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Immobilization of Yeast Alcohol Dehydrogenase on Weakly Basic Anion Exchange Resin Beads

Đurđa Vasić-Rački ; Faculty of Technology, The University of Zagreb, Zagreb, Croatia, Yugoslavia


Puni tekst: engleski pdf 5.867 Kb

str. 305-311

preuzimanja: 138

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Sažetak

Yeast alcohol dehydrogenase was immobilized on weakly
basic macroporous anion exchange resin beads Lewatit MP-64.
After the adsorption the enzyme was crosslinked by glutaraldehyde:
The activity of the immobilized enzyme was investigated
in the pH 8.9 recirculation reactor system at 303 K. It was found
that the immobilized enzyme was destabilized upon addition of
semicarbazide hydrochloride to the buffer solution.
A greater amount of protein was attached to the support when
ethanol was present in the enzyme solution, but the activity of
the bound enzyme was lower than in the absence of ethanol.

Ključne riječi

Hrčak ID:

194167

URI

https://hrcak.srce.hr/194167

Posjeta: 280 *