An exopectate lyase of Butyrivibrio fibrisolvens from the bovine rumen.
An extracellular pectinolytic enzyme produced by Butyrivibrio fibrisolvens isolated from the bovine rumen was studied. The enzyme had a pH optimum of 8.0 to 8.5 and was stimulated by Ca2+ and inhibited by EDTA. The products of pectinolysis had an absorption peak at 235 nm and reacted with thiobarbituric acid, indicating a lyase type of action. The enzyme cleaved the substrates terminally from the reducing end; action on poly- and oligogalacturonates resulted in the formation of an unsaturated trigalacturonate. The enzyme was classified as an exopectate lyase (EC 4.2.2.9). A pectinesterase was also produced by B. fibrisolvens but polygalacturonase was not detected.
D000818:Animals; D002417:Cattle; D005260:Female; D006089:Gram-Negative Anaerobic Bacteria / Q000201:enzymology*; D007700:Kinetics; D010368:Pectins / Q000378:metabolism; D011133:Polysaccharide-Lyases / Q000378:metabolism*; D012417:Rumen / Q000382:microbiology*; D013379:Substrate Specificity; D014783:Viscosity
D010368:Pectins; D011133:Polysaccharide-Lyases; C037051:pectate disaccharide-lyase