Abstract
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.
Keywords
CARBOXY-LYASES
ESCHERICHIA COLI
EXPERIMENTAL LAB STUDY
GLUCOSE OXIDASE
HYDRO-LYASES
METABOLISM
NUCLEOSIDASES
OXIDOREDUCTASES
MeSH Terms
Carboxy-Lyases
Escherichia coli
Glucose Oxidase
Hydro-Lyases
Metabolism
N-Glycosyl Hydrolases
Oxidoreductases
Research
Chemicals
Oxidoreductases
Glucose Oxidase
N-Glycosyl Hydrolases
adenosylhomocysteine nucleosidase
Carboxy-Lyases
lysine decarboxylase
arginine decarboxylase
Hydro-Lyases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
DUERRE J A
RIBI E
References (11)
11 references, click to expand
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