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  1. 3 Biotechnologia

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  1. 2 2009

  2. 1 2008

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  1. 3 Sinkiewicz I.

  2. 3 Synowiecki J.

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1

Characterization of bacteria of the genus Thermus and their biotechnological importance

100%
Sinkiewicz I., Synowiecki J.
Biotechnologia
|
2009
|
issue 3
148-162
EN
Gram-negative, aerobic bacteria of the genus Thermus which have been isolated from many natural and artificial, thermal environments are used as a source of thermostable restriction nucleases and DNA polymerase, as well as can be exploited for the production of many other enzymes with a great industrial importance. The strains belonging to the genus Thermus utilize carbohydrates, amino acids, carboxylic acids and peptides and their optimal growth temperatures ranged from 55 to 85oC. This review is focused on the adaptation of Thermus strains to thermostability and on characterisation and possible application of their enzymes.
2

Suitability of Thermus ruber as a source of trehalose synthase

100%
Sinkiewicz I., Synowiecki J.
Biotechnologia
|
2008
|
issue 1
168-176
EN
Thermus ruber is a producer of trehalose synthase, which catalyses the conversion of maltose into trehalose by intramolecular transglucosylation. The specific activity of cell-free extract of Thermus ruber cultivated on a media without saccharides was 0.016-0.028 U/mg protein and it increased up to 0.086 U/mg in presence of 0.5% maltose in the culture broth. The maximum degree of maltose conversion of about 90% was achieved at 10% substrate concentration. The trehalose synthase does not catalyse formation of trehalose from maltotetraose, maltohexaose and other oligosaccharides. The optimal temperature for enzyme activity was 65C. A maximum activity of the maltose transglucosylation was performed at pH 6.5. The highest yield of trehalose synthase was attained during cultivation of bacteria at 55C for 48 h on media composed of 0.5% peptone, 0.1% yeast extract and 0.5% maltose or starch.
3

Evaluation of Thermus ruber as a source of thermostable (-glucosidase useful for production of glucose syrups

100%
Sinkiewicz I., Synowiecki J.
Biotechnologia
|
2009
|
issue 2
134-146
EN
Thermus ruber produces (-glucosidase detected in the crude extract of cell proteins. This enzyme exhibits optimum actiivity at 65(C and pH 6,0. The enzyme was stable within a range of pH 5.5 to 8.0 and in 65(C for 60 min. The rate of p-nitrophenol-(-D-glucopyranoside cleavage was higher than that for maltose. With maltotetraose, maltopentaose and maltohexaose, the hydrolysis rate decreased with increasing the molecular weight of the substrate. Our data suggest that the starch converting process could be improved using (-glucosidase from Thermus ruber.
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