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Abstracts
The gene encoding thermostable beta-galactosidase from Pyrococcus woesei was cloned and expressed in Escherichia coli cells. Furthermore, the obtained recombinant strain was used without additional cell permeabilization as a catalyst for the synthesis of galactosylfructose. The optimum pH and temperature for galactosylfructose production by recombinant cells were 5,4 and 80C, respectively. The highest process productivity (7,6 g/lh) was attained at the cells' concentration of 40 mg/ml of the reaction media, using a substrate containing 10% of lactose and 20% fructose. The transgalactosylation activity during the repeated bath processes was almost unchanged after sixfold application of the cells.
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152-162
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author
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ARTICLE
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Jozef Synowiecki, Katedra Chemii, Technologii i Biotechnologii Zywnosci, Wydzial Chemiczny, Politechnika Gdanska, ul. G. Narutowicza 11/12, 80-952 Gdansk, Poland
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YADDA identifier
bwmeta1.element.element-from-psjc-3118da1e-f3f9-34a9-b973-be395c9686e7