Tp ch Khoa hc i hc Quc gia H Ni, Khoa hc T nhin v Cng ngh 23 (2007) 75-85

Tng lai ng dng Enzyme trong x l ph thi

(Tng quan) Trn nh Toi1, Trn Th Hng2, *
2 1 Vin Ho hc, Vin Khoa hc v Cng ngh Vit Nam, 18 Hong Quc Vit, H Ni, Vit Nam Trng i hc Khoa hc T nhin, i hc Quc gia H Ni, 334 Nguyn Tri, H Ni, Vit Nam

Nhn ngy 2 thng 4 nm 2007

Tm tt. Ngy nay, tc nhim mi trng ang gia tng, do cn phi thc hin nghim ngt cc tiu chun i vi vic thi cht thi vo mi trng. Cc phng php x l ho hc v sinh hc thng thng ngy cng kh t c mc cn thit loi b cc cht nhim ny. Do , cn phi trin khai nhng phng php x l nhanh hn, r hn, ng tin cy hn v vi nhng dng c n gin hn so vi nhng h thng x l hin hnh. Hin nay ngi ta bit nhiu loi enzym khc nhau ca thc vt v vi sinh vt. S lng enzym bit t ti con s hn 3000 enzym. Cc enzym, c bit l Hydrolases v Oxidoreductases c tc dng c th trong x l cc nhim bng cch kt ta hoc chuyn ha cc sn phm phn hy cht thi. Enzym c nhiu trin vng ng dng trong tng lai. Mt s enzym c ng dng thnh cng trong vic x l cht thi. Tuy nhin cn c nhng nghin cu tip theo tm ra enzym c hot tt nht v ti u nht trong thc t s dng.

1. M u Ngy nay, tc nhim mi trng ang gia tng, do cn phi thc hin nghim ngt cc tiu chun i vi vic thi cht thi vo mi trng. Cc phng php x l ho hc v sinh hc thng thng ngy cng kh t c mc cn thit loi b cc cht nhim ny. Do , cn phi trin khai nhng phng php x l nhanh hn, r hn, ng tin cy hn v vi nhng dng c n gin hn so vi nhng h thng x l hin hnh. Nhiu nghin cu chng minh c enzyme c nhiu kh nng v trin vng gii

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Tc gi lin h. T: 84-4-5583001 E-mail: tthong@vnu.edu.vn

quyt vn nu trn trong gim nh v x l nhim mi trng. Hu ht nhng quy trnh x l rc thi u s dng mt trong hai phng php ho l hoc sinh hc hoc kt hp. Phng php x l bng enzyme l trung gian gia hai phng php truyn thng, n bao gm cc quy trnh ho hc trn c s hot ng ca cc cht xc tc c bn cht sinh hc. Enzyme c th hot ng trn cc cht nhim c bit kh x l loi chng bng cch kt ta hoc chuyn chng thnh dng khc. Ngoi ra chng c th lm thay i cc c tnh ca cht thi a chng v dng d x l hoc chuyn thnh cc sn phm c gi tr hn. Phng php x l bng enzyme so vi phng php x l thng thng c nhng 75

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u im sau: c p dng i vi cc hp cht sinh hc kh x l; tc dng c vng nng cht nhim cao v thp; mt s enzyme ring bit c tc dng trn phm vi rng pH, nhit v mn; khng gy ra nhng bin ng bt thng; khng gy ra cc cn tr ph v cn bng sinh thi. Trong bi ny, chng ti xin trnh by ngn gn v vic nghin cu ng dng mt s enzyme v nh gi mt cch c bn tim nng ca chng ng dng trong thc tin v tng lai x l cht thi. Cho ti nay, ngi ta bit c khong 3.000 enzyme. Tt c cc enzyme u c gi tn v c xp vo H thng phn loi gm 6 lp (class). Trong cc lp c cc lp ph (subclass), nhm (section). Mi enzyme u c k hiu phn nh cc th t phn loi trn [1]. Cc cht c hi trong mi trng thng l cc cht hu c c vng thm nh cc hp cht phenol, cc amin vng, hoc cc cht hu c phospho. t c mc ch x l mi trng, cn phi ph hy hoc loi b cc cht c hi nu trn. Cc enzyme xc tc phn ng oxy ha - kh thuc lp 1 (Oxidoreductase) v cc enzyme xc tc phn ng thy phn thuc lp 3 (Hydrolase) c vai tr tch cc trong vic ny. 2. Cc enzyme Oxidoreductase trong x l mi trng Vi ngha i vi cng ngh mi trng, trong lp Oxidoreductase c th k n cc enzyme peroxidase, cc enzyme ny c ngha quan trng. 2.1. Cc enzyme peroxidase phn lp EC 1.11 Trong s cc enzyme peroxidase, u tin phi nhc ti Catalase. Catalase (k hiu EC

1.11.1.6) xc tc phn ng c hiu phn hu H2O2 [2]. Ngoi ra, catalase cn c th phn hu formaldehyde, formic acid v alcohol. Cc cht nu trn l nhng cht c hi vi mi trng, c thi ra trong nc thi ca cc nh my ch bin sa, pho mt hoc cc nh my dt, si. Catalase vi khun c tc dng tch cc trong vic ph hy chng. Trong cc enzyme peroxidase nu trn, catalase, peroxidase v manganese peroxidase c nghin cu nhiu phc v cho vic pht hin mt s ion kim loi c cho mi trng nh: Hg+2, Pb+2, Cd+2 , Cr+6, Mn+2 [3]. Peroxidase c ci nga (Horseradish peroxidase-HRP) c k hiu EC 1.11.1.7, tc ng nh catalase, xc tc phn ng c hiu [4]. HRP l mt trong nhng enzyme c nghin cu nhiu nht c lin quan ti phng php x l rc thi bng enzyme. HRP c th xc tc phn ng oxy ho mt ph rng cc hp cht thm c bao gm phenol, biphenol, aniline, benzidine v cc hp cht thm d vng nh hydroxyquinoline v arylamine carcinogen nh benzidine v naphthylamine. Sn phm phn ng c polyme ho thng qua qu trnh khng c enzyme xc tc dn ti hnh thnh cc cht kt ta c th d dng loi b khi nc hoc nc thi nh qu trnh lng ng hoc lc. HRP c bit ph hp vi x l nc thi bi n gi nguyn hot tnh phm vi rng pH v nhit . HRP c kh nng lm kt ta nhiu cht thi kh loi b cng vi nhiu hp cht d loi b hn bng cch hnh thnh cc polimer phc tp c tnh cht tng t nh cc sn phm polimer ca cc hp cht d loi b. Mt h qu ca c tnh ny i vi cc loi nc thi nguy him c chng t khi ngi ta thy rng cc cht biphenyl c polichloride ho c th b loi b khi dung dch khi kt ta vi phenol.

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Ngi ta dng peroxidase chit xut t c chua v d hng nc polimer ho cc c cht phenol. Cc peroxidase ny c kh nng loi b c cht guaiacol v cc loi r cy tp trung cc cht nhim phenol trn b mt r. Cc enzyme peroxidase c trong r cy c kh nng gip hn ch ti thiu s hp thu cc hp cht phenol vo trong cy bng cch tp trung chng ko ra b mt ca r. Peroxidase cn c s dng ci thin qu trnh kh nc bng cn phosphate. Cn phosphate cha mt lng ng k nh t st c th trng n c kch thc nh v v tnh sa lng ca n nn lm chm qu trnh kh nc [5]. Dng peroxidase trc khi x l bng cn phosphate s to nn mt lin kt c hc mnh hn gia cc phn t ca cht lng v peroxidase thc y mnh s sinh trng ca to v nm mc, c li cho vic tp trung cc phn t, to tnh nht v to gel. Nh vy, khi nht tng v to gel s gip cho vic to lp lng cn. Chloride peroxidase (k hiu EC 1.11.1.10) xc tc phn ng c hiu [6]. Ngoi kh nng oxy ho mt vi hp cht ca phenol, Chloroperoxidase t nm Caldariomyces fumago [7] cn cho thy kh nng xc tc cc phn ng vn chuyn oxy nh phn ng oxi ho ethanol thnh acetaldehyd hoc oxy ho kh cc ion clorua. Cc enzyme phn gii lignin (phn lp EC.1.11) [8]. Lignin l mt trong cc polysaccharide ca thnh t bo ca thc vt, ni ng hn l mt polymer vng thm. Lignin l mt i phn t, c khi lng phn t ln hn 10.000. Lignin c cu trc nhiu vng thm, c c tnh khng a nc. Do rt kh phn hu. V vy, cc enzyme phn gii lignin c vai tr quan trng trong chu trnh vn chuyn carbon trn tri t.

V cu to, lignin gm cc mch phenylpropanoid phc tp, cu trc khng ng nht (heterogeneity). Chnh v tnh cht nn vic phn hu sinh hc lignin (biodegradation) cn i hi h enzyme oxy ha mnh. Trong cc enzyme oxidase phn hy lignin, enzyme c hot tnh rt mnh l Ligninase (Lignin peroxidase) v Manganese peroxidase EC 1.11.1.13. Enzyme Manganese peroxidase xc tc phn ng c hiu phn hu H2O2 [9]. Manganese peroxidase (MnP) xc tc phn ng oxy ho mt vi loi phenol n vng v sc t vng, nhng nhng phn ng ny ph thuc vo s c mt ca Mg2+ v m. Trn thc t, MnP xc tc phn ng oxy ho kh Mn(II) thnh Mn(III) khi c mt ligand lm bn vng Mn(III). Kt qu l to thnh phc hp Mn(III) sau khi xy ra phn ng oxi ho kh cc cht hu c. Ligninase EC 1.11.1.14 [10] (LiP) l mt phn ca h thng enzyme ngoi bo ca nm mc trng Phanerochaete chrysosporium. LiP c c tnh gy khong ho nhiu loi hp cht thm kh x l v oxy ho mt s lng ln cc hp cht phenol v hp cht thm a vng. LiP c nh trn cht mang xp ceramic hoc trn mng silicon, n c th s dng x l cc rc thi nguy him kh ph hy. 2.2. Cc oxidase thuc cc phn lp oxidase EC.1.1 Trong phn lp EC.1.1, L-galactonolactone oxidase (EC 1.1.3.24) c ngha i vi vic x l nhim mi trng. Enzyme ny xc tc phn ng c hiu l phn ng oxi ho L-galactono-1,4-lactone thnh L-ascorbate [11]. L-galactonolactone oxidase t nm men Candida norvegensis c th c dng bin galactose t qu trnh thu phn lactose trong dch sa chua thnh axit L-ascorbic. Enzyme

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ny c th nghim x l nc thi ca nh my ch bin sa. 2.3. Mt s enzyme phn lp khc: Polyphenol oxidase Cc enzyme polyphenol oxidase l mt h khc trong nhm enzyme oxy ho kh c kh nng xc tc cho cc phn ng xy ho cc hp cht phenol. Cc enzyme ny c chia thnh hai phn h: tyrosinase v laccase. Hot tnh ca c hai h u cn s c mt ca oxy phn t nhng khng cn c mt cc coenzyme. Tyrosinase c k hiu EC 1.14.18.1 [12] cn gi l polyphenol oxydase, phenolase hay catecholase xc tc cho hai phn ng lin tip: phn ng th nht l phn ng thu phn monophenol nh oxy phn t thnh cc o-diphenol v phn ng th hai l phn ng dehydrogen ho cc o-diphenol nh oxy thnh cc o-quinon. Cc quinon thng khng bn v b polime ho khng cn enzyme thu c cc hp cht khng tan trong nc v d dng b loi b nh qu trnh kt ta n gin. Tyrosinase c nh trn chitosan cho kt qu x l hp cht phenol rt hiu qu (loi b phenol 100%). Vic c nh tyrosinase c u im trong vic gi li c cc enzyme trong bn th phn ng v bo v chng khng b mt hot tnh khi thc hin cc phn ng vi quinon. Tyrosinase c c nh vn cn gi c hot tnh ngay c sau 10 chu trnh phn ng. Do vy iu ny cho thy s kt hp gia tyrosinase c c nh v chitosan l mt phng n c hiu qu loi thi cc phenol c. Laccase (EC 1.10.3.2) l mt enzyme kim loi xc tc cho phn ng oxi ho hydroquinone thnh benzoquinone [13]. Trong trung tm hot ng ca enzyme ny

c ion Cu2+ tham gia. Dng laccase c nh trn cht mang x l cc thuc nhum anthraquinonic lm gim ti 80% c ca cc thuc nhum ny [14]. So vi cc cht ho hc kh c ca cc cht nhum vi th laccase c cc u im quan trng hn hn v x l bng phng php ho hc th hp cht azo ca cht mu nhum vi thng chuyn v cc dng amin tng t, m cc amin ny thng l cc tc nhn t bin gy ung th [15]. 2.4. ng dng kt hp mt s enzyme phn gii lignin - ng dng kt hp Peroxidase v laccase Qu trnh ty trng giy c p dng rng ri trong cng nghip nghin bt giy loi b cc gc lignin trong bt giy. Cc gc ny l nguyn nhn lm cho bt giy c mu nu v c loi b m t tn km bng cch dng cc cht ty trng nh chlorine v cc oxid chlorine. Qu trnh ty trng to ra dch lng c mu nu en cha cc sn phm b chlorin ho c v c kh nng gy t bin gy nguy him i vi mi trng. Peroxidase v laccase c tc dng tch cc trong vic x l dch lng sau qu trnh ty ni trn v dng c nh ca cc loi enzyme ny trong mi trng hp u hiu qu hn so vi dng t do. - ng dng kt hp laccase vi manganese peroxidase Laccase kt hp vi manganese peroxidase t nm trng Dichomitus squalens cng cho nhng kt qu rt kh quan phn gii lignin. c bit, laccase c th oxy ho cc hp cht phenol thnh cc gc anion t do tng ng c kh nng phn ng cao do Laccase cn c s dng x l cc hp cht Clo hoc phenol trong nc thi ca cc ch bin sn phm cha cellulose. Trong

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trng hp ny khi laccase kt hp vi manganese peroxidase c nh cho hiu qu ng k. Ngi ta s dng hai enzyme ny c nh trn mng siu lc polysulphone loi b cc hydrocarbon vng thm trong nc nhim bi du m [16]. 3. Cc enzyme Hydrolase trong x l mi trng 3.1. Cc enzyme thy phn amylose: cc amylase Trong cu trc ca tinh bt, khng ch c lin kt (1- 4) glucosit to nn thnh phn ch yu l amylose, m cn c lin kt (1- 6) glucosit to nn phn nhnh amylopectin. Do , vic thu phn hon ton tinh bt cn c amylase vi nhng tc ng c trng ring bit. Th d: Exoamylase gm -amylase v -amylase, y l nhng enzyme thu phn tinh bt amylose t u khng kh ca chui polysaccharide [17]. Cc Amylase l cc enzyme ng ho, c kh nng phn hu amylose v amylopectin, glycogen v cc polysaccharit tng t gii phng glucose. Trong s cc enzyme , mi enzyme c mt chc nng phn bit. -amylase (EC 3.2.1.1); -amylase (EC 3.2.1.2) tc ng lin kt (1-4) amylose ca tinh bt, -amylase ct tinh bt thnh dextrin, cn -amylase ct tinh bt hoc dextrin thnh maltose. Maltase tip tc ct lin kt (1- 4) ca maltose to thnh glucose. (1-6)-gluosidase ct lin kt phn nhnh (1-6) ca amylopectin to thnh cc on amylose [18]. V vy, cc enzyme ny c ngha quan trng trong vic phn hy ph thi cha cc ngun tinh bt t cc lng ngh lm bn, bnh a, bnh cun, ch bin nng sn ng khoai, sn ... T cc ph thi lng thc ny, nh cc amylase c th dng sn xut alcohol. Cng nh cc enzyme ng ho

-amylase v glucoamylase, t cc ph thi lng thc cha tinh bt ca cc dy chuyn quy trnh ch bin thc n c th sn xut mng bao gi c tnh cht phn hu quang hc v sinh hc. -amylase trc tin c dng ph v cc phn t tinh bt mch di to thnh nhng mnh nh. Tip theo glucoamylase tc dng to thnh glucose thng qua qu trnh ng ho (hn 90% tinh bt c chuyn thnh ng). Glucose c ln men thnh axit lactic nh chng vi sinh vt sn sinh axit lactic. Axit lactic cui cng c thu li, tinh sch v dng sn xut mng bao gi kiu ny. Sn phm cui cng cha 95% axit lactic v 5% cc cht thi an ton vi mi trng [19]. nc ta, vic nghin cu s dng cc enzyme vi khun amylase x l nc thi ca cc lng ngh lm bn, bnh a c nhng kt qu ng k. 3.2. Cc enzyme phn hu cellulose Trong thp k qua, enzyme thu phn cellulose ngy cng c quan tm. S quan tm ny l do cc enzyme ny c kh nng thy phn cht thi cha cellulose, chuyn ho cc hp cht kiu lignocellulose v cellulose trong rc thi to nn ngun nng lng thng qua cc sn phm ng, ethanol, kh sinh hc hay cc cc sn phm giu nng lng khc. Th d: t cc cht thi nh my giy nh cc sn phm t bt giy v giy c th thu ngun nng lng nh ethanol [20]. Hin nay vn c s lng ln cc cng trnh xut nhng phng php c th thc hin c trong vic s dng cc enzyme thu phn cellulose c trong cc cht thi hu c ti cc thnh ph ln (MSW) thu cc sn phm ng c th ln men v cui cng l to ra ethanol v butanol.

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Trong cu trc ca cellulose v cellotetraose ch yu l lin kt -(1-4) glucosit. Ni chung, ph hu hon ton cu trc ca polysaccharide ny cn c cc Cellulase vi nhng tc ng c trng ring bit. Sau khi Cellulase (EC 3.2.1.4) (cn gi l endoglucanase D) v -glucosidase (EC 3.2.1.21) (cn gi l cellobiase) ph hu khng chn lc -1,4-glucan thnh cc mnh c khi lng phn t nh oligocellulose, enzyme cellobiosidase (EC 3.2.1.91) cn gi l cellobiohydrolase ph hu tip cc mnh nh ny cho ti n v nh nht l ng n [21]. Nh vy, vic thy phn cellulose, hay ni mt cch ng n hn l thy phn cc polysaccharide ca thc vt, khng phi ch mt hoc hai enzyme l , m cn ti mt h enzyme. Chnh v vy, c nhiu nghin cu cp n vic sn xut cc ch phm bao gm mt s enzyme x l ph thi l cc polysaccharide thc vt. Th d ch phm enzyme t nm Econase c s dng nghin cu hiu qu ca cc enzyme thu phn cellulose i vi vic x l MSW [22]. Ch phm Econase c thnh phn chnh l endo-1,4--Dglucosidase (EC 3.2.1.4), cellobiohydrolase v exo-1,4--D-glucosidase (EC 3.2.1.74) v mt s cc enzyme khc. Vi cc tnh cht nh nu trn, cc enzyme cellulase c nhng ng dng trong lnh vc x l nc thi nh my giy Nguyn liu lm giy l g, sinh khi ca thc vt bc cao. Sinh khi ny cha rt nhiu loi polysaccharide, trong cc polysaccharide quan trng quyt nh n cht lng s lng giy nh cellulose. Ngoi ra, cn c cc polysaccharide khc cng gp phn quan trng nh aminopectin, pectin, xylans, galactomannan, V vy, nc thi ca cc nh my giy, cc c s ch bin g cc xng mc, cc xng sn xut

my tre an u cha cc loi polysaccharide nu trn. Do , ngoi cc enzyme nu trn, vi mc ch x l trit nc thi loi ny, cn c th s dng b sung mt s enzyme khc phn hu cc polysaccharide khc ngoi cellulose. Th d nh: s dng mannobiohydrolase (EC 3.2.1.10) gi l exo-mannanase hoc mannan 1,2-(1,3)-mannosidase (EC 3.2.1.77) v endo-mannanase (EC 3.2.1.78) ph hu mannan [23], galactanase (EC 3.2.1.89) cn gi l arabinogalactanase ph hu arabinogalactan [24]. Cellulases v Hemicellulases ph hu hemicellulose. Hai enzyme cui ny c th sn xut t nhiu chng vi sinh vt, trong c Cellulomonas biazotea [25]. 3.3. Cc enzyme thy phn pectin Pectin l heterosaccharide ca thnh t bo thc vt, c cu to mch di to nn bi cc n v monosaccharide, gm cc lin kt (1,4)--D-galacturonic acid v cc methyl ester: Pectin l thnh phn quan trng tn ti trong rc thi. Khng nh cellulose, Pectin kh phn hu. V vy phi tm c cc chng vi sinh thch hp gii quyt vn ny. Trn c s la chn 100.000 gen khc nhau ca nm (Fungus) Aspergillus japonicus, ngi ta tch c cc enzyme phn gii pectin (pectinolytic enzyme) nh Pectinase, Pectinesterase (Pectinmethylesterase 3.1.1.11). Ngoi Aspergillus japonicus, gn y, nhiu nm khc cng c kho nghim kh nng phn hu tt pectin nh: Euglena gracilis [26], Ceriporiopsis subvermispora [9], Aspergillus fumigatus [27], Sitophilus oryzae [28], Aspergillus niger [29], Clostridium thermosulfurogenes, Clostridium thermosaccharolyticum Sitophilus oryzae [30].

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3.4. Cc enzyme thu phn protein Protease thuc nhm enzyme thy phn protein c s dng rng ri trong cng nghip thc phm, chng hn trong ch bin c v tht. Protease c th thy phn cc protein c trong cht thi, sn xut cc dung dch c hoc cc cht rn kh c gi tr dinh dng cho c hoc vt nui. Protease thy phn cc protein khng tan thng qua nhiu bc, ban u chng c hp th ln cc cht rn, ct cc chui polypeptit to thnh cc lin kt lng trn b mt. Sau , qu trnh ho tan nhng phn rn xy ra vi tc chm hn ph thuc vo s khuch tn enzyme ln b mt c cht v to ra nhng phn nh. Chnh v tnh cht trn m protease c s dng, mt mt tn dng cc ph thi t ngun protein nhng ph thi ny khng cn l cc tc nhn gy nhim mi trng, mt mt x l cc ph thi protein tn ng trong cc dng chy thnh dng dung dch ra tri khng cn mi hi thi [31]. Lng to nn 5% trng lng c th gia cm v c th c coi nh l ngun protein cao trong to nn cu trc keratin cng c ph hu hon ton. Lng c th c ho tan sau khi x l vi NaOH, lm tan bng c hc v bng cc enzyme thu phn, nh protease kim t Bacillus subtilis to thnh sn phm c dng bt, mu xm vi hm lng protein cao c th c s dng lm thc n. Protease ngoi bo c tit ra t Bacillus polymyxa Bacillus megaterium, Pseudomonas marinoglutinosa v Acromonas hydrophila c th c nh trong canxi alginat thc hin cc phn ng lin tc thu c sn lng cao trong cc phn ng thy phn tht c [32]. 3.5. Cc enzyme ph hu hp cht cha halogen Cc enzyme vi sinh vt ph hu hp cht cha halogen, ph hu lin kt carbon-

halogen c th chia lm 2 loi haloalkane dehalogenase and haloacid dehalogenase (HAD) [33]. Rt nhiu enzyme c vai tr trong vic kh chlo nh: 4-chlorobenzoate dehalogenase (EC 3.8.1.6); 4-chlorobenzoyl-CoA dehalogenase (EC 3.8.1.7); atrazine chlorohydrolase (EC 3.8.1.8); 2-haloacid dehalogenase (EC 3.8.1.10); 2-haloacid dehalogenase (EC 3.8.1.11). Mi enzyme ny c cc c th ring. Chng hn, Alkylhalidase EC 3.8.1.1 (halogenase) hoc haloalkane dehalogenase (EC 3.8.1.5) [14], 1-chlorohexane halidohydrolase xc tc phn ng phn hu haloalkane to thnh aldehyde [34]. Atrazine l mt cht c dit c (herbicid) hu nh hon ton khng tan trong nc (33mg/lt), nhng nng cho php trong nc l 0,2 mg/lt. Mt s chng vi sinh nh Pseudomonas sp. strain ADP c kh nng chuyn ho atrazine. Chng ny tit ra Atrazine chlorohydrolase xc tc phn ng chuyn ho atrazine. Nh vy, bng phn ng Atrazine chlorohydrolase, atrazine c, khng tan c th chuyn ho cc sn phm tan c v khng c [35]. 4. Cc lp enzyme khc 4.1. Enzyme tham gia vo qu trnh kh c cc kim loi nng. Kh nhim arsen Kh nhim arsen Cc kim loi nng nh arsenic, ng, cadmi, ch, crom v mt s kim loi khc, u l nhng cht nhim nguy him tm thy trong mt s dng nc thi cng nghip v m khai thc cng nh cc cht thi rn, bn thi ca thnh. Hin nay, vn nhim arsen ang l vn thi s, cn cp bch gii quyt. Trong khun kh ca bi bo, chng ti trnh by quan im s dng

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enzyme vi sinh gp phn vo gii quyt vn ny Trong cuc sng, con ngi tip xc vi arsen qua khng kh, nc ung v thc n. Lng arsen i vo c th hng ngy c 20300g vi khong 25% l arsen v c, phn cn li l arsen hu c. Cc dng arsen hu c trong thc n nh asenobetain, asenocholin tng i khng c, ngc li cc dng arsen v c li rt c, vi liu lng gy cht ngi l 100-200 mg oxyt arsen. Trn th gii, ngun nc ngm c cha arsen trn 50g/L c pht hin nhiu nc nh Achentina, Mehic, Myanma, Vit Nam, v.v... Vit Nam, theo kt qu nghin cu ca nhiu tc gi cho thy, hm lng arsen trong cc ging khoan c nng ti 50g/L, thm ch c ni cao hn 150g/L. Nh vy vn nhim arsen trong nc ging khoan dng cho sinh hot ti nng thn v ngay c mt s ni trong thnh ph ca Vit Nam l mt thc trng ng lo ngi nh hng ti sc kho con ngi. Vic x l nhim c arsen bng phng php ho hc rt kh khn. Phng php enzyme c th khc phc c nhng kh khn. Nguyn tc chung ca phng php enzyme l chuyn ho Arsenite (ho tr III) rt c thnh Arsenat (ho tr V) t c hn, hoc chuyn ho Arsen dng v c sang dng hu c. Arsen trong dng hu c t c hn trong dng v c. Chng hn, enzyme Arsenate reductase (cn gi l arsenite oxidase) (EC 1.20.98.1) t chng Alcaligenes faecalis, xc tc cho phn ng chuyn ho Arsenite (ho tr III) rt c thnh Arsenate (ho tr V) t c hn [36], hoc arsenate reductase (donor) (EC 1.20.99.1) (cn gi l glutaredoxin), t chng Chrysiogenes arsenatis xc tc phn ng chuyn ho Arsenite [37]. Cht cho electron phn ng

ny c th l benzylviologen hoc mt s cht khc hoc cng c th chuyn ho arsenite dng v c sang dng hu c (methylarsonate) nh Arsenite methyltransferase (EC 2.1.1.137) xc tc phn ng [38] chuyn ho cc arsenite thnh methylarsonate t c hn nh S-adenosyl-L-methionine. 4.2. Enzyme tham gia vo x l cc cht c hot tnh b mt Cc tc nhn c hot tnh b mt hay hot ng b mt l cc cht hu c, l cc phn t c tnh phn cc mnh v l thnh phn c bn ca cht ty. Cc cht c hot tnh b mt c th gy ra s nhim nghim trng khi nng cao v d nh t cc nh my x phng, h thng thot nc thnh ph v c th pht sinh cc hin tng khng mong mun nh vic to bt [37]. Alkylsulfatase t Pseudomonas C12B Pseudomonas putida hoc t Pseudomonas aeruginosa [38] c th lm gim hiu sut cc cht c hot tnh b mt xung ti nng 750 mg dm-3.. Enzyme ny c hiu vi cc gc alkyl sulfate, v c th ph hu hon ton gc alkyl sulfate, alkyl ethoxy sulfate hoc aryl sulfonate trong cc cht c hot tnh b mt. Tuy nhin, trn thc t, enzyme ny khng th tn cng cc alkane sulfonate. Ni chung, alkylsulfatase ha hn mt ng dng trong tng lai v vic x l mt phm vi rng cc cht c hot tnh b mt c trong nc thi. 4.3. Enzyme x l cht thi xyanua, Cyanide hydratase Ngi ta c tnh rng mi nm c khong 3 triu tn xyanua c s dng trn ton th gii vo cc mc ch cng nghip khc nhau nh cc sn phm ho hc trung

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gian, tng hp t si, cao su v dc liu cng nh cc m qung v m kim [39]. Ngoi ra, nhiu loi thc vt, vi sinh vt v cn trng cng c kh nng thi ra HCN cng vi cc enzyme thy phn. Cui cng, thc phm hu ht u cha mt hm lng ng k xyanua bt ngun t cyanogenic glycoside c ngun gc t mt vi loi thc phm. Khi c mt xyanua s c ch qu trnh trao i cht, c th gy cht ngi v cc sinh vt khc, cn phi loi b chng trc khi thi ra mi trng. Cyanide hydratase (EC 4.2.1.66), hoc formamide hydro-lyase l mt enzyme c kh nng chuyn ho cyanide [39] trong nc thi cng nghip thnh amoniac v formate thng qua mt bc phn ng [40]. Cyanide hydratase c phn lp t mt vi loi nm v c to ra t nm khi nng xyanua thp. Khi c c nh, tnh bn ca Cyanide hydratase tng ln nhiu v enzyme t Gloeocercospora sprrghi bn vng hn t Stemphylium loti [41]. Cyanide hydratase t nm thch hp x l cc cht thi cng nghip cha xyanua. Mt s vi khun Gram-(-) nh Alcaligenes denitrificans cng tit ra cyanidase c i lc bn cao v c kh nng loi xyanua nng rt thp, v d nh < 0.02 mg dm-3 CN. Sau ny, khi cng ngh sinh hc pht trin, ngi ta tch c gen cyanidase t Pseudomonas stutzeri AK61 [39] Pseudomonas pseudoalcaligenes [42]. Hot tnh ca cyanidase khng b nh hng bi cc ion thng thng c mt trong nc thi (v d nh Fe2+, Zn2+ v Ni2+), hay bi cc cht hu c nh acatat, formamide, acetamide v acetonitrile. pH ti u trong khong 7.8-8.3 v mt hot tnh hon ton, khng phc hi khi pH cao hn 8.3 [40]. Tm li, vic s dng enzyme trong x l ph thi c mt tng lai y ha hn. y

l mt trong nhng hng nghin cu ng dng s dng c hiu qu enzyme trong cng ngh x l ph thi sinh hot nc ta hin nay. Cng trnh c hon thnh di s h tr kinh ph ca Chng trnh Nghin cu c bn trong Khoa hc T nhin. Ti liu tham kho
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[10] P.O. Magalhaes, A. Ferraz, A.F. Milagres, Enzymatic properties of two beta-glucosidases from Ceriporiopsis subvermispora produced in biopulping conditions, J Appl Microbiol. 101 (2006) 480. [11] H.S. Bleeg, F. Christensen, Biosynthesis of ascorbate in yeast, Purification of L-galactono1,4-lactone oxidase with properties different from mammalian L-gulonolactone oxidase, Eur. J. Biochem. 127 (1982) 391. [12] M. Golicnik, J. Stojan. Slow-binding Inhibition., A Theoretical and Practical Course for Students: Tyrosinase (EC 1.14.18.1) properties, Biochemistry and Molecular Biology Education 32 (2004) 228. [13] J. D. Crowe, S. Olsson, Induction of Laccase Activity in Rhizoctonia solani by Antagonistic Pseudomonas fluorescens Strains and a Range of Chemical Treatments, Applied and Environmental Microbiology 67 (2001) 2088. [14] M.R. Mokela , K.S. Hildon, T. K. Hakala, A. Hatakka, T. K. Lundell, Expression and molecular properties of a new laccase of the white rot fungus Phlebia radiata grown on wood, Current Genetics 50 (2006) 323. [15] Elias Abadulla; Tzanko Tzanov; Silgia Costa; Karl-Heinz Robra; Artur Cavaco-Paulo; Georg M. Gua Bitz., Decolorization and Detoxification of Textile Dyes with a Laccase from Trametes hirsuta, Applied and Environmental Microbiology 66 (2000) 3357. [16] DAnnibale, A.S. Rita Stazi, V. Vinciguerra, G. Giovannozzi, Oxirane-immobilized Lentinula edodes laccase: stability and phenolics removal efficiency in olive mill wastewater, J. Biotechnol. 77 (2000) 265. [17] H. Iefuji, M. Chino, M. Kato, Y Iimura, Rawstarch-digesting and thermostable alphaamylase from the yeast Cryptococcus sp. S-2: purification, characterization, cloning and sequencing, Biochem J. 318, Pt 3 (1996) 989. [18] P. Tomasik, C. H. Schilling. Chemical modification of starch Advances in Carbohydrate Chemistry and Biochemistry 59 (2004) 175. [19] J.H. Auh, H. Y. Chae, Y.R. Kim, K.H. Shim, S.H. Yoo, K.H. Park, Modification of Rice Starch by Selective Degradation of Amylose Using Alkalophilic Bacillus Cyclomaltodextrinase, J. Agric. Food Chem., 54 (6) (2006) 2314 . [20] M.A. Elberson, F. Malekzadeh, M.T. Yazdi, N. Kameranpour, M.R. Noori-Daloii, M.H. Matte, M. Shahamat, R.R. Colwell, K.R. Sowers, Cellulomonas persica sp. nov. and

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The future of Enzyme application in waste treatment

Tran Dinh Toai1, Tran Thi Hong2
1

Institute of Chemistry, Vietnamese Academy of Science and Technology, 18 Hoang Quoc Viet, Hanoi, Vietnam 2 College of Science, VNU, 334 Nguyen Trai, Hanoi, Vietnam

The implementation of increasingly stringent standards for the discharge of wastes into the environment has necessitated the need for the development of alternative waste treatment. Nowadays, it is well known a number of enzymes derived from a variety of different plants and microorganisms has been reported to above 3000 ones more. Among these, many of them lay an important role in an array of waste treatment applications. Enzymes, especially Hydrolases, and Oxidoreductases can act on specific recalcitrant pollutants to remove them by precipitation or transformation to other products. They also can change the characteristics of a given waster to render it more amenable treatment or aid in converting waste material to value-added products. Enzymes seem to have a promising future. There is a presentation of some enzymes have successful application in waste treatment. However, further research need determine which enzyme is best corresponding to reality and to optimize the enzymatic process as a whole.

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