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1

Immobilization of recombinant beta-galactosidase in reactions catalysed by transglutaminase

100%
Wolosowska S., Synowiecki J.
|
EN
Thermostable beta-galactosidase from Escherichia coli transformant containing the enzyme gene from Pyrococcus woesei was immobilized at pH 5.5 on silica gel by crosslinking with transglutaminase. The obtained preparations had a specific activity of 11.573 U/g of support at 70C using oNPG as a substrate. The optimum pH and temperature for immobilized beta-galactosidase activity were 5.5 and 95C. The immobilized enzyme is stable at the temperatures close to the optimal value and the residual activity for oNPG hydrolysis of the preparations incubated 1 h in 0.1 M phosphate citrate buffer (pH 5.5) at 100C was about 70% of the initial value.
2

Production and selected applications of immobilized enzymes

100%
Synowiecki J., Wolosowska S.
Biotechnologia
|
2007
|
issue 2
7-26
EN
The presented data explain why application of immobilized enzyme systems is advantageous in many modern industrial technologies. Also, this reviev article contains information concerning the main methods developed for enzyme immobilization, as well as characteristic, suitability and properties of different carriers used for these purposes. Furthermore, the influence of immobilization process on changes of enzyme activity, selectivity, stability, conditions of catalysed reaction and other properties important in practical applications are described. Emphasis is placed on the choice of immobilized enzyme system adequate for the designed technology.
3

The supports for enzymes immobilization and their applications

75%
Lobarzewski J., Ginalska G.
Biotechnologia
|
1994
|
issue 1
44-63
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