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: 4

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

Search results

Search:
in the keywords:  THERMOPHILE
help Sort By:

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

Suitability and properties of beta-galactosidases from different sources

100%
Synowiecki J., Maciunska J.
Biotechnologia
|
2000
|
issue 1
117-123
EN
The article reviews the progress of investigations of b-galactosidases from microbial sources. These enzymes show great differences in optimal conditions of lactose hydrolysis and their utilisation create new possibilities to improve milk and milk by-products processing. Some beta-galactosidases from extreme thermophiles have significant activity above 100?C. Possible applications and interrelationship of both molecular structure and thermostability of these enzymes are also discussed.
2

Thermophiles as a source of alpha-glucosidases suitable for production of glucose syrups

100%
Synowiecki J., Zdzieblo A.
Biotechnologia
|
2002
|
issue 2
165-174
EN
Alpha-glucosidases release terminal, 1,4- and to lesser extend, 1,6- linked -glucose residues of disaccharides, oligosaccharides, and aryl-glucosides. Among these, novel thermostable enzymes from hyperthermophiles and moderate termophiles have been investigated. The aim of this article is to demonstrate different sources of thermostable alpha-glucosidases, as well as properties and suitability of these enzymes for production of glucose at 90-100C, e.g., during one step process initiated by starch liquefaction using commercial alpha-amylase (Termamyl).
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.
4

Characterization of bacteria of the genus Thermus and their biotechnological importance

88%
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.
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.