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ZIJLSTRA,G.M.,DE GOOIJER,C.D.,TRAMPER,H.: Extractive bioconversions in aqueous
TÉZISEK
I. A fruktooligoszacharidok szintézisére alkalmazandó, fruktozil-transzferáz aktivitással rendelkezı kereskedelmi Pectinex Ultra SP-L enzimkészítményt rögzítettem abból a célból, hogy megnöveljem a biokatalizátor stabilitását. Az Amberlite IRA 900 Cl típusú anioncserélı gyantát alkalmasnak találtam hordozónak. A szilárd fázisú biokatalizátor elıállítására egy újszerő, kétlépéses rögzítési technikát dolgoztam ki. Elsı lépésben az enzimoldatot az aktivált gyantán adszorbeáltattam, így ionos jellegő kötések alakultak ki a gyanta és a fehérjemolekulák között. Második lépésben a gyantán megkötıdött enzimmolekulák között – stabilizálás céljából – keresztkötéseket alakítottam ki glutáraldehid segítségével. A kötıreagens nemcsak a fruktozil-transzferáz molekulákat vitte keresztkötésbe, hanem a Pectinex Ultra SP-L készítmény fı tömegét kitevı egyéb fehérjéket is. Így egy stabilizáló „fehérjeháló” alakult ki a biokatalizátorszemcsék külsı és belsı felületén. Az általam kidolgozott újszerő enzimrögzítési módszer tehát úgy tekinthetı, mint ionos és kovalens kötések konszekutív létrehozásán, továbbá segédfehérjék stabilizáló hatásán alapuló módszer. Fruktozil-transzferáz immobilizálására a módszert más szerzık biztosan nem alkalmazták, de alapos szakirodalmi vizsgálódásaim szerint más enzimre sem található ilyen módszer. (2.
publikáció)
II. Meghatároztam a fenti rögzítési módszer optimális körülményeit. Ennek során 16,7 g g
-1 biokatalizátor/hordozó arányt, 0,25 % kovalens rögzítıágens koncentrációt és 15 min keresztkötési idıt állapítottam meg, mint optimumokat. A kialakított immobilizált enzimkészítmény mőködési paramétereinek vizsgálata során pH=5,6 és 53°C értékeket kaptam optimumként. Az ezen körülmények között létrehozott és alkalmazott biokatalizátor felezési ideje ~ 40 nap, tehát mőködési stabilitása gyakorlati szempontból megfelelı. A megállapított optimális mőködési paraméterek mellett az új típusú szilárd fázisú biokatalizátor alkalmazásával, rázatott lombikos kísérletekben vizsgáltam a fruktooligoszacharidok elıállításának lehetıségét. A kísérletek során az optimális körülmények között 64,4 %-os termék-hozamot sikerült elérnem, amely megfelel a szakirodalomban talált adatoknak. (2. publikáció)
III. A fruktooligoszacharid szintézis reakció melléktermékeként keletkezı glükóz eliminálására glükóz-oxidáz – kataláz koimmobilizált enzimkészítményt állítottam elı.
Az alkalmazott hordozó és a kombinált rögzítési módszer analóg a fentiekben bemutatott módszerrel, de mivel azt a jelen esetben glükóz-oxidáz – kataláz rendszer szimultán koimmobilizálására alkalmaztam – a vonatkozó szakirodalom adatainak vizsgálata alapján – újnak minısül. Megállapítottam, hogy a koimmobilizált enzimek aktivitásai jó közelítéssel azonosak azokkal az aktivitásértékekkel, amelyeket akkor kaptam, amikor a két enzimet külön-külön rögzítettem. Meghatároztam a preparátum optimális rögzítési paramétereit (0,5 % glutáraldehid koncentráció és 60 min rögzítési idı), valamint a készítmény alkalmazási optimumait (pH=5,1 és 30°C hımérséklet). (1.
és 3. publikáció)
IV. A kialakított rögzített biokatalizátorok felhasználásával egy, az együttes termék-elıállításra és melléktermék-eltávolításra alkalmas, eredeti konfigurációjú, laboratóriumi mérető, két, oszlopból álló, integrált reaktorrendszert állítottam össze és vizsgáltam a kesztóz, nisztóz és fruktozil-nisztóz fruktooligoszacharidok elıállításának lehetıségét. A két oszlopreaktor közül a szintézisreaktor állóágyas, a glükóz-oxidációs reaktor kevert ágyas üzemben mőködött. A mőködési ciklusuk úgy volt beállítva, hogy a ciklus alatt azonos mennyiségő glükóz keletkezett a szintézis reaktorban, mint amennyi eliminálódott a glükóz-oxidációs reaktorban. Ezután a kapcsolt csı- és szeleprendszer és szivattyúk felhasználásával megcseréltem a két reaktor mőködési módját, majd egy újabb ciklust indítottam el. A ciklikus mőködéső kétreaktoros reaktorblokk az idıben integrált folyamatok megvalósítására alkalmas reaktorok új típusa.
A reaktorblokkban több ciklusból álló kísérletsorozatban 74,44 %-os termékhozamot sikerült elérnem, amely lényegesen nagyobb, mint a melléktermék eltávolítása nélkül kapott érték. (1. és 5. publikáció)
THESES
I. I immobilized a commercial grade enzyme product, Pectinex Ultra SP-L having fructosyl-transferase activity to enhance the stability of the biocatalyst. I found applicable the Amberlite IRA 900 Cl type anionic ion exchange resin as immobilization matrix. I established a new two step immobilization method for this biocatalyst: In first step the enzyme solution was adsorbed onto the activated resin particles and ionic bounds were formed. The second step was a covalent bound formation with glutaraldehyde between the protein molecules and enhanced the stability of the solid phase biocatalyst. (2. publication)
II. I determined the optimal immobilization parameters. They were as follows: 16.7 g g-1 biocatalyst/matrix ratio, 0.25 % covalent binding agent concentration and 15 min cross-linking time. I determined the optimal operational parameters of the developed biocatalyst, they were pH=5.6 and 53°C temperature. I studied the stability of the established solid phase biocatalyst and I appointed 40 day half-time period, which value is appropriate from the practical point of view. I studied the production of
II. I determined the optimal immobilization parameters. They were as follows: 16.7 g g-1 biocatalyst/matrix ratio, 0.25 % covalent binding agent concentration and 15 min cross-linking time. I determined the optimal operational parameters of the developed biocatalyst, they were pH=5.6 and 53°C temperature. I studied the stability of the established solid phase biocatalyst and I appointed 40 day half-time period, which value is appropriate from the practical point of view. I studied the production of