Full-text resources of PSJD and other databases are now available in the new Library of Science.
Visit https://bibliotekanauki.pl
Preferences help
Polish version English version Language
enabled [disable] Abstract
Number of results

Results found: 3

Number of results on page
first rewind previous Page / 1 next fast forward last

Search results

Search:
in the keywords:  THERMOSTABILITY
help Sort By:

help Limit search:
first rewind previous Page / 1 next fast forward last
1

Thermostability conditions and catalytic characterization of isocitrate dehydrogenase from Bacillus licheniformis

100%
Zabielski P.
Biotechnologia
|
2001
|
issue 3
219-230
EN
The NADP+ - dependent isocitrate dehydrogenase (IDH) from Bacillus licheniformis was partially purified using ammonium sulphate fractionation and gel filtration on Sephadex G-200 column. The enzyme preparation had specific activity of 1.52 U mg-1. The temperature optimum for the IDH activity was about 59C. The Arrthenius activation energy was determined to be 65.3 kJ/mol below 47C, and 18.3 kJ/mol above this temperature. The IDH activity at 65C was much protected by isocitrate and magnesium, but no NADP+. Manganese ions were more efficient activators of the enzyme than Mg2+. Calcium ions rather inhibited the IDH. The Km values for DL-isocitrate and NADP+ in phosphate buffer (pH 7.4) at 20C were 85.5 and 4.9 muM, respectively; at 58C the corresponding values were 181.5 and 69.3 muM.
2

Improvement of beta-galactosidase properties and conditions for its microbial biosynthesis

88%
Bednarski W., Kowalewska-Piontas J.
Biotechnologia
|
2000
|
issue 2
131-141
EN
We present examples of genetic modification of microorganisms capable of beta-galactosidase synthesis. The technological characteristics as termostability, high activity in a low temperature is improved. We also describe intensification of beta-galactosidase secretion to the medium.
3

Preparation, properties and suitability of thermostable enzymes

88%
Synowiecki J.
Biotechnologia
|
1998
|
issue 3
98-105
EN
Some enzymes from extreme thermophiles and hiperthermophiles have half-lives up to 13h at ,temperatures above 100?C. They are suitable for starch and whey processing, oil mining, PCR techni and oligosaccharides synthesis. The differences in structure and function between these very stable and the prevailing less stable enzyme forms are relatively small and are comparable with those differences found among enzymes of similar stability. The relationship of both conformational stability and enzymatic activity with protein flexibility suggests that stability at temperatures far above those which are optimum for the growth of microorganism is rather unlikely.
first rewind previous Page / 1 next fast forward last
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.