Mode of Action of Pectic Enzymes II. Further Purification of Exopolygalacturonate Lyase and Pectinesterase from Clostridium multifermentans

Autor:	L. Miller, J. D. Macmillan
Rok vydání:	1970
Předmět:	chemistry.chemical_classification Pectinesterase activity biology Size-exclusion chromatography biology.organism_classification Lyase Microbiology Esterase Pectinesterase Clostridium Enzyme Biochemistry chemistry Sephadex Molecular Biology
Zdroj:	Journal of Bacteriology. 102:72-78
ISSN:	1098-5530 0021-9193
DOI:	10.1128/jb.102.1.72-78.1970
Popis:	Exopolygalacturonate lyase and pectinesterase from Clostridium multifermentans were purified 156-fold and 178-fold, respectively, by gel filtration chromatography on Sephadex G-200. The activities of both enzymes coincided in a single protein peak. Profiles of the two activities also coincided in diethylaminoethyl-cellulose chromatography and zonal centrifugation. These studies indicated that the esterase and the lyase were either complexed or similar molecular species. The former seems more probable because of the relatively high molecular weight. Both activities were most stable at p H 6.0. The esterase was inactivated rapidly at p H 5 or 7. Lyase preparations were freed of pectinesterase activity by heating for 30 min at 38 C and p H 7.0.
Databáze:	OpenAIRE
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