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A Study by High Voltage Electrophoresis of the Amino Acid Decarboxylases and Arginine Dihydrolase of Bacteria Isolated from the Alimentary Tract of Pigs
Author(s) -
Cheeseman G. C.,
Fuller R.
Publication year - 1966
Publication title -
journal of applied bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 0021-8847
DOI - 10.1111/j.1365-2672.1966.tb03513.x
Subject(s) - arginine , ornithine , lysine , putrescine , biochemistry , arginine decarboxylase , lysine decarboxylase , bacteria , escherichia coli , amino acid , lactobacillus plantarum , biology , alimentary tract , ornithine decarboxylase , microbiology and biotechnology , enzyme , chemistry , lactic acid , genetics , gene , cadaverine , medicine
S ummary . The use of high voltage paper electrophoresis for studies on the breakdown of amino acids by bacteria is described. Examination of a number of different isolates from the alimentary tract of the pig showed that the decarboxylase activity was restricted to Escherichia coli and one strain of Lactobacillus fermenti. In some isolates studied the optimum pH of activity differed from those previously reported for similar systems, being higher for ornithine, glutamic acid and lysine decarboxylases. The heterofermentative lactobacilli all converted arginine to ornithine and this may contribute to the final level of putrescine in the gut by providing a substrate for the ornithine decarboxylase of E. coli.