Pregled bibliografske jedinice broj: 535286
Immobilization of alcohol dehydrogenase enzyme within microchannels of different origins
Immobilization of alcohol dehydrogenase enzyme within microchannels of different origins // 2nd Conference on Applied Biocatalysis and 7th Meeting of Students and University Professors from Maribor and Zagreb / Habulin, Maja ; Primožič, Mateja (ur.).
Maribor: Tiskarna tehniških fakultet Maribor, 2011. str. 63-64 (predavanje, međunarodna recenzija, sažetak, znanstveni)
CROSBI ID: 535286 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Immobilization of alcohol dehydrogenase enzyme within microchannels of different origins
Autori
Pindrić, Katarina ; Šalić, Anita ; Zelić, Bruno
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
2nd Conference on Applied Biocatalysis and 7th Meeting of Students and University Professors from Maribor and Zagreb
/ Habulin, Maja ; Primožič, Mateja - Maribor : Tiskarna tehniških fakultet Maribor, 2011, 63-64
ISBN
978-961-248-298-5
Skup
2nd Conference on Applied Biocatalysis and 7th Meeting of Students and University Professors from Maribor and Zagreb
Mjesto i datum
Maribor, Slovenija, 07.11.2011. - 08.11.2011
Vrsta sudjelovanja
Predavanje
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
microchannel; immobilisation; alcohol dehydrogenase; hexanol
Sažetak
Microreactors are very useful tools for bioprocess development. They are produced in many different forms, from small laboratory devices consisted of one or numerous microchannels, to microplants. In recent years, a successful application of enzymatic microreactors has been reported, mainly in biotransformation processes and kinetic studies. Now, possibilities to incorporate microreactor technology in chemical and biochemical processes are being explored. In this study, possibility to use immobilized enzyme alcohol dehydrogenase within microchannel of different materials (glass microchannel with inner diameter of 50 µm, and polytetrafluoroethylene (PTFE) with inner diameter 1000 µm) was explored. Immobilization was performed by covalent immobilisation using 3- aminopropyltriethoxysilane (APTES) and glutaraldehyde solutions to get covalent bonding for immobilization and H2SO4 solution to promote silanization. Using immobilized enzyme, enzymatic biotransformation of hexanol to hexanal was performed. Together with oxidation process, immobilized enzyme stability was studied by measuring protein concentration in the outflow. Data obtained from the experiments, were compared with results from batch experiments and microreactor experiments performed with free biocatalysts. In comparison to macro experiments, enzymatic oxidation of hexanol performed with free and immobilized enzyme was highly efficient when it was carried out in the microchannel.
Izvorni jezik
Engleski
Znanstvena područja
Biotehnologija
Napomena
Ovaj rad financijski je potpomognula Nacionalna zaklada za znanost, visoko školstvo i tehnologijski razvoj Republike Hrvatske.
POVEZANOST RADA
Ustanove:
Fakultet kemijskog inženjerstva i tehnologije, Zagreb