[Role of intramolecular bonds in stability of certain enzymes of the cellulolytic complex].
Stability of C1- and C2-cellulases, CX-exo- and CX-endoglucanases and beta-glucosidase of Aspergillus awamori was studied as affected by monoatomic aliphatic alcohols --methanol, ethanol, propanol and isopropanol; bi- and triatomic alcohols - ethylene glycol and glycerol, urea as well as detergents of dodecyl sulphate and sodium nonilate. The mentioned enzymes are established to manifest the highest activity in 40-60% glycerol. It is also shown that their stability is changed differently under the effect of other alcohols, urea and detergents. The latter testifies to the fact that the studied enzymes are nonidentical, in particular, they differ between themselves by a ratio of intramolecular forces which stabilize their macrostructure.
D000438:Alcohols / Q000494:pharmacology; D001230:Aspergillus / Q000201:enzymology*; D002480:Cellulase / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D004355:Drug Stability; D005959:Glucosidases / Q000378:metabolism*; D006026:Glycoside Hydrolases / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D000438:Alcohols; D005959:Glucosidases; D006026:Glycoside Hydrolases; D002480:Cellulase
Rol' vnutrishn' omolekuliarnikh zv'iazkiv u stabil'nosti okremikh fermentiv tseliulolitichnoho kompleksu