ENZYMES RELEASED FROM ESCHERICHIA COLI WITH THE AID OF A SERVALL CELL FRACTIONATOR.
The release and stability of the enzymes S-adenosylhomocysteine nucleosidase, lysine decarboxylase, arginine decarboxylase, glutamic decarboxylase, formic hydrogenlyase, formic oxidase, and glucose oxidase from Escherichia coli during disruption of the organisms in a Servall-Ribi refrigerated cell fractionator were examined. With the possible exception of arginine decarboxylase, maximal activity was retained by all the enzymes reported here when the cell suspensions were processed at pressures necessary for rupture of all the organisms (15,000 to 25,000 psi). Considerable variation in the stability of different enzymes liberated by disruption at higher pressures (45,000 to 55,000 psi) was observed. It is reasonable to assume that mechanical forces rather than effects of temperature are responsible for inactivation of these enzymes.
D002262:Carboxy-Lyases; D004926:Escherichia coli; D005949:Glucose Oxidase; D006836:Hydro-Lyases; D008660:Metabolism; D009699:N-Glycosyl Hydrolases; D010088:Oxidoreductases; D012106:Research
D010088:Oxidoreductases; D005949:Glucose Oxidase; D009699:N-Glycosyl Hydrolases; C019606:adenosylhomocysteine nucleosidase; D002262:Carboxy-Lyases; C021520:lysine decarboxylase; C019722:arginine decarboxylase; D006836:Hydro-Lyases
CARBOXY-LYASES; ESCHERICHIA COLI; EXPERIMENTAL LAB STUDY; GLUCOSE OXIDASE; HYDRO-LYASES; METABOLISM; NUCLEOSIDASES; OXIDOREDUCTASES