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Kvasny Prum. 2003; 49(7-8): 182-185 | DOI: 10.18832/kp2003012
We were veryfying α-acetolactate degradation efficiency as a diacetyl percursor with α-acetolactate decarboxylase, which was immobilized in various ways into calcium alginate, because of its possible reuse in the subsequent fermentations. During the first fermentation the way of enzyme agent's immobilization didn't influence its stability, diacetyl concentration in hopped wort was null. During the same immobilizate reuse the concentration of diacetyl was moving in the range from 0 to 0,11 mg/l in the second cycle and in the range from 0,04 to 0,16 mg/l in the third cycle depending on the way of enzyme agent`s immobilization. Enzyme was the most stable when it was absorbed on the DEAE cellulose surface and then closed together with ferments into the alginate gel, which reduced its washing up out off the carrier.We were veryfying α-acetolactate degradation efficiency as a diacetyl percursor with α-acetolactate decarboxylase, which was immobilized in various ways into calcium alginate, because of its possible reuse in the subsequent fermentations. During the first fermentation the way of enzyme agent's immobilization didn't influence its stability, diacetyl concentration in hopped wort was null. During the same immobilizate reuse the concentration of diacetyl was moving in the range from 0 to 0,11 mg/l in the second cycle and in the range from 0,04 to 0,16 mg/l in the third cycle depending on the way of enzyme agent`s immobilization. Enzyme was the most stable when it was absorbed on the DEAE cellulose surface and then closed together with ferments into the alginate gel, which reduced its washing up out off the carrier.
Published: July 1, 2003