Jounal of life Science 2009 Vol. 19. No.9. 1321~1327 us /1SSN 1228-9918 QS CHAt S+ alcohol dehydrogenase (ADH) % acetaldehyde dehydrogenase (ALDH) Sol] O1A1= OFA] Sst AMG BOs - BME - IAF - ASEH - OS" HERG EOE Received September 2, 2009 / Accepted September 8, 2008 Effects of Amino Acids on the Activities of Alcohol Metabolizing Enzyme Alcohol Dehydrogenase (ADH) and Acetaldehyde Dehydrogenase (ALDH). Jae-Young Cha, Hoe-jung Jung, Joe-jun Jeo Hyun-Ju Yang, Yong-Taek Kim and Yong-Soo Lee*. Technical Research Institute, Daesun Distling Co. Lid. - The present study examined the comparative effects of various amino acids on the alcohol de- hydrogenase (ADH) and acetaldehyde dehydrogenase (ALDH) activities of yeast Saccharomyces c= cvicice and rat liver homogenate in cifro. Methionine showed the highest activity in yeast ADH among the amino acids used in this study, but this was not higher than that of the hangover product, Condition-Power (CP) used as positive control. Methionine was also found to be the best amino acid in terms of the ALDH activity in rat liver homogenate among the treatment amino acids, which was comparatively higher than that of positive control CP. It was chosen for further experiments and yeast ADH activity increased in parallel with increased methionine concentration, but not rat liver ALDH activity, and it was comparatively higher than those of the positive control. Arginine showed the highest values in yeast ALDH and rat liver ADH activities among amino acids, and it was chosen for further experiments, Yeast ALDH activity increased in parallel with increased arginine concen- tration, which was higher than that of positive control CP, and rat liver ADH activity was also com- paratively higher in all treatment concentrations of arginine than that of positive control CP. The na- tive electrophoresis of ADH and ALDH from celhfree extracts of yeast Saccharoyos ceeisae cultured, in the growth medium containing various arginine concentrations by 0~0.1% showed two active bands upon zymogram staining analysis, and the straining intensity of ADH and ALDH active bands in anginine treatment yeast was stronger than that of non-yeast or low treatment yeast, These results indicate that alcohol metabolizing enzyme activities can be enhanced by arginine and methionine, sug- gesting that arginine and methionine have potent ethanol-metabolizing activities. Key words : Alcohol dehydrogenase (ADH), acetaldehyde dehydrogenase (ALDH), amino acid, arginine, methionine 42 FE $9 42 S84 Ueye dee daa aI Aujol Bole VAS] 80~o0Le ALA SA 22 bs) betel ae GEL oe alcohol dehydrogenase {ADH} s]88 WA) acetaldehyde ASH] 91M SS] WO S45} Ag AR GOS —_ BAI, CH] aldehyde dehydrogenase (ALDH) Hel 2] Sad Sc. Payt EAT IE VALS HEAR A slo) aac aids BAL F olMaHEAS E> Se Ba) Aol RASA Zoe renobiotiad] @ SAE — Leh Io} Vas] Lobs}gS AA aoH2}. eels] st cebldchydes} 22 HALES al GIAEMAM Ie MIE AS, SE, Fe SF Ada 9S waa a AZGUS FISH FA ULOS Vela HD]. Isto ole BEF Sa ALE HG Sa mY IEA dale, Se MAGA whol SAA Shel AOS OA Eloi ld de ed arial md a FE wel Fas 4 a8 1 AMMO Bs ey Ae nie GLO a Ry) Fea UE Bee ad wa otinamide adenine dinucleotide phosphate (NADP) 3 ace- ake}. He] Pel HBS Gee wave bldehyder} HAM 9 OMI AP CSS AY Gee FRA HE Sa] ARE shal ALAM, Blo, Moll] 2) $2. PAZ BRS SAlo] HZ Deal acetaldehyde ‘oh IDS] SS ol Bs: zhao] GE Seta om, SMe HA SBS BAG CUES Man, 8, AP clea RH FSETY HBSERE Aaa AZ ——_—av.$§$§$~ eNgE muse vasa ae vee “Coespontng author PARES GSA ABS] LS ADH BA ei AB HV e Aa Ae] YHO14 OU, OF EVA 41322 -BBTIAEIT] 2009, Vol. 19. No.9 AOE Lait FHSAL acetaldehydes 2% 22 ge} 4 Slo] ALDH RA BIS SAG Aol 2alel Bo} aot ECL. eA IML 7H UPA G2) OLE ADH HA GY Sawa oe} ALDH BA BYS HA Sal Aas aloleb #4 she Alama Ol GAL SAA FZ aspartic acid, aspar- agine, glycine 3 glutamic acide] 4@s}o} 2 BS Rah se Bae WAbel eee] Me Ree uD sison}oi02128), lS % arginine, aspartic acid 3! glutamic acid: of .4-e} Saale Ahoz Z Well BYE, Mo}! dust Se £9 GAUSS FA opltlow AS d SAA Wal Meas} Ie lee vod y goult6, ola}e] Fo] UY opolscked ealo] BsLe Aol hale Bo) REFS UE Bold. Heyy, B BPAL AZ Bol BHC IAS Ae oles BAA Ysts Ao} WE ADH 8 ALDH 4 B40 oie IOS in vito AMAA BEAM, SA AA SYS] Ms ao} AWS SMe SRE Fela] Besa. Me Sobel wal me YRS Bo BUR RA yeast Sarharomyos cereisiar rel ADH 8! ALDH SigmaAl(Sigma Chemical Co, Saint Louis, Mo, USA}o1A}, 21212 2 $9 rat liver homogenate 4% Molfox Co, (North Carolina, USA)AA FAA20}, 2 ABA ABE ofl: 1082 AjinomotoA}(Tokyo, Japan) AES Fs AG. FAA See delat SALARY FY PH RA I BadLTS Ae asia. 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ALDH ata oi ADH 3 ALDH #4) G4 920) Saccharomyces ver cvisine KCCM 11350 9. 4-8 YPD (yeas extract 2%, polypeptone 1% § dextrose 28)o14) a Ala] ash A121 YPD Hh}of arginine? O~01% SEL BIA CHA IBA LMG AE. Moe AS BAS AER HUGE 38 MAME BALL 148} sonicator} | AB SE GE OS 5000 pmol 20! a1AEel aol BS 4S 915 sate}. AR Beto) Ula ee bovine rum albumin g EER so} 3YsAHLL8], Native pol- yacrylamide gel electrophoresis: Gennady} *}415]0 th #3. shah] ADH BE ALDH WHS 22} whey 75% slab-type polyacrylamide gel A}2-3}0] Trislvcine @&a (25 mM Tris, 192 mM glycine) @l]44 1.5 mA/gel (cm)2} BATS Fo} Ph, Co} WAGES sake. ADH 23 FAS 05 M ethanol, 7 mg/ml NAD’, 25 ug/ml phena- zine methosulfate (PMS), 2. mg/ml nitro blue tetrazolium chloride (NBTC) 2 60 mM Tris-HCl (pH 8.6) te zy- rmogtam staining solution ®.=. 25°Co}4} 14)2 WS-A}.2.04, ola Ga) bande: blue bande Veh Hs AS APS 8}Sh th 6] sf ALDH @49 24S ethanol lel 71424 05 M acetaldehyde 4499), Yo}2) WES ADH BA a 3 EVal aaa. BANe| QaezHe} dole Ae oneway ANOVA Z¥al 9} Ee VTAD MEQAMesSE)E LAL AAHUL aaa ze ADH S0H OIE Ofo|scdto] oat Ae $48 VIS PHS Sabb AQoLA] BFS) of ULE OES F aS AA Bal Shed, baled URS MAL WIL HHA Ue SS RaL # YHD) VA MA s|= Bae Bole Wa] ADH cy-tochrom P4500] 9}8 @st2o] acetaldehyde? Aes} e 0), ln 4A acetalehydes] SA AROSE eh Be, , MAmg, Uae So] debated Gal sel ueh eb chat SIE 715 AAS Me Be, AE 34 71S Aa Mt Solslety). 2 2A Date WAP = Wa ADH #44 AGE FE Ade JA aad > SVEALSA), AeA VL BA, LAU, SAG, P71 A, BE S91 WE AD FHL Tas AH 440] DE ALE Gels HIF 1726. Ke SHS, che, FMR $9) ABA AAAS AY. Spel ADH BIS FAV] ale asp} 32 YF a1eH(n SHde Gao] Fa SAS esa Ve WIE a FE89] VF UES ADH BUG ALDH BAS ¥] Sa]OEH 2A acctaldehydes W]7 S2i3h 2d) $us) Apt die Aes uel ago, EE AeE SpRHES} $4434) ADH Wl ALDH F 2 BF gS 4486] slalom), ADH 84 4a Bee 4a del ABS|z2 Slt abled FORE FHA 5% USES ME Woe BD AL a, Ades 89] FA opo|.eAIel aspartic acid A71S}o} ADH BIS Bd Bh NLT GE 4G 2) 1979%01 Blah AZ aspartic acid 1% 7}94 18H MAKE. BA] OE S7AHL at, ALDH #42 1% aspartic acid 27} 2} 168.4% 2 ate|], AS] FH 79 bel 28A) aspartic acide} 3}3h AS Salle $2 DHS 1s + DatdD atc, ADH @4}2 Go", Zn", Co BH} LE vl AEA 9] a 2A Salsi7ty AAR He alow Vela} sl ADH BS FAA Ziel Go} opel ARES APS RF WAZ FH3HEU), aspartic acids} alanine NAD*9) Aly 2210) 9}@: NAD'/NADH ¥| 2 37} @lét ADH #3 & V4 Pao] LoS Fel-]1xL2}, asparagine’ acelaldehydes} W2s}o] PLES Waste =e) SES Whol S48 Hepes Wee va yalg PML AeA oho) Sala] 4 aspartic aid, asparagine, glycine '! slutamic acide] S5}o] 2 WE Ba} 3 RS ashol Go] se AOE UR AsiaLIO1628) APH Saleh dou ddd WUE, Hol FSH] Fa beled arginine, aspartic acid 8! glutamic acide: oot 3} Zh BE Sop} la IAAL ola) Be BieSI oboe SA 8] 14 opeltlel Febsto| see bel elatte 489] BE so} LS Belch ADH RS] Aha a AS Sol Ge eA eben, & adalae ADH BA 4157} M4) Se yeast 3 rat liver $245) BAR AGSlo| old SHY BASS Hla Bas BEstAC. Rat liver sels] ADH BAS oped ola} arginine A2)-Fo14} 7444 $942.4 Fg. 1), arginine 217} Jounal of life Science 2009, Vol. 19. No.9 1328, ES Gelso] ADH RA BAS 498 astye 10 mg/ml 914} 120683 30 8! 50 mg/ml AI 232+ 119% 1%} FIL] 6% We} oI ee ROS Ue}steH Pig, 2. eel, ADH Be aspartic acid 05% a2] fol 1U38el Wey Ike Ae] BES eel BEE WAZ DESAY Vo] RA WS FE Yolalen, AAT aspartic acid 0.5%, 1% YW 1SKE A} HR- of ADH #4) Bal Rohe 2H} 198%, 1263% ¥! TSS, Wa See S7eh et ood z EEE Bel Moai QHS Bel Bol arginine HE ols} Ab @-4G22 Vel 10 mg/ml o}B5] EAI ADH Bo] of op alsya| We lew sbsto} AHP] est Hels] ADH #4 SOV aelel oblscat FolA| methionine AAPA 156182 7H HE BIS UBOU, BARAT 9) 168% Bote BF ORE Ue 9S Veh A sieH Cig 3) ‘}e}4] yeast eh) ADH #49 3-912} methionines| Az] BSS Vaqe Wy, 10, 303 50 mgfml FEA 2p ¢ ot LOLI SEG SE Fig. 1. Effects of water-soluble amino acids and hangover prod: uuct Condition Power (CP) on the alcohol dehydrogenase (ADH) activity from sat liver homogenate. Values are ‘meanéstandard deviation (193) | | | | Arginine (g/m Fig. 2. Effects of various arginine concentrations and hangover ‘product Couition Pacer (CP) on the aleohl dehy drogen- ase (ADH) activity from rat liver homogenate. Values are meanéstandard deviation (93)1324 -8BIIMEIT] 2009, Vol. 19. No.9 Fig. 3, Effects of water-soluble amino acids and hangover prod ‘uct Contin Power (CP) on the alcohol dehydrogenase (ADH) activity from yeast Saccharomyces Values are meansstandard deviation (a=3), 1563%, 196% 3 MSGS BE ACE SE BE & 29204, 30 3) 50 mg/ml Fz] SEAS BZ T 165.8% Bx} ee BAS UeHHIHg 4 ALDH std o/s ofolicalo} sist Aol SH, SLO] UES Zo] ADH Bol s}8 acelaldehydes. 2148) #8451 cg ALDH Rebol 23 Agee Sle 192 AAA aD] OF F AMaoe LIE GA SIL acetaldehydes] $Y 4404 Oe glo] = 70 NMG 43] AAS ALDH £4 BG BH Sa Aalenl Aaho) BRA ee. we} acetaldchydes} 2 aol VBA AES vale ALDH RA EOL oa 2h oho etl9] 4 LESS. Rat liver $219] ALDH #4) AAG A oblts] BBE VER WHs 9), 1B o}e)ie Abt Sol methionine TAA 7H ee. Hl & GLC. Methionines} 37} 31 48el AAS 10 mg/ml 144 30 3! 50 mg/ml 7} BEA Boh ee HIS Bale Methionine Go) Fig, 4. Effects of various methionine concentrations and hang- ‘over product Coit Power (CP) on the alcohol de- hydrogenase (ADH) activity from yeast Saccharomyces cerevsie, Values afe meanstandard deviation (03) oo LLL S oY Fig 5. Elects of water-soluble amino acids and hangover prod: uuct Condition Power (CP) on the acetaldehyde de- hydrogenase (ALDH) activity from rat liver homogenate Values are meantstandard deviation (r3). 4, oF BE Az] SR ALDH BS QadT we 8S3) Ze BYS UMcHFig. 6). 441 yeast #2} 9] ALDH 89 SUA 4 opolcaba @ elt GL9U, arginine 4 Se BAS VAC(Fig. 7), Arginines) AE SE BANE Ae SE SALE yeast HA] ALDH Bo} ty BBE 2 BRO, SQdsF Bo se AS Yeh Ag 8). 1G AFA ABS telat SAA arginines} methionine 24214] slslx) ADH SE ALDH #492 Sa7l= ee Yehted, & bea Aa APolAl arginineS 70% o]4 %2)8}it Ne FAS Eng gol dal Fold dbeys z 24 Fo] ALDH BAS Fad Ae LE, in vito PAINE E438 BLA) yeast als] ALDH BAS Saale ahs de YF alo} QA Asbo} e118} sHe4 (data not shown) Arginine 2/0 (HE BS ADH 8! ALDH wa S44 o}oieat SoA} anginines) 38. sree] ALDH #49} rat Fig. 6. Eifects of various methionine concentrations and hangover product Conition Power (CP) on the acetaldehyde de- hydrogenase (ALDH) activity from rat liver homogenate. Values are meanstandard deviation (a3),LOELE Gof OEE? Fig 7, Effects of water-soluble amino acids and hangover prod= ‘uct Contin Poawr (CP) on the acetaldehyde de- hydrogenase (ALDH) activity from yeast Saccharomyces cerevisiae, Values are meantstandard deviation (n=3) 0} ‘| | | | | wot of 300 Coots 10 ‘Arginine (aim) Fig. 8. Eifects of various arginine concentrations and hangover product Contin Power (CP) on the acetaldehyde de- hydrogenase (ALDH) activity from yeast Saccharomyces cereisia Values are meansstandard deviation (n=3). liver $242] ADH #48 Sale Raph aston, ole} HA OY Ale B29 Aq SE BA] Ao] o17]U} iso- zymes) 2}o]o} 9}@ OE AS7] oho} ole] gh & Yepw7] fale} zymogram staining Yy.oz sela}gh Uh. YPD slo arginines O-O1% FEZ BA Me ‘AY E404 ADH BA 4S 5 AO) Fa dee UE 20), 8 GY BEE arginine FA7} LE AGE (O05) ariel Plal OM 2125) 7} SEAM AeA Yel BA Bo) G7 Asse Use AHS WS + sNsHHg. 9). ALDH #4 G4 445 ADHS} She Aes Ach Fig, 9). Rt arginine 0.01% 9}$2] 27} koa ADH Bt ALDH 3 #4) Q4 QE7E OHI Boe AS Ba ee, oleh AR A 71h 419 A SEL HE srt adel Suet @ oe Aes ae. Oe, ADH #4 249] BF Bed UIg WA AL 5. ar evisine RA-7A-2 3 BRA S. cerevisiae D THA 2749} FR WEE AZ ELSA, S. corevisine D HS SPC ME Joumnal of Life Science 2009, Vol.19. No.9 1826 son ALDH Fig. 9. Alcohol dehydrogenase (ADH lef) and acetaldehyde de- hydrogenase (ALDH; right) activities zymogram band patlers from cell-free exacts of yeast Saclaronces cr «vise cultured inthe growth medium containing various arginine concentrations by 0~01% (/). BO IMC MOA ANA BA a4 Yer gratsle UY, S. conaisne RATE B49) BH MF SEA I 2] = MAdH IAAL) EF wey eae YE aoa Kiayooromyers marcus RAIS? #42] ADH #4 4 BE ES. cerevisiaes} CHE PES Mo} Kluyveromyces marsians $99] ADH HAAS 2a gle 2oe Bo} ach wey AY $e ALDH 8A YS Sa FSS 1a angle ined: 9. Wopel 7A BS AL Wy ALDH dt E7t S7HEOZM arginines ALDH BIS aalzhis 541 invieo DUA ABMS WHE SZ sale, 49] 2B Asbo bole AL F anginines} methio- nines] ADH 3! ALDH @4 4a14}71% 4-84 sl 32 MOE Ne Oe AE SHA STE ace. taldehydes) Bohs alee 7540) oh 2) oA Bt Ed us ade le dee Ny ga ad. ay] arginines} methionine #5} Bol 784 st BY ad MA Qi} gus ASS Hel 7s MS SAS SLE 24 2 SPE Salelto] $e lez Weld AB AAs) FA oieS Eee] RA BAA IFS viAE We Qa owiete Aes, 22 WS ee © yeast9} rat liver #249] ADH 9} ALDH 25 aoe ase Wl aa A Eo Sa Rabl sto} ae BAL. Rat liver $12] ADH BAS Alea cheek Soh 4} arginines*] 7) $9}. Arginines} 7} SSS Bele o| a PRS SVE Bs} 10-50 mg/ml EAA 118~ DOLE HAAS FS| HY Beh oI we Bez Yet Uh SEAL, yeast hehe] ADH JS methioninest 4 7H $e BAS UA, methionines} 2] SES BIE VHA1826-8 BIMELIA| 2009, Vol. 19. No.9 Ae WEBS JEACE BE BAS Val. Rat liver #2] ALDH #41 methionines| 74 2 BAS watch Methionines| 7} S58 48O4E 10 mg/mle} 30 50 mg/ml 47 FSM Deh ee YS WA, BE Ae SSA GARTER AYS we BASS Sth. Gal yeast al] ALDH BAS 2} oh] @ Ao] MOU, arginine} eS BAS Vc. Arginines} B7} SEY SRANE Aa] SE ASALZ zo] ry S7ishe BOS Uslon, dader Ud we BGS EhYSICH LL sh ALDH 3! rt liver fr ADH BA 2 Swit ASS 7a anginines RS MA 7D MEW ALDH 3! ADH &4 ql) 27} Shee arginine: ALDH 3! ADH 43% 24] 752 BO] in viow AMAIA BIAS ogo] A astola obelead S 144% arginine} methionine] ADH 3! ALDH a2 &2l Ave AG 6h StS BolAeNd o}1) 2} acetadehydes} BAS Sz eA] So} Salsa Boke HED 2 RSE EAol 1S Rez AA} Mo} ach whe} arg nines methionines} BE oh): 5 MBL SHA 2 4F Gals Bas} dws BSS WL BE UehE # 1G eve] ASTI. References 1. Bergmeyer, H. U. 1974, Methods of Enzymatic Analysis. Academic Press, New York, pp. 28 2 Cha, J. ¥, JS. Heo, and Y.$. Cho. 208, Efect of zincen- riched yeast FF-0 strain on the alcoholic hepatotoxicity in aleohol feeding rats. Fea! Sc. Bitedinl, 17, 1207-1213. 3, Crabtree, B, and E, A, Newsholme, 1972. 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