 1984, 1986a and b, 1987; Abdel Rahim, bilised at pH 7, freeze-dried and stored at -20 oc. 1987; Mehaia, 1987a and b; Mohammed The individual caseins were separated by ion and Larsson- Raznikiewicz, 1989, 1991; exchange chromatography on QAE-Sepharose Farah, 1993) is related mainly to the Ara- (Pharmacia, Orsay, France), by applying a gra- bian dromedary Camelus dromedarius dient from buffer A (0.02 mol/L imidazole, pH 7.0, 3.3 mol/L urea, 0.3% (v/v) 2-mercap- species, and very scarce for the camel toethanol) to buffer B (0.02 mol/L imidazole, Camelus bactrianus species. The present pH 7.0, 3.3 mol/L urea, 0.3% (v/v) 2-mercap- work has been carried out in order to pre- toethanol, 1 mol/L NaCI), at room temperature, Caseins from Mongolian ruminants 603 with a flow rate of 200 mUh. The ion exchange solvent N40% solvent B (80% acetonitrile/20% chromatography was performed on an Econo H20IO.085% TFA) to 30% solvent A/70% system (Bio-Rad, Ivry sur Seine, France) equip- solvent B during 40 min. The flow rate was ment. 1 mL/min and absorbency was recorded at 214 nm. Polyacrylamide gel electrophoresis Amino acid analysis Polyacrylamide gel electrophoresis (PAGE) was performed in a vertical mini slab gel apparatus The proteins were hydrolyzed under vacuum in Protean II (Bio-Rad). The acrylamide gel (10% the presence of constant boiling 6 N HCI for 24 h in 4 rnol/L urea, Tris-HCl, pH 8.8 buffer solu- at 110°C in a Pico-Tag station (Waters). After tion) was prepared according to Davis (1962). acid hydrolysis, the ami no acids were deriva- Electrophoresis was performed at constant tised with phenyl isothiocyanate (PITe) accord- amperage (15 mA during 7 min in the stacking ing to Bidlingmeyer et al (1984) and quantified gel, and 30 mA for about 30 min in the running by RP-HPLC on a Pico-Tag Cl8 column (3.9 mm gel). The SDS-PAGE was carried out according id x 15 cm). Speed-vac dried samples were dis- to the method of Laemmli (1970). The running solved in 95% 2 mmollL Na2HP04, pH 7.4, 5% gel (8.0 x 6.0 x 0.075 cm) contained 15% and acetonitrile. The column was equilibrated in sol- the stacking gel 4% acrylamide. Casein ratios vent A (94% 0.14 mollL CH3COONa, 0.5 mL were calculated by scanning the electrophoretic TEAIL, pH 6.4, 6% acetonitrile): the elution was gel, by using a Bioprofil station Program. performed with a gradient from solvent A to sol- vent B (40% H20 / 60% acetonitrile) according to Dalgalarrondo et al (1990). Both the column and solvent were maintained at 38 oc. The flow Chymosin test rate was 1.0 mL /min and absorbency was recorded at 254 nm. Chymosin of calf stomach (EC 3.4.23.4.), 23.6 Ulmg ofprotein (Sigma Chemical Co), was dissolved in distilled water (1 mg/mL). An aliquot N-terminal sequencing (5 ug) of the enzyme was supplied to 1 mg of bovine lC-, and p-casein, and to 10 mg of camel and dromedary caseins issued from fraction 3 of The N-terminal ami no acid sequence analysis ion exchange chromatography (see Results), dis- was performed on an Applied Biosystems model solved in 1 mL of a 50 mmol/L imidazole/ HCI 477 A sequencer with an on-line identification buffer (pH 6.5).
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