2003
DOI: 10.1007/s00253-003-1312-9
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?-Poly-l-lysine: microbial production, biodegradation and application potential

Abstract: epsilon-Poly-L-lysine (epsilon-PL) is a homo-poly-amino acid characterized by the peptide bond between the carboxyl and epsilon-amino groups of L-lysine. epsilon-PL shows a wide range of antimicrobial activity and is stable at high temperatures and under both acidic and alkaline conditions. The mechanism of the inhibitory effect of epsilon-PL on microbial growth is the electrostatic adsorption to the cell surface of microorganisms on the basis of its poly-cationic property. Due to this antimicrobial activity, … Show more

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Cited by 337 publications
(225 citation statements)
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“…This outcome may correlate with the 100 fold decrease in antimicrobial activity that pεK, with <9 lysine residues, has when compared with longer chain residues. [ 33,34 ] There may not be enough of a difference in the number of free amino groups side-by-side within the polymer backbone to make a signifi cant difference to antimicrobial activity between the three cross-link densities. To test this hypothesis, pεK was added post-polymerization to the hydrogel as longer chains.…”
Section: Doi: 101002/adhm201600258mentioning
confidence: 99%
“…This outcome may correlate with the 100 fold decrease in antimicrobial activity that pεK, with <9 lysine residues, has when compared with longer chain residues. [ 33,34 ] There may not be enough of a difference in the number of free amino groups side-by-side within the polymer backbone to make a signifi cant difference to antimicrobial activity between the three cross-link densities. To test this hypothesis, pεK was added post-polymerization to the hydrogel as longer chains.…”
Section: Doi: 101002/adhm201600258mentioning
confidence: 99%
“…Biosynthesized ε-PL is a hydrophilic cationic linear homopoly-amino acid typically composed of 25 to 35 identical L-lysine residues with an isoelectric point around 9.0 and is described as having a peptide bond between carboxyl groups and ε-amino groups of L-lysine residues rather than the conventional peptide bonds linking ␣-poly-L-lysine (␣-PL) (8). ε-PL is produced by a membrane-bound ε-PL synthetase that has the characteristics of nonribosomal peptide synthetases, which does not bind the elongating ε-PL chain covalently during polymerization (9).…”
mentioning
confidence: 99%
“…There are two classes of outer membrane permeabilizers: (i) polycationic agents, such as polymyxin and its derivatives, which interact with phospholipids in the cell membrane (163,164), or lysine polymers, which adsorb to the cell surface and block growth (164,165); and (ii) chelators, such as EDTA, which remove ions from the outer membrane, leading to its disintegration (163,164), or weak organic acids, which penetrate the cell wall and interfere with bacterial physiology (163,164). Nonetheless, it is important to highlight that the in vivo toxicity of the outer membrane permeabilizers might limit the applicability of this approach.…”
Section: Phage-derived Antimicrobialsmentioning
confidence: 99%