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,|uĚ#(Č¸âcÃ-I51:I4I}ċåĘACEęĐËd ' 4 A@8<,sěSwĚ*'A@8< ACE Đ»&! in vivo  )XÊ,¢' ),ÓÒěºJæ«|Ě#(Č¸â,í/1I¶)ĆªĚNaOH &)cĚP/1IR±ì
7/-/1I AMP01 &!;D>KG HW-50 &)2HC;3E?.KZ)&(ĚSHR)đyXÊ in vitro  ACE Đ»,Y FII Ëd,üôě³Ě
FII , Cosmosil 5C18
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ACE ,Đ)&(ĚòyđN, ā Ùv*ě

P 20
CAM O YjdDXB(QAm&
9F]K 12ZCr 15tfR 2"ZH, 2 0 / 2VTh) 11|9^c1414yXQ'=`4_b`2 @:1414y  _bsÓÒ òßÈ Ě òß 'òßç *)Åÿ)ěéÈ¨%h_¹ÐĉÚ
ÈÆÒòßÈĚxîÏĚäÍçïÎ%ďàF0C8ÍÒòßÈdĔ*)ě&ĚòßÈ °ÌÍďO) ¢' )ě©×Ü
\ĚX á](ĚÖ¨Ďæ«'*) in vivo úĕĚCAM (Chorioallantoic
Membrane)º (ėê¿ïº),ØÝĚº&(Ěin vivo  )?EB=/<ĔòßÈf»,ù\ěºJæ« CAM º Ěoãėm CAM Mú,½iĚòßÈf»,ù\)º)ě
aWÒ Ěú½i 3 ¡Ó )òßÈf,÷Ě»,Óö&( 5 ´Ēù\ěù\,$ĚòßÈfÄ,Þc)čk,óěSwĚin vitro úĕ&(òßÈf» Øû*) 4 Û?EB=/<ĚGalangin, Kaempferol,
Quercetin, Myricetin Ě CAM º,Ê in vivo »,ù\ě*'krÃ Ě?
EB=KGdĔ*ĚB Ç OH { ** 0, 1, 2, 3 ^)U~ `ć¯Ĉ,)ěCAM º&)ù\ ĚqúĎĚOH {Ċ&)»}k #(õ'*  Ěqú*$ĚÀ[ÒòßÈf» ÷*ě*'
?EB=/<ù\æ« 'Ěin vitro úĕ&!C06,Ê in vivo úĕT¤º CAMº ¦Ê) Ùv*ěP 21$3<!  ;?C7W KM
X0J 1^>&* 1,2^[. 1,2, @VR5 1
1\ Y1IN-/ FC 4L/KML^2 Y1IN-/ E,L/KM:]ãâ £ ù¥+Þ áßI62!ĴÛ£ ó 2 dİ Ĵ AN2!º½ +
~,+ĵĕĴÞÉ.Ìà+ ! ĴWĤ¡ē&e.ö®+WĤv üµ ¸x*Ĵ,]Ĭ©n ±y(+ÙÏû§Þ WĤ'³ģ¡ ħ$+ĵÞð ñêÝ¥.ĎWĤvâçí!áĘP nğ+ Ĵ¶¾X£ !TÜ»&İ Ĵ º½ ß×.WĤ + !¡ēiehº½.ĚÒĞąċĪ+ĵ¾çí!Ĭ©n(+Þ WĤ³
.ãâĴč09BHCL Oì+4?6;0L ­ÄÏ£.º½G<J+w²mH:=.ÚÃĆĵµÍMõ¿ w²mH:=4?6;0LĲ0.1Ĵ1Ĵ10Ĵ100 mg/kgĳ. 1 ¶Ĳæ½ĳ(" 14 ¶ĢĲġ½ĳôz¬SĴĴZĄâ­r 62IN?L3«Í+ Porsolt pÊÎĉį(Forced
Swimming Test: FST )bĵj`â!ĴėĜR{ÿÊ.lÁ UH:=.g,+ÆïÎ . )%Ótu+ Ĵ Ót·Ģ æø.¯Å4?6;0L ­ÄÏ£.Ĉcĵ õ¿Ĵ4?6;0Læ½¬Sú!ÔúÈĔÓt·Ģ æø!èĊ   Ĵ4?6;0LĲ10 mg/kgĳ ġ½¬S(* FST (+Ót·Ģ æøĵ$Ĵ4?6;0L 10 mg/kg ġ½¬Sú ÐĮUĴ>N@DLZČĴ8K=?LZČ uèĊ,ĵ[P õ¿(*Ĵw²mH:=4?6;0L ġ½¬S­ÄÏ£
*Ĵ aÚF1?7E O!Ākêô\ěÕď u(+{ÿ£ é,ĵ

P 22
OS9"  U8/PQ' 6Z+=)B 1^ H 1^D2# 1^AG%( 2 ^@VR5 1\1 Y1IN-/ FC 4L/KML^2 Y1IN-/ T/KML]ãâ ¶¾X !ĴªĬÙÏ ³(īĒâ^"Ĵ$'TÜ¼´ ġĵ Ĵİıu!ÙÏû§Þ áßØ.İ%Ĵ,ĐĊåß ¥ýs+ĵþ¹ )Ĵ¶ÙÏ.āîfÉĚ+½ĢĴ-e^ Ë%),+ĵÖĊåß(+ć¨Mûÿ _Q!ĴeâÙÏ.Ė+Pĥ+ĵ ć¨Mûÿ ö®!e ^S+ü),+ĵ¾çí!ĴUÀêôò çí ă-,+÷Ă©n;/?L.ÚĴH:= ć¨Mûÿx#ĩ.ÃĆĵ¾çí!Ĵătĉį("êôÂĭÃĆĵµÍMõ¿ tÕį Wistar òĦH:=.ÚĴ5L=KNJú;/?Lúnĵ;/?L!Ĵ
Ā ©ġĚë+mÙä)±yĵĨVqH:=!Ĵ;/?LÊ.±ÊÇH:=ÇV );/?L.±yĴĨV !ä°;/?LÊ.±Êĵătĉį.ÃĆ+H:=! 0.3% (w/w) ;/?LÊĴêôÂĭ.ÃĆ+H:=! 0.25%, 0.5%, 1% (w/w) ;/?
LÊ.±Êĵć¨Mûÿ.o+ătĉįĴ4 ęıH:= passive avoidance test (¤¢ģ-+ć¨Mûÿ Ĉcò)Ĵ5 ęıH:= novel object test (Õ`Ċåģ-+ć¨MûÿĈcò) .ăĵ$ĴELISA Í(*Ĵ1 ęıH:=ÐĮĴêôÂĭ O+BDNF Ġ.Ñĵ õ¿Ĵpassive avoidance test +ć¨Mûÿ ¯Å!Ĵ;/?Lú
5L=KNJúÈĔ¼¦sĵ) novel object test +ć¨Mûÿ ¯Å
&Ĵ;/?Lú 5L=KNJúÈĔ¼¦sĵ$ÐĮ BDNF Ġ!Ĵ;/?Lú
5L=KNJúÈĔ¼¦sĵ¾çíõ¿ )Ĵ;/?L!H:=ć¨Mûÿ.}P+aÚ +ü),ĵ$Ĵ;/?L±y ÐĮ BDNF Ġ.s )Ĵ;/?L(+aÚ Oĝ!ĴBDNF |©.YôđģS+ü),
+ĵ

P 23
  Q= Pichia methanolica  Pex14 ;HL8
I$B 1WI+. 2WI64" 2W*?<%P 2W3> 2W-E 2 W
1-. 1W-2J 1 (1 ,$/ACW2 7O$TC)ÝÜ QAVCVYJąÉQ?GYTgùÒÙÜąæĒ-T6YT029@Y=ĐAODđ$:IDV29-<CW9W?Y=ĐDASđLT029>YPĐPsđ?WH3ú'ē&Ē Ps ?WH3úüþÄÂºąÉQ?GYTgù{¥ 'ćôKV<;'ê%('ē¬ĒÔ  P. methanolica Q?GYTgù{¥ AOD -.>8.P*`¦ö¼*!ĒPs üþ94ET 1ĐPTS1đU<K?YPex5p
AOD -.>8.PÌ©ÛÔ§č'* ēdĒPex5p Þcl×*¯LT029W Pex14p ö¼*ðē
´ËXè½
 eąÉØ» Pex14p -OGĆĄz*ĒPmPEX14 *3VYFW4ēPmPex14p Ē4 1­
 Pex14 nĎĒclass II SH3-ligand tĀĄz*n¯ēZ´ĒĂiª* Pmpex14¿*l«ĒñÔåõēPmpex14¿ Ps øÑæÏ'Q?GYT'Öëí*s&ĒQ?GYTø© Ps ąæ AODĒDAS $1?RY=ĐCTAđ
Ì©ăxçìúē%ĒPTS1 *f^ GFP-PTS1 ĈÖ¿ Ps '"ĒPmpex14¿çìú$Íìē(%è½ĒPmPex14p
AOD -.>8.P*!?WH3ú Ps üþ§č&ĒQ?GYTgù{¥ćô£}*¯*á'ē

P 24
5-aza-2’-deoxycytidine M) DNA 0/D;:
9KNW56!W&6EUR$SA@#A 'FGA@(VÝÜ DNA QATĒDNA QATCRW;J/RY= (DNMT)J,OSY$&{¥(ĒĂiÛÔ{¥#¾îkÂāćô'ēDNMT1  DNA óòmÜQATH?YW*é ¯  ' é ¯ Q A T  ą æ   & Ē DNMT1  Å ±  ç ì  +  # ç ì Ç *  ē
5-aza-2’-deoxycytidine (5-aza-dC)ĒDNA óò·5GP`&ý ('Z´ĒDNMT1 ÷DQ.W]ÿÜt¸è'ĒąæÌ©*ċ' DNA QATċ|'ē¡àâ$&Ē5-aza-dC  DNA óò¹ (S ¹)ÒÙÜ DNA ±p*ø' ) &Ē
5-aza-dC çìÊ©øÛ' á(ēºàâĒaďçì*×
5-aza-dC vÕ$&Ì©' DNA ±p¨äÄÂ*ö¼'*ÝÜē´ËXè½ 5-aza-dC çìÈ^'¢Č*ö¼'!Ēaďçì (HeLa, VA-13, m5S)* 5-aza-dC vÕēvÕ¤ 1Ĕ3 µ¤ÈÓj\ĒÖçì²ÎēJVY7.CQY?Y$&çì ¹*ö¼è½Ē5-aza-dC vÕçì S ¹_ G2 ¹oÆ' ) ēDNA±p$'A/B3M.WCÄÂÌ© ß%('ēĒ5-aza-dC vÕ$& DNA ±pø(' *ö¼'!ĒDNA bºĊy³NY1Y?WH3ú'SWĆI;
CW H2AX (-H2AX)*rÚïq¾îË$&Áwēè½Ē5-aza-dC Ð mÜÀu
-H2AX ĉ ~' %Ē5-aza-dC  DNA bºĊy³*ø' ) ē Ē
AB3M.WC2EY=?WH3ú' Chk1 Ì©*ĒSWĆ Chk1ser317 *°Ãö¼ēWestern blotting è½Ē5-aza-dC vÕ$&SWĆ Chk1 ĉ ~ %Ē5-aza-dCvÕ$& S/G2 A/B3M.WC Ì©' ) ē%ĒChk1 *ú'
A/B3M.WC ATR ċ|'1J/.W* 5-aza-dC tvÕ'çì ¹oÆû%ĒçìÈÓj\"x®%(ēh[è½ %Ē5-aza-dC vÕ$&Ì©(' DNA ±p¨äÄÂZã ¶% ēP 25BJ)+RGVTa#JLZ: LY:7b
N2W5gfXJH6 2f)09 2f*J@ 3 f" (_ 3 f\8. 3f<=Mgf
D2 ;g(1 &$0,/^I'[f2 ?![Of3 3CS[O)ÉÈ -$o] 3 st¥¯»Ă¦øÂ±Ãpw/ï PCR-DGGE ³)+±ÃqyPÀ,ÚåàĆĎ×½åàĆê« æ.-Ď¥¯»øÂ(stĎ~ÔúàĆ­÷$+Ĉ/f#/Ï(ª* 2007ĎÊ* 2008)ď§ËÑĎ±ÃqyP×½åàĆ¼/*ì ,&Ď±ÐøVÃÇqyÓ¿/æ,ôÃ) òÆ×½åàĆ/ DGGE ³)+ê«,ď-)+ĎÃÆô ) Æò
×½åàĆ­÷f#Ĉ/¢* ,/ÉÈ,ď³KÜ¬ ©cõË(SNĎ{¤)]ôÃĎQ²ßõË(SNĎÒ)]òÆ *hVqqy *^ DNA /ÂĎ×½å 18S rDNA º/ PCR xĎDGGE /æď*?J=@;LJÞëê«)+ĎôÃ ) òÆ×½åàĆ¼/¢* ďÜ¬ĎDGGE  [7JCH\ö?J=  è*-ĎqyÓ¿)*À,×½å}r ¢* ďMĎ±ÐøVÃ%*-ĎôÃ(òÆ¼¥?J='é-ď$ĎÞëê«Ü¬ĎôÃ({¤)òÆ(Ò)Ď±ÐøVÃÇ×½åàĆ -, Ïl-ď¥¯»øÂ(stĎ~Ôú×½åàĆ­÷$+Ĉ/f# (Ê* 2008)°ó,ĎÃÆô(ÆòĎ±ÐøVÃÇ,qyÓ¿Ď âÓ¿)+'×½åàĆĈ/O ( ¢* ďP 26
Asaia bogorensis K> UDP-    ] OQ
%F`fB\AEf\1 fPJcf-\U6d,4eÉÈ
 Asaia bogorensis ćÚ9HIL8B02?L/ÀÁ, Ďýÿå Gluconacetobactoer
xylinus °"ÀÁĀ ďenMĎ9HIL8jvð, UDP-5H6
L8WÝmĉ, á *-,ď§ËÑĎåU] UDP-5H6L8/j, A
bogorensis  UDP-5H6L8AIB38B3GFL:ċUDPGPČ¯ãê«/æĎUDP-5H6L
8À9HIL8ÀÁĄX/ê¢,/ÉÈ,ď³KÜ¬ 292 1E>ÿ *,Ø 32 kDa ;J@4ð, A. bogorennsis  UDPGP /,&ĎþÙûT|/ pET21a D4;LZĎ-/Â{äå BL21(DE3)pLysS /ðòď
Û¹ 0.1 mM IPTG )+î/æ 37 12 £ăuĊÜ¬ĎåUÍÌµi¸Å_ 32
kDa ÉÈ;J@4ð *-ďÕþÙ/Â G1P * UDP-5H6L8!z´/NADPč NADPH üY,g/Â¶Ü¬Ď182 U/ml ď$ĎRñ·Ä¨
UDPGP k® Mg2+¹)+´ zb,'Îíď ĎÕþÙ½d¡
{d CI<1L:)+_ê-$ &Ď¾rāCI<1L:ą`, EDTA 
/a Öç/ù&,ďP 27
Cellobiohydrolase I  cellobiose phosphorylase I  1 YGH[ LO^,'"cDZCEcZ`)c$V#:cMJ_c?F7+c/ZU6a&.4b·¶  õ=LMP<ÁC14G< )Ë/+4K:Àó8L9;L6;MP<õGXô/æÂn+¹»/Ó öëõ=LMP</ Cellobiohydrolase IóEx1ô(e×=ME4P<óG2ô/+Ö + õEx1 ±­+ G2 (ê|,#rî öõ¹» G2 )8L9P< 1 KNçóG1PôgKNçe×+ cellobiose
phosphorylaseóCBPaseô/ Ex1 ok+õ=LMP<h¯¶e× GX ±²
ÖUé²­+ G1P "v/Ú$ö¤OÅ
 ¹»_³æÂ Ex1 j! CBPase õ,,å[xÄ /³òÑ Aspergillus oryzae(*±²ötÝÅ=LMP</³õk±­ TLC (ºÛöEx1
 CBPase Ïä pH ,, 5.0õ7.2 +ö pH 6.6 Ü 10 mM KNç5K2I
ÈÔ¦(PPB)/³mæÂk/¡à-õTæÂ& pH 6.6  ^³+/ºÛö10 mM PPB (pH 6.6) Å=LMP</ 0.2 wt%+(ª Ex1 /§gõ
30Q{ékõoQkÁ CBPase /â§gk/ÆÇöÅõ
CBPase §gf Ex1 (+=LMP< ) G2 "v V]*õCBPase §g G2 )G1P "v/ºÛ+ döY TæÂ/³ckÁäZØ/ÓX{+öP 28
D-TDQXQ -K0(
BS8-* -K%I D-AP
NJ>R 1c@5;6 2c.19 3c=&< 1 a1 N!.\4c2 ]2.\Wc3

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Pyrobaculum islandicum ´ D-FMKNÌ£ÂæÂ/l*Rõ3JPFMPN¤(+vµ~a(*oæÂË/v+(*õD-=KN}+ñtÝ®µ/·ö¤OÅ
 JN>Ivµ~a¤ error-prone QuickChange ¤/³ö),u²­/¿ÕõÝß/ö),9MAP D-FMKNõD-=KN}+Ì£ÂæÂ¥/¡àØ+õ<7KPAN8/ÓöÅõTtÝ}+¥ pRvµ] 14 ºÛ,ö°sõ) D-=KN}+¥pRl/ã%+ö

P 29
 b\_  Siglec   4 >FL!I9* ;h6 ?Ch2Y3Sh[7^hd7"* (+)50181OTR)ÍÌ Ē×ÞæîċÜćð*) 'ĕhn$·nÞæ¾+q¦ n( Î&)(Ė9-QăĕÜć¨Öxĕùĉë%'Þæ±ç÷ÚĈ*(Ąïh(Ėv\č9-QăàsR3>T Siglec [eÇÞæîċËÀ 'ĕ
LPS $JI>A4P1T%'õ)(K3SG,V:»É+j ( ®ó¤& (ĖW£ĕ.T;PTĊÙ(II y)ÜÈ$Ø­}ĕì ¥µÊÂ·ãÈĕêñÒ»É ow(ö þ§l(ĖEQL>Tă$;?-PTă×ĎđÅªďuèåă TLR +_»É+ û|t) 'ĕ©ÏÕ)&°»Éõ¼ú%(K3SG,V:·n+ Siglec
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»É8.@1.T IL-10  Siglec %'õ)Ė!ĕĎđh(EQL>Tă%ÃÂ)( TNF-ĕSiglec ËÀÞæ b Ñ)Ė

P 30
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3PVCT4%'r¬-<>Q<QSV;ēCAĔ+{ú]²;3PVCT4
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L-AspDH %.F8§Nh pEAF1838 %¯MnCl2 % Y DNA >B@AF3n%OH tDFBE-/F,Cdm%¯dm%f%o¢¤w #¯§Nh¨XVPAE5?e lU $ePA(<ABF%Q°p1,
BF9E- ¯q!$ 750 eP 43 eP©s^G ¦ pH
eZ ¡ $°`¯ !#®sP]q eP |%#°P 32
Electrochemical behavior of dye-linked L-proline dehydrogenase on glassy carbon electrodemodified by multi-walled carbon nanotubes
 Haitao Zheng1, 3, Leyi Lin2, 3, Yosuke Okezaki3 and Shin-ichiro Suye3, *(1School of Environmental Science and Chemical Engineering, Tianjin Polytechnic University, Tianjin
300160, P.R. China; 2College of Life Science and Technology, Beijing University of Chemical Technology,
Beijing 100029, P.R. China; 3Department of Applied Chemistry and Biotechnology, Graduate School ofEngineering, University of Fukui, Fukui 910-8507, Japan.)Purpose
As an essential component, L-proline is important for proper functioning of joints and tendons. It not only
implicates some disorders in human body, but also a practical subject in food and pharmaceutical industries.
An electrochemical biosensor based on nanotube-modified electrode was constructed in this research.
Experimental and results
A glassy carbon electrode (GC) was modified by multi-walled carbon nanotubes (MWCNTs), and the cyclic
voltammetric behaviors of the modified electrode were investigated. A redox pair of peaks was found clearly,
which was owned to the oxygen-containing functional groups on the nanotube surface. Recombinant
thermostable dye-linked L-proline dehydrogenase originally from hyperthermophilic archaeon (Thermococcus
profundus) was further immobilized, and the modified electrode (GC/MWCNTS/L-proDH) exhibited
electrocatalytic properties to L-proline compared to bare GC, GC/L-proDH and GC/MWCNTs electrode,which suggested that the presence of MWCNTs efficiently enhanced the electron transfer between the active
center of L-proline dehydrogenase and the electrode surface.

P 33
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R

chaxine A (1) : R=

HO
H
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O

H
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O

H

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2 : R=

P 34
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D1ARMÖÜÏci§Ïã"#jb.³ä$ãÉ£V FAã13C-FAãSAã13C-SA ã¿ÅVãÃÅVãÀV CAã13C-CAãFAã13C-FAãSAã13C-SA ã8PEMU 30 ^h8PEM¤|ÐU 120 ^¤| ¢x+>R: ),ãÄVã,ci§'U 30 ^U 120 ^¤|zË),ä» )ãtujYZÏci§ªZ\?NR8R_« +¾),äP 35
Enhanced surface functionality of soy globulins
through attachment of carbohydrates and fatty acid chains
Athanasia O. Matemu, Shigeru Katayama, and Soichiro Nakamura(Department of Bioscience and Biotechnology, Shinshu University)
Objectives
Soy proteins have been widely used as a source of highly functional proteins in many formulated foodproducts. For further industrial uses, it is desirable to improve their functional properties. Introduction ofcarbohydrates and fatty acid chains onto the protein molecular can alter its structure facilitating change inphysic-chemical and functional properties. The aim of this study is to investigate the effects of glycosylationand lipophilization on the surface functionalities such as emulsion stability (ES), emulsifying ability index(EAI), and water or oil-binding capacities (WBC or OBC) of soy globulins.
Methods and Results
Glycinin (11S) or -conglycinin (7S) were covalently conjugated with carbohydrates such as xyloglucan(XG), chitin and chitosan oligosaccharide, through naturally occurring Maillard-type glycosylation at
controlled temperature 60°C, relative humidity 65% and pH 7.0 for 7 days, or acylated with
N-hydroxysuccinimide esters of fatty acids (6C-18C). As the result, the XG or chitin oligo conjugates showedalmost 3.0-4.5 times improvement in ES but no significant difference in EAI. The EAI of 7S and 11S was
increased by acylation with increasing chain length of fatty acid. The OBC of 11S was significantly increased
by glycosylation with chitosan oligo but the OBC of 7S and the WBC of 7S and 11S were not improved. In
contrast, the WBC and OBC of soy globulins were improved upon acylation, except for the WBC of 11S. In
conclusion, it is revealed that covalent attachment of carbohydrates and fatty acid chains to soy globulin, 7S
and 11S, resulted in enhancement of the surface functional properties.

P 36
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acid Éĥ{ Ö 2, 3 %ÅđĆÀ.ôÁĤ{ Ö 2 { Ö 1 3SMESĔ
niĤ") D14 Ėñi* Ĥ"{ Ö 3 { Ö 1  6’-O-malonate *Éĥ

P 39
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R2 OOH          

R 1

R2

20(S)-Protopanaxadiol 

H

H

Ginsenoside Rc

 glc-2-glc

glc-6-araf

R1O

FigĔ1 : Chemical structure of 20(S)-protopanaxadiol and ginsenoside

P 40
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-Ĕ
NH2 - GL - EQAF - CNL - KF - KQNVNRPS*RADVF - NPRAGRINT*VDS*NNL - PIL - EF - IQL S*AQHVVL-YKNAIL-GPRWNL-NAHS*AL - YVT*RGEGRVQVVGDEGRS*VF - DDNVQRGQIL VVPQGF-AVVL-KAGNEGL-EWVEL - KNDDNAIT*S*PIAGKT*S*VL - RAIPVEVL-ANS*YDIS*T*KEAF - RL - KNGRQEVEVF - RPF - QS*RDE - KERERF - S*IV - COOH

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