Antibacterial characteristics of fish protamines. VI Changes in the cell morphology and the release of soluble constituents from the washed cells of Bacillus subtilis by the action of protamine.

Islam, Nazrul; Oda, Hiroshi; Motohiro, Terushige

doi:10.2331/suisan.53.297

Cited by 16 publications

(15 citation statements)

References 4 publications

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“…Japanese studies have reported that protamines have bacteriostatic or bacteriocidal effects on Gram-positive bacteria while Gram-negative cells in most of the published studies seem unaffected (Islam et al, 1987;Yanagimoto et al, 1992). It has been shown that the protamines cause leakage of cell material as they bind to the cell surface (Islam et al, 1987), indicating an inhibitory mechanism similar to the bacteriocins.…”

Section: Protaminesmentioning

confidence: 99%

See 1 more Smart Citation

Biopreservation of Fish Products—A Review of Recent Approaches and Results

Huss¹,

Jeppesen²,

MSc³

et al. 1995

Journal of Aquatic Food Product Technology

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Section: Protaminesmentioning

confidence: 99%

“…It has been shown that the protamines cause leakage of cell material as they bind to the cell surface (Islam et al, 1987), indicating an inhibitory mechanism similar to the bacteriocins. Protamines inhibit moulds (Kamal and Motohiro, 1987), particularly when combined with sorbate.…”

Section: Protaminesmentioning

confidence: 99%

Biopreservation of Fish Products—A Review of Recent Approaches and Results

Huss¹,

Jeppesen²,

MSc³

et al. 1995

Journal of Aquatic Food Product Technology

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“…Ptm from herring milt (clupeine) has 20 arginine residues and a molecular weight of approximately 4.2 kDa. It is the most highly cationic, naturally-occurring CAP reported to date with a pI of 11-13. The antimicrobial characteristics of Ptm have been widely studied and reported [26][27][28][29][30][31][32][33][34][35][36]. When gram-negative Shewanella putrifaciens cells were treated with Ptm, cellular aggregation, pore formation and complete lysis of the cell envelope was obvious.…”

Section: Introductionmentioning

confidence: 99%

Interaction of protamine with gram‐negative bacteria membranes: possible alternative mechanisms of internalization in Escherichia coli, Salmonella typhimurium and Pseudomonas aeruginosa

Pink

Hasan

Quinn

et al. 2014

Journal of Peptide Science

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This study was concerned with the interaction between the cationic antimicrobial peptide, protamine (Ptm) and the cytoplasmic membranes of the gram-negative bacteria Escherichia coli, Salmonella typhimurium and Pseudomonas aeruginosa. The objective of the study was to explain the observed paradox of internalization without permanent disruption of the cell envelope. We carried out Monte Carlo computer simulation of Ptm in an aqueous environment in the presence of~100 mM NaCl and model membranes consisting of either (65:35) or (75:25) PE:PG molar ratios. The (75:25) model, representative of the gram-negative cytoplasmic membrane, showed that the Ptm center of mass remained at least 7 nm from the membrane surface leading to the prediction that Ptm would not internalize via disruption of the inner membrane.By using immunoelectron microscopy of Ptm-treated cells, we showed that Ptm internalization to the cytoplasm took place rapidly in the presence or absence of the outer envelope. Ultrastructural examination revealed no obvious morphological changes to cells that were treated with subinhibitory or bactericidal levels of Ptm. Reconstituted phospholipid bilayers were constructed and were unperturbed by Ptm treatment over a wide range of concentrations and applied transmembrane voltages. We conclude that in the cases of the cell envelopes of E. coli, S. typhimurium and P. aeruginosa, Ptm internalized by means independent of the phospholipid bilayer, most likely mediated by one or more membrane proteins such as cation-selective barrel-like proteins. Work is currently underway to test this hypothesis.

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“…This may explain why less protamine is more inhibitory at pH values at or above 7·0 despite the 90% reduction of soluble protamine caused by electrostatic interactions with the proteins in the assay substrate. Islam et al . (1987) also showed that the amount of protamine adsorbed to isolated cell walls from Bacillus subtilis increased when pH was raised from 6·2 to 8·0, thus indicating that the number of binding sites depended on pH.…”

Section: Discussionmentioning

confidence: 99%

Solubility and antimicrobial efficacy of protamine on Listeria monocytogenes and Escherichia coli as influenced by pH

Hansen

Gill

2000

J Appl Microbiol

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Listeria monocytogenes and Escherichia coli was evaluated at concentrations from 50 to 10 000 mg ml À1 and pH levels from 5Á5 to 8Á0. The minimum inhibitory concentrations decreased with increasing pH. Protamine inhibited E. coli at all pH values while L. monocytogenes was inhibited at pH 6Á5 and above. The antimicrobial ef®cacy of protamine decreased in the presence of negatively charged gelatine B but remained almost unchanged with addition of the positively charged gelatine A. Binding studies showed that the amount of protamine adsorbed to culture media components in tryptic soy broth and bacterial cells increased with increasing pH values. The increased ef®cacy of protamine at alkaline pH may be explained on the basis of an increase in electrostatic af®nity for the cell surface of target cells. E. coli produced a protamine-degrading enzyme, however, was still susceptible to protamine.

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Antibacterial characteristics of fish protamines. VI Changes in the cell morphology and the release of soluble constituents from the washed cells of Bacillus subtilis by the action of protamine.

Cited by 16 publications

References 4 publications

Biopreservation of Fish Products—A Review of Recent Approaches and Results

Biopreservation of Fish Products—A Review of Recent Approaches and Results

Interaction of protamine with gram‐negative bacteria membranes: possible alternative mechanisms of internalization in Escherichia coli, Salmonella typhimurium and Pseudomonas aeruginosa

Solubility and antimicrobial efficacy of protamine on Listeria monocytogenes and Escherichia coli as influenced by pH

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