Full-text resources of PSJD and other databases are now available in the new Library of Science.
Visit https://bibliotekanauki.pl
Preferences help
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

help Sort By:

help Limit search:
first rewind previous Page / 1 next fast forward last
EN
Lipases, esterases, acylases, glycosidases, aldolases are the most used enzymes in synthetic organic chemistry. Among the biocatalysts, lipases are the most frequently used. This class of enzymes is able to catalyze the hydrolysis of carboxylic acid esters in aqueous medium on the reverse reaction in organic solvents. The use of enzymes in organic solvents is now well established and there are several advantages of conducting enzymatic reaction in water poor media such as increased solubility of hydrophobic substrates, shifting of thermodynamic equilibrium in favour of synthesis over hydrolysis and increased thermostability of the enzyme. However, the practical application of enzyme in organic solvents has been hampered by the low catalytic activities compared to those expressed in water. This review highlights recent research on the stabilization of enzymes using both chemical and biological means to increase the lifetime o the biocatalyst.
EN
Four inorganic supports (sand, silica gel, crushed pumice and controlled-pore glass) were used for immobilization of invertase. The possibility of application of thus obtained immobilized enzyme in continuous production of inverted sugar was tested. The best support for immobilization of invertase was controlled-pore glass (CPG, average pore size of 31 mm). The conditions of production of inverted sugar by immobilized enzyme were optimised (also in column). Unter the optimised the column (dimensions: 0.7x27 cm) with immobilized invertase was able to degrade sucrose to glucose and fructose in an amount of 60 g/h. Immobilized invertase in the column remained fully active for 120 days.
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.