Abstract
The growth studies of methionine requiring mutant of Escherichia coli disclosed that several acyl methionines were utilized by the mutants. Furthermore, the cell-free extracts of Escherichia coli and Aerobacter aerogenes were found to show almost equal hydrolytic activity towards acyl amino acids.In order to find the enzymatic properties of the acylase activity, the experiments were carried out with the alcohol-fractionated extracts of the acetone-dried cells of Escherichia coli K-12. As a result of the investigation, acylase activity of the preparation from Escherichia coli was found to be lower and also a lesser number of acyl amino acids were hydrolyzed than the mold acylase which had been previously studied by the authors. Activation by cobalt ion and several other observation were also presented.
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