BIOCHEMICAL AND MOLECULAR ANALYSES OF ALPHA S1-CASEIN POLYMORPHISMS IN CAMEL (CAMELUS DROMEDARIUS) AND DESCRIPTION OF BIOLOGICAL ACTIVE PEPTIDES AND ALLERGENIC EPITOPES

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ORAL PRESE,TIAT/OIVS Session 2 The production and products of Camelids The difierences in the PCR results of the isolates

Xl

, X3, X23 suggest these isolates were distinguished genetically, but they have the same physiological and biochemical propeÉies by conventional method. The same environmental factors could explain similarity of the morphology, the physiology and the biochemical features of

Xl,

X3 and X23 isolates..

Conclusion

The gene difference among these yeast isolates is showing that, the yeast isolates might be mutated and started to belong

to different species of taxonomy during evolution. And therefore the combined research using conventional or traditional and advanced methods should be more effective for identification of yeasts.

References

1.

Fleet G.H, "Yeasts in dairy products" .Journal of.Appl. Bacteriology,1990,68, pp. 199-211

2.

lrcna Savova, Marìa Nikolova, "lsolation and taxonomic study of yeast strains from Bulgarian dairy products" .Journal of culture collections, Yol.3,

2000-2002, pp. 59-65

3.

Watanabe Koichi et al, "Diversity of LAB and yeasts in Airag and Tarag, traditional fermented milk production" World Journal of microbiology and

biotechnology, Yol. 24, 2008, pp. 1313-1325

4.

Delgermaa S, Enkhtuul Ts, ldentification methods of yeasts and UB. Ulaanbaatat,2Ol2

5.

Enkhtuul Ts, Delgermaa S "lsolation and taxanomic study of lactose-fermenting yeasts from Mongolian dairy producis", The 8th intemational

forum on Stratgy technology 2013, proceedings Volume p495

6.

C. Andrighettol , E. Psomas2 , N. Tzanetakis2 ,

c.

Suzzi3 and A. Lombard "Randomly amplified polymorphic DNA (RAPD) PCR for the identification of yeasts isolated from dairy products" Letters in Applied Microbiology 2000, 30, 5-9

Acknowledgments

Part of this work was supported by the Project Reg. 03/2012 (MUST, SIT) 'Pure culture of useful microorganisms in foods'

BIOCHEMICAL AND MOLECULAR ANALYSES

OF

ALPHA S1-CASEIN

POLYMORPHTSMS

IN

GAMEL (CAMELUS

DROMEDAR US)

AND

DESCRTPTTONS

OF HOLOGTCAL

AGTIVE

PEPTIDES

AND

ALLERGENIC

EPITOPES

Erhardt

G.1,

Shuiep

E.S.1,2,

Lisson

M.1,

Giambra

1.J.1,

El

Zubeir

1.E.M.3,

Pauciullo

A.1

l.Department of Animal Breeding and Genetics, Justus-Liebig-University Giessen, Ludwigstr.

218,

35390 Giessen, Germany, Email: georg.erhardt@agrar.uni-giessen.de. 2. Department of Animal Production, University of Nyala, 155

Nyala, Sudan. 3. Department of Dairy Production, University of Khaftoum, P" O. Bax 321 Khaftoum, Sudan

Abstract

Milk samples of 93 camels (Camelus dromedarius) from different regions of Sudan were screened for casein variability by isoelectric focusing. Kappa casein and beta-casein were monomorphic, whereas two protein patterns, named qs1-casein

A

and

C

were

identified.

The major

allele

A

revealed frequencies

of

0.82

(Lahaoi)

and 0.86

(Shanbali)

in the

two ecotypes.CSNTST*A

and

CSN7S7-C

are

both characterized

by

missing

of

exon

16

on

mRNA-level compared

to

the already described CSN7S7*B. Furthermore, CSN7S7"C shows a single G>T nucleotide substitution in the exon 5, leading

to

a

non-synonymous

amino

acid

exchange

(p.Glu30>Asp30).

A

polymerase chain-restriction

fragment

length polymorphism method (PCR-RFLP) was established as a DNA-based test for this mutation.The occurrence and differences of lgE-binding epitopes and bioactive peptides between qs1-casein A, B, and C after digestion were analysed rn s/tbo. The amino acid substitutions and deletion affected the arising peptide pattern and

thus

modifications between lgE-binding epitopes

and

bioactive peptides of the variants were found. The allergenic potential

of

these different peptides

will

be investigated by microarray immunoassay using sera from milk-sensitized individuals, as it was already demonstrated for

bovine osr-casein variants.

Keywords: milk proteins, genetic polymorphisms, CSN7S7, lgE-binding epitopes, bioactive peptides

rytae cyTtHEEfl

ALPHA

sI-

GASEIN nOrI]4MOPO143MH!H

El,loxhMkrffnHK

)l(OHE

MOrr

EKynfl

pn

br

AHArr r43EEpr

M

EH Er,lOnO

rHfl

n

bl

K

EEflCEHTT

n

EnTTflTEP

M

EH

Arrrr

E P

rufl

,r br

_K

3 n

l4To

nrAPEbl

l-{

c

r

nATTAM Afl

APbl

CygauHur4 ap

_rypni

aygaHAapbtH4arur 93 ryùenepgiq cyriuen anbrHraH cbrHaManap4aH Ka3eilHHiH esrepyiH usoenerrpnir

6onin any xacaJrbtHgbt. MoHoxporugut Kanna Ka3ehH ueH 6era Ka3euH.qep a(ybr3 epHeKTepi peringe, gs1-casein A xeHe

C Oonsrn ra6urngur. Eri

erorunre

Heriari A 6eniri 0.82 (Lahaoi) xaHe 0.86 (Shanbali) annenugepi 6ongut.

CSN'IS1"A

_xatre

CSN1S1*C e«eyi

_ae

16 mRNA OeniuAe

_{canucrupManH rypge}

CSN1S1-B cunarratZgut. Coserues

farap, CSNI

Sl.C

G>T xeKe HyKfleorr,r4

periHge

5 e«couga aybrcrbrpa,qbr, aMuHo Kbrrxr(brnAbr( aybrcrbtpyAa cmuoHrrrr4i

eMec opbtH

aybtcrbtpyra

xereneÉg(p.Glu30>Asp30). l-lonuvrepaagH r.JrbrHxbrpnbr peaKrlr4n ysa6

norru$opusrrl

agiciHitl

beniri periHge

(PCR-RFLP)

_EHK

HerigÀi

recr

periH4e

ocbr

Mfrallilfl

yr-uin opuanacrbrpbrnÀbr.

5yn

xa4anul6

ocbr

annenbgep yruin xsrHurcrbt( KarbtHac neH naKTal{tafl re:e4iHeH 6oc xaHyapnapgbr 3eprreyre

uyurix

6onutn caHanaAbt. qs1-casein

_A,

_{B, xeHe C 6r,ro6enceugi}

_nenrrgrep

_{MeH onr4ronrap apacbrH,qarur baùnasurcrapgbr-l ocut}

_xargaùnap

_MeH atiutpua _{ulurn ul(rapbl ac (opbrryAaH coH aHanr34eH erxisingi.}

Tyùin

_cesÒep:

_cym

_{a$ybt3òapat, eeuemuKanbtK nonuMpfuwM, CSN7S7, tgE-mypa4mar onumonmapar, 6uo6encenòi}

nenmuòmep

ORAL

PRESENIAIIONS

Session 2 The production and products of Camelids

Enoxt4Mr/qEcKHùr

t4

MonEKyIifipHbtH

AHAJI[,13

noJ'll4MoP@vt3MA

ALPI-NA

s1-

KA3Et'll-lA

y

_BEpEnloEoB

(CAMELUS

DROME;Àniu§l h

oru'lglHl4E

EUOnOTHL{ECKI4

AKTLlBFlblx

nEilTHEOB

1'l

AJIfiEPFEHHbIX

SnhTOnOB

O6pa:qur

MonoKa

or

93

eep6nrogrq (Camelus dromedarius)

r'r:

pa3Hblx peruoHoB

Cygaua

HccnefloBanilGb

Ha

r3MeHqrBocrb Ka3erHa Mero,qoM

t43oefieKrpr4qecKoro

QorycrpoeaHrr' kanna-raserH

'

6era-rasetlH

6utnr

rrlOHOruopquutMt4, B To BpeMff KaK pee 6utnu yr,eHrra+vrqrPoeaHsi xax 6enxOeute no.ne'q.BaTeflbHocTl4'

rrnut

A U C qs1-casein.

laa

ocHoeuurx

anreflfl

A

npoRsnrn,""

*u

uuliJrà

0,82 (flaxaorz) r,r 0,86 (tlJan6ann) B AByx 3Kor,nax'

csN1sl.A

r,r CSN1S1-C

o6a

xaparrep,3ylorc'

"",qoarrorlrM

sK3oHoM

i6

'a

ypo"tre

urPHK

no

cpaBHeHvtlo

c pxe

onHCaHHblM

CSN151*B. Eonee

roro,

CSN1S1-C

no*r.","r&""g;*r,,o"

G>T garvreqeHile HyKfleorrrqa.B 3KsoHe

5'

qro

eneqer

HecHHoHnMtrqHbtù

auuuorrcnorHutù

o6rueH

1p.Ctuao',RSp30)'

_-,Merog

nonruopQrsua Qparueura

rlacru

l-lenil nonuMepa3bl (PCR-RFLP) 6utn ocHoeaH

,,

,"àn"u

Myrallh, [HK"

PacnpocrpaHeHre

r

pacxo)KAeHhe onHronoB H

6uoarruauurx

n"nrroo"-LLTI[il;ffir*;,

B ra C 6irnr,r

npoaHanil3,poeur"iin

silico nocne nepeBaprBaHus' Sutnu

BbrFBfleHbr aMhHoKrcnorHbre 3aMeu.le Hwn tAyAanelr4r, Bbr3BaHHble Bo3pacraouleù nenrnEHoù nocneÀoearellbHocrblo t4'

coorBercrBeHro,

,o,rer"*;u;;;;*y

if,L

,rrron

atavt w 6noaw,,BHbrM14 nenrilEaM14 Bap'laHroB' AnnepreHn'{ecKrÉ

noreHLlran

orhx

pa3nnrrHbrx

nenrrEoB

6yger

ilccneEoBaH Mero,qoM

urr,rrvlyno$eprueHTHblx M'tKpoqvlnoB c

rcnoflb3oBaH,eM cblBoporKt4

or

rono"ro-"",1!^rarp""u".,.',"x oco6eù'

KaK

oro

6utno

no«aaauo

Ha

os1-ra3eilHe

KOpOBbero MonoKa.

Knpqeearculoea:6enxumonoxa,eeHemuLtecxuùnonuuop$usu,csNlSl,enumonttu1uoaxmUeUArcnenmuòatlgE

lntroduction

camel

milk plays an important role as protein source for many humans especially for the people living in the arid lands

of the wortd

(Konuspayev;"i;i;

ioooy.'tn

additioì1Éeie

is

a'growing

interest

inusage

of

camel milk

as

a

healthy

food

(Nikkah, 201.1

),

and atternative protein

,orr"".fo|.

humans

riitn

,iit

protein allergy (Hinz

et

al',2a12)'

However' the knowledge

in

mitk protuln

ortr.,i,

species_and

il'l"

s"À"il

rariation

is

iery

limited.

kappeler.et

al'

(1998) described two

genetic variants

ot

o",-Ctl

1$f.ffèf

"n;

CSNf

Sì-Él

OV protein- and. mRillA-sequencing within Somali camel (Camelus

dromedarius).Therefore,

the

aim

of

this

study

*u"

to

investigate

the

occurrence

of [o[morphisms in

camel

qsr-cN

especially in sudan.

ru.tnàr*orà,

options to oéscrùL the allergènic potential as well as bioactive peptides of those protein

variants should be

demonstrated-

Material and

methods

Milk and blood samples from two camel ecotypes

iar,aoi

(n=65) and shanbali (n=28) rrye1e gollgcted

(shuiep et al' 2013)'

Fresh milk samples (n=5)

of camelus

dromedarius

*àr"

obtuin"d

from

Kamelhof Rotfelden (Rotfelden-Ebhausen'

Germany) and immediately kept at

4"C..Simulla*"r" pnànolqitg

of camel milk protein variability on protein level was done by isoelectric focusing

ltrr;

acggld!p_!o Erhardt 1ìOeO). DNAwas_isolated according to sambrook et al' (1989) from

the btood samptes on the fitter paper

(FTA@ch";ì;è;;i- wÀàiÀrnteioscience,

Maidstoné, UK). somatic cells of the fresh mirk sampres were gainàd for mRNA'extraction àlcoroìng

tà

Boutinaud

etal.

(2o02)" lnvisorb@

soin

RNA Mini Kit (lnvitek GmbH, Berlin, Germany) was used forextraction of total È.run*r,i"r,

*u.i"u"tà"

transcribed to cotttR using VersorM

.DNA

kit (Thermo Fisher scier{titic, wartman,

M&

usAiF;iìuquun"ing

of

csN1s1

cDNA a set of primers for amplification and sequencing were designed by means_of

oNasis-iltai;]à^0 ;;ft*are

(Hitachi software,

san

Bruno,

cA,

USA), using

first the complete

r"qu"n"""

of éamel cDNAs reporteO by Kappeler e-t

al-(1998)

and then-the new sequences determined' pCR was used to amptify complete cDNA of

Còù1§i. ihb'amptifiel

tàg'"ntt *"t-".I"]YTds

sequenced using

a

Big

Dye Terminato,

,"qu"nJng

r',ir.ì.r

(Applied.Bùàvitu*r,

Fors'ter City,

én,

usn;.

A

PCR-RFLP test was developed for the screening ot singre';uÉteoìiOe

poìV*orpnisÀsiSNpilO.ntmed

.in-.CSNiS1 (é'150G>T GenBank

lD:

JF429138)'

To determine peptides containing lgE-binding

_"pitoò".

ànJ É1fe1en9el between the genetic variants after digestion'

potential

cteavage sites

were

prfi"tÉo

-using

thà iri

riiil"

ÈrÈÀsy tool,

Peptide

cutter

(httpJ/web.expasy'orgipeptide-cutter/)'

Resulting peptides were compared with epitopes describedin bovine qs1-casein (chatchatee-et al', 2001)' For identification

of

bioactive peptiOei

the

amino

acid' sequences

of

osl-casein

A, B'

and

C

were

digested

in

silico

(http://www.uwm.edu -plibiochemia/) usino

different;Jfrl::Ì

discussion

simultaneous typing of camel milk protein uring

irièuealed

polymorphic protein pattern.named

q"r-cN

in the most acidic

fraction of the gel. Rtpnà- o"r-casein A revealuÉ ttre

,ost

alkaliné isoelectric poini 1pt;, ulhereas allele

c

was just focused

in its acidic side. Naming was done consioertng nàmenclature of Kafpeler et al. (1998). Due to this

o'r-CN

C seems

to be

a new variant. screening of all g3 camel milk

ràrpÉr

ov

rrF

revealed dominance of

q"r-cN

A in comparison to qs1-cN

c

with frequencies

of

0.8à ànd

0.82

in

Lahaoi and Shanbali ecotypes, respectively' .sequencing

of the

complete coding sequence of camel

céN7st

ot

tÉr-pre+yp"o-o.,-òr.r A

cDNA éàmptes showed futt sequence similarity

to

qs1-cN

A

of Kappeler et al. (1998). Samples with o"1-cN

c

are characterized by a non-synonymous

Gd-sNP

(c'150G>T; GenBank

lD: JF429138) resutting in the amino aciO suOstitutùn p.Glu30>Asp30 in

thé

maiure

protein'

CS^/757.C and q"1-CN B

(Kappeler ei al., 1998) àre both characterized ov

ò.g"sg'etq3q'Lt1'

deduced mature protein sequence' and are differing

by missing or non-missinO of ex91 tO, respectlvlly. The PCR-RFLP test developed confirmed the IEF and can therefore

be used for typing

"u*ur?srvlsl

vaiiaoitity indefiendent of

ag_e, sex and lactaiion stage. A comparison of the identifled

peptides

after insi/ico digestion of qsr--casein^A;

B;;à

C

witr

tgÉ-ninding epitopes descr-ibed in bovine qs1-casein showed

that lgE-binding

epitop;i

rz

443

andf153-i6g

did not resist dlgestion iÀ intact form and ihat the amino acid substitutions and deletion influence the resulting peptide puttuin.

ir'rr,

peptYrde f28-40 occurred in all 3 variants' Peptide f15'1 -159 was

only identified

in

variant

A

and

c,

whereas

_Éptià*

trÉi

ìss

and f160-167 were found

in variant

B'

These peptides comprise

major parts

of the

lgE-uinoing epitJpe

Ìtsa-toa.

To

determine

the

allergenic potential

of

these

peptides

microarray immunoassay using synthesizeo peplioes and sera from humans with cow milk allergy are currently in progress. A totat of 83 bioactive peptides wiih ACE inniniiorv isà1, srimutating (8), antioxidative ('12), inhibitory (9), and hypotensive

(1)activitieswerefoundin osr-caseinA,Bandé.'ouitothedeÉtionofSaminoacids,twofurtherACE-inhibitoryand

'188

ORAL

PRESENIAI/ONS

Sesslon 2 The production and products of Camelids antioxidative peptides (fAY and fHL) were exclusive identified in os1-casein B. This confirms that genetic variants of camel

case

iii aie

a

s!ì.iice

of o;fieier-;

;,;ac:;',;

pepiL.res as aii'eacy ,iesci-i:ed

il

cai',ie 1''\'eii;'ar-,i-;

ei

a,

20i37 and ie'reais .i-re

aCdiiional pcientìal cf milk protein ',,anants fct- hunran health.

References

1.

Boutinaud,[4.,Rulquin,H..Ketsler,D.H..Djiane,J.,Jammes,à.,20A2. Useof somatlccel]sfromgoatmilkfordynamicstuciiesof geneexpressìor. in the mammary gland. J. Anim. Sci. 80. i258-1269.

2.

Chatchatee. P., Jàrvinen. K.lM., Bardina, L., Beyer, K., Sampson, H.A.,2001. ldentifrcation of lgE- and lgG-binding epitopes on alpha (sl)-caseirL: Differences in patients with persistent and transient cow-s m ilk allergy. J Allergy Clin. lm m unol. 1 07, 379-38 3.

3.

Erhardt, G., 1989. r,Kaseine in der Rindermilch - Nachweis eines weiteren Allels (r-CNÉ) in verschiedenen Rassen. J. Anim Breed. Genet. 106 225-231.

4.

Kappeler, S., Farah, 2., Puhan. 2.,1998. Sequence analysis of Camelus dromedarjus milk caseins. J. Darry Res. 65.249-2?-2.

5.

Konuspayeva, G., Faye, 8., Loiseau, G.,2009. The composition of camel milk: A meta-analysis of the literature data.

J

Food Compos Anal 22, 95-1 01

6.

Hinz, K., O'Connor. P.N,,1., Huppedz, T., Ross, P.M., Keìly, A.L.,2012. Comparison of the principal proteins in bovine, caprine, buffalo, equine and

camel milk. J. Dary Res.79. 185-191.

7.

Nikkah,A,.,20ll.Equidae,camel,andyakmilksasfunctional foods: areview.J.Nut.FoodSci. 1,1'16.doi:10.417212155-9600.1000'1 16.

8.

Sambrook, J., Fritz, E., iManiatis, T., 1989. Molecutar cloning. A laboratory manual. (2"ded.). Cold Spring Harbor Laboratory Press, New York, NY, USA.

9.

Shuiep E.S., Giambra 1.J., El Zubeir LE.N4., Erhardt G., 2013. Biochemical and molecular characterizaiion of poiymorphisms of os1-casein in Sudanese camel (Camelus dromedarius) mìlk. lnt. Dairy J. 28, 88-93.

1

0.

Weimann, C., Meisel, H., E rhardt, G , 2009. Bovine K-casein variants result in difFerent ACE inhibitory peptides. J. Dairy Sci. 92, 1 885-1 888.

Acknowledgments

This work was partly funded by DAAD by a scholarship

to

E.S. Shuiep and by German Research Foundation (DFG ER

122113-2)"

LOW MILK CHOLESTEROL

IN

CAMEL MILK:

TRUE

OR

NOT?

Fave

B.1,2,

Bengoumi

M.3,

Al-Masaud

A.1,

Konuspayeva

G.1'4

1. Camel project, P.O.Box n"721, 11942 Al-Kharj, Saudi Arabia, faye@cirad.fr; 2. CIRAD-ES, Campus intemational de

Baittarsuet'

rA cn

12

A'

UMR

'-',iYi{i,llf,3i;,#ii'fl[F!,5[ì;i?'

i;#r?

',f,lll[i';I:1r:i:;"'

runisia;

4

At-Farabi

Abstract

Many authors argue that camel milk oontains less cholesterol than cow milk while other reported the reverse. To compare the cholesterol content in camel and cow milk in similar farming conditions and to assess the impact of short underfeeding on cholesterol concentration in milk and serum, seven cows and seven camels were sampled (milk and blood) at the middle of lactation at morning and evening milking, then two weeks after distribution of low energy-protein diet, another sampling was achieved. Cholesterol content in camel milk (5,64 È 3.18 mg 100g-1) was lower than in cow (8.51

t

9.07 mg

1009i),

but the difference

was

not significant. Moreover, the ratio cholesterol/fat was similar in the

two

species (225

x

125 mg

1

00gi

fat in camel and 211

!

142.4 mg 100gr fat in cow). Serum cholesterol concentration was significantly higher in cow

(227.8

r.60.5 vs

106.4

t283

mg

100mLi).

There was significant difference between morning and evening milking in milk fat composition and concentrations in cholesterol. The present study showed that cholesterol concentration in camel serum is lower than in cow in similarfeeding and environmental conditions, but further researches are needed to demonstrate the relationship between feeding and cholesterol content in camel milk.

Key words: camel milk, cholesterol, serum, low diet

TYtae CYTIHEETI

XOflEGTEPOfl

EEHrEl4l

TSMEH: PAC

nA?

KenrereH aBropnap ryrZe cyrin,qeri

xonecrepon

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7

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Tyùin cesòep: myùe cymi, xonecmepon, epmiuòi, 1ynapnarru as òuema

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Koropbrx or6mpanucb npo6st uonoxa ta KpoBt4 ua yrpeuueù

189

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