NAD+-dependent hydrogenase from the hydrogen oxidizing bacterium Alcaligenes eutrophus Z1. Stabilization against temperature and urea induced inactivation.
Chemical modification of the NAD+-dependent hydrogenase from the hydrogen oxidizing bacterium Alcaligenes eutrophus Z1 results in considerable enzyme stabilization towards urea and temperature induced inactivation. The stabilizing effect was shown to originate from the suppression of hydrogenase tetramer dissociation. The magnitudes of the stabilizing effects (5-fold and more) were in agreement with the values predicted on the basis of the enzyme thermoinactivation mechanism postulated earlier. Hydrophobic interactions are considered to be critical for the stability of the enzyme quaternary structure. Various methods of hydrogenase immobilization were tested. The enzyme was immobilized with a high retention of activity on aminated silochrom via its carboxylic groups.
D000171:Acrolein / Q000031:analogs & derivatives / Q000494:pharmacology; D000421:Alcaligenes / Q000201:enzymology*; D055598:Chemical Phenomena; D002621:Chemistry; D003432:Cross-Linking Reagents / Q000494:pharmacology; D003959:Diamines / Q000494:pharmacology; D004355:Drug Stability; D004800:Enzymes, Immobilized; D005976:Glutaral / Q000494:pharmacology; D006358:Hot Temperature; D006864:Hydrogenase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D007096:Imidoesters / Q000494:pharmacology; D046911:Macromolecular Substances; D009243:NAD / Q000494:pharmacology*; D011725:Pyridines / Q000494:pharmacology; D014508:Urea / Q000494:pharmacology
D003432:Cross-Linking Reagents; D003959:Diamines; D004800:Enzymes, Immobilized; D007096:Imidoesters; D046911:Macromolecular Substances; D011725:Pyridines; D009243:NAD; C049633:vinylpyridine-acrolein copolymer; D000171:Acrolein; D014508:Urea; D006864:Hydrogenase; D005976:Glutaral