Immobilization of fatty acid synthetase from Mycobacterium smegmatis by radiation-induced polymerization.
Fatty acid synthetase of Type I from Mycobacterium smegmatis was immobilized by radiation-induced polymerization of 2-hydroxyethyl methacrylate (HEMA) in the presence of trimethylolpropane trimethacrylate (TMPTMA). The stability of immobilized synthetase toward low ionic strength increased in comparison with the free form, but the stabilities of immobilized preparations assessed by pH and temperature were identical to those of the free form. The apparent Km of immobilized enzyme for acetyl-CoA and malonyl-CoA were both 6 microM, essentially the same as those of the free form; acetyl-CoA, 5 microM and malonyl-CoA, 6 microM.
Kikuchi
S
S
Department of Chemical Engineering, Muroran Institute of Technology, Hokkaido, Japan.
Kolattukudy
P E
PE
D000105:Acetyl Coenzyme A / Q000378:metabolism; D002849:Chromatography, Gas; D003432:Cross-Linking Reagents; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000378:metabolism; D064429:Fatty Acid Synthases / Q000737:chemistry* / Q000378:metabolism / Q000528:radiation effects; D005455:Fluorescent Antibody Technique; D006863:Hydrogen-Ion Concentration; D008316:Malonyl Coenzyme A / Q000378:metabolism; D008689:Methacrylates; D009161:Mycobacterium / Q000201:enzymology*; D011108:Polymers; D013696:Temperature
D003432:Cross-Linking Reagents; D004800:Enzymes, Immobilized; D008689:Methacrylates; D011108:Polymers; D008316:Malonyl Coenzyme A; C005044:hydroxyethyl methacrylate; D000105:Acetyl Coenzyme A; D064429:Fatty Acid Synthases; C028643:trimethylolpropane trimethacrylate