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1

Beta-galactosidase activity of proteins extracted from Sulfolobus shibatae

100%
Wolosowska S., Synowiecki J.
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issue 2
268-279
EN
The cytoplasmic -beta galactosidase/beta-glucosidase from hyperthermophilic archaeon Sulfolobus shibatae has been characterized with regard to its use in lactose hydrolysis. Cell extract was purified 16-fold to a specific activity 29.5 U/mg using ammonium sulfate precipitation, ion-exchange chromatography, and gel filtration. Isolated enzyme exhibited optimum activity at pH 5.5 and 98C and had a half-life of 7 h in acetate buffer (pH 5.5) at 90C. Cu2+, Hg2+ and Zn2+ strongly inhibited the enzyme, whereas catalytic properties of other investigated cations were barely influenced. Glucose and galactose were predominantly produced from lactose. However, at the substrate concentration of 0.15, M small amount of lactose was converted into transgalactosylation products.
2

Suitability of thermostable enzymes for improvment of starch processing

100%
Synowiecki J., Grzybowska B.
Biotechnologia
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2001
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issue 2
26-35
EN
Commercial processing of starch to mono-and oligosaccharides depends on the availability and properties of the applied enzymes such as -amylase, glucoamylase, -glucosidase and xylose isomerase. Each of these enzymes has a different pH and temperature optimum for use. Therefore starch processing is carried out in the stages of liquefaction, saccharification, and isomerisation. This article discusses the application of thermostable enzymes leading to higher quality products and lower production costs caused by the simplification of the processing.
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