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Enzymatic Modification of Soluble Cyanophycin Using the Type II Peptidyl Arginine Deiminase from Oryctolagus cuniculus
Author(s) -
Wiefel Lars,
Steinbüchel Alexander
Publication year - 2016
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.201500433
Subject(s) - arginine , chemistry , chemical modification , biochemistry , lysine , enzyme , escherichia coli , citrulline , arginine deiminase , heterologous , recombinant dna , heterologous expression , amino acid , stereochemistry , gene
An increased structural variety expands the number of putative applications for cyanophycin (multi‐ l ‐arginyl‐poly‐[ l ‐aspartic acid], CGP). Therefore, structural modifications of CGP are of major interest; these are commonly obtained by modification and optimization of the bacterial producing strain or by chemical modification. In this study, an enzymatic modification of arginine side chains from lysine‐rich CGP is demonstrated using the peptidyl arginine deiminase from Oryctolagus cuniculus , purified from Escherichia coli after heterologous expression. About 10% of the arginine side chains are converted to citrulline which corresponds to 4% of the polymer's total side chains. An inhibition of the reaction in the presence of small amounts of l ‐citrulline is observed, thereby explaining the low conversion rate. CGP dipeptides can be modified with about 7.5 mol% of the Asp‐Arg dipeptides being converted to Asp‐Cit. These results show that the enzymatic modification of CGP is feasible, opening up a whole new area of possible CGP modifications for further research.