Pregled bibliografske jedinice broj: 534707
Extraction and purification of alcohol dehydrogenase from yeast cells
Extraction and purification of alcohol dehydrogenase from yeast cells // 2nd Conference on Applied biocatalysis and 7th Meeting of Students and University Professors from maribor and Zagreb / Habulin, M. ; Primožič, M. (ur.).
Maribor: Tiskarna tehniških fakultet Maribor, 2011. (predavanje, međunarodna recenzija, sažetak, znanstveni)
CROSBI ID: 534707 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Extraction and purification of alcohol dehydrogenase from yeast cells
Autori
Valinger, Davor ; Sudar, Martina ; Findrik Blažević, Zvjezdana ; Vasić-Rački, Đurđa
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, M. ; Primožič, M. - Maribor : Tiskarna tehniških fakultet Maribor, 2011
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
alcohol dehydrogenase; ultrasound; cell disruption; baker's yeast; gel filtration
Sažetak
Alcohol dehydrogenase (E.C. No. 1.1.1.1) is an enzyme that occurs in large amounts in the microorganisms and liver of the animals. It plays an important role in several physiological functions including metabolism of alcohol. Generally, a good source for this enzyme is Baker’s yeast (Saccharomyces cerevisiae) [1]. In this work alcohol dehydrogenase (ADH) was isolated from Baker's yeast and then purified. Considering that ADH is an intracellular enzyme, it was necessary to break yeast cells and carry out a series of separation procedures. Yeast cells were broken using a combination of ultrasound and glass beads, which showed to be very efficient. After the disruption of cells, glass beads and cell residues were separated by centrifugation at 4 500 and 14 000 rpm. Amonium sulphate was added to the supernatant containing ADH in order to precipitate the enzyme. ADH is precipitated between 40 and 70% of amonium sulphate saturation. After the precipitation, which is caried out to separate undesirable enzymes which can be present in the solution, the sample was purified using several gel filtration columns, Sephadex G-50 and Sephadex G-100.
Izvorni jezik
Engleski
Znanstvena područja
Biotehnologija
POVEZANOST RADA
Projekti:
125-1252086-2793 - Biokatalizatori i biotransformacije (Vasić-Rački, Đurđa, MZOS ) ( CroRIS)
Ustanove:
Fakultet kemijskog inženjerstva i tehnologije, Zagreb
Profili:
Martina Sudar
(autor)
Zvjezdana Findrik Blažević
(autor)
Davor Valinger
(autor)
Đurđa Vasić-Rački
(autor)