scholarly journals Karakterisasi Plantarisin IIA-1A5 sebagai Antimikroba dan Evaluasi Aktivitas Sediaan Kering Beku Terenkapsulasi

2020 ◽  
Vol 9 (1) ◽  
pp. 30
Author(s):  
Mochammad Sriduresta Soenarno ◽  
Irma Isnafia Arief ◽  
Cece Sumantri ◽  
Epi Taufik ◽  
Lilis Nuraida
Keyword(s):  
Molecular Weight ◽  
Staphylococcus Aureus ◽  
Antimicrobial Activity ◽  
Lactobacillus Plantarum ◽  
Exchange Chromatography ◽  
Single Band ◽  
Food Preservatives ◽  
Maldi Tof ◽  
Freeze Dried ◽  
Sds Page

Bakteriosin adalah peptida dengan aktivitas antibakteri yang diproduksi oleh bakteri asam laktat dan digunakan sebagai pengawet alami. Penelitian sebelumnya menunjukkan bahwa Lactobacillus plantarum IIA-1A5 memproduksi bakteriosin yang diberi nama Plantarisin IIA-1A5 pada medium pertumbuhan yang dibuat dari whey yang diperkaya skim. Untuk aplikasi sebagai pengawet alami dan untuk memperbaiki masa simpan dan aktivitas anti mikrobanya, plantarisin perlu dienkapsulasi dan dikeringbekukan. Tujuan dari penelitian ini adalah untuk mengkarakterisasi dan mengevaluasi aktivitas antimikroba dari sediaan plantarisin IIA-1A5 yang terpurifikasi parsial dan terenkapsulasi kering beku. Ekstraksi dan purifikasi dari bakteriosin dimulai dengan presipitasi dengan ammonium sulfat, yang diikuti dengan dialysis, dan penukar kation kromatografi. Purifikasi parsial dari plantarisin kemudian dimikroenkapsulasi dengan maltodextrin kemudian dilanjutkan dengan proses kering beku. Berdasarkan pada SDS-PAGE, fraksi protein ke-7 (F7) dari plantarisin yang dipurifikasi parsial memiliki pita tunggal dan berat molekul sekitar 9,65 kDa. Konfirmasi lebih lanjut dengan menggunakan MALDI-TOF MS, ternyata pita tunggal tersebut terdiri dari 5 peptida yang diidentifikasi berbobot molekul masing-masing sebagai berikut 5,5, 7,80, 7,96, 9,09, dan 9,27 kDa. Plantarisin kering beku memiliki aktivitas antimikroba terhadap Staphylococcus  aureus tiga kali lipat dibandingkan dengan aktivitas antimikroba dari supernatan bebas sel, dan lebih tinggi dibandingkan dengan nisin, namun kurang bila dibandingkan dengan antibiotik ampisilin dan penisilin. Kesimpulannya, aktivitas antimikroba plantarisin kering beku dapat ditentukan dan lebih tinggi dibandingkan dengan nisin, ampisilin dan penisilin.Characterization of Plantarisin IIA-1A5 as Antimicrobial subtances and Evaluation of Acitivity of Freeze-dried Microencapsulated PreparationAbstractBacteriocins are peptides with antibacterial activity produced by lactic acid bacteria and used as natural preservatives. Previous studies showed that Lactobacillus plantarum IIA-1A5 produces bacteriocin named plantaricin IIA-1A5 in the medium consisting whey enriched with skim milk. For application as food preservatives and to improve its shelf-lie and activity, plantaricin was needed to be microencapsulated and freeze dried. The objective of this research was to characterize and evaluate the activity of partially purified freeze dried microencapsulated plantaricin IIA-1A5. Characterisation of partially purified plantaricin IIA-IA5 includes the identification of active fractions and molecular weight, evaluation of activity at different stage of purification and evaluation of antimicrobial activity of freeze dried microencapsulated plantaricin IIA-IA5. Extraction and prificafication of the bacteriocins started with precipitacion with ammonium sulfate, followed by dialysis, and cation exchange chromatography. The partial purified of plantaricin was then microencapsulated in maltodextrin followed by freeze drying. Based on SDS-PAGE, the protein fraction F7 of partially purified plantaricin had a single band and molecular weight about 9.65 kDa. Further analyses using MALDI-TOF, it revealed that five peptides were identified from one single band plantaricin with molecular weight 5.5, 7.80, 7.96, 9.09, and 9.27 kDa, respectively. The freeze dried plantaricin freeze showed antimicrobial activity against Staphylococcus aureus three times stringer as compared to the activity of cell free supernatant, and was higher than nicin, but less than antibiotic ampicilin and penicilin. As concusion, the activity of freeze dried plantaricin could be determined and had a higher value than nicin, ampicilin and penicilin.

Antimicrobial activity of bacteriocin isolated and purified from rumen liquor collected from slaughtered goats

2015 ◽  
Vol 49 (6) ◽  
Author(s):  
S. Barathiraja ◽  
J. Thanislass ◽  
P. X. Antony ◽  
S. Venkatesaperumal
Keyword(s):  
Molecular Weight ◽  
Staphylococcus Aureus ◽  
Antimicrobial Activity ◽  
Bacillus Subtilis ◽  
Gel Filtration ◽  
Diffusion Method ◽  
Chromatographic Techniques ◽  
Ammonium Sulphate Precipitation ◽  
Sds Page ◽  
Overlay Method

Bacteriocin like substance with antimicrobial activity was purified from freshly collected rumen liquor using 60% ammonium sulphate precipitation followed by ion exchange(SP-Sepharose) and gel filtration (Sephadex G25) chromatographic techniques. Purity of the product was checked on SDS-PAGE, having molecular weight of 6.5 kDa. Anti-microbial activity was demonstrated using <italic>Bacillus subtilis</italic> by gel overlay method and agar cut well diffusion method. Proteomic analysis confirmed the substance as bacteriocin. The purified sample was resistant to the action of protease. The substance was active at pH 4, 7 and 10. It was also active at autoclave temperature. The peptide purified was found to inhibit the growth of <italic>Staphylococcus aureus</italic> (MTCC87), <italic>Listeria monocytogenes</italic> (MTCC 657) and <italic>Pseudomonas aeurginosa</italic> (MTCC 424).

scholarly journals 2155. Accelerated Confirmation of Porin Loss in Carbapenem-Resistant Enterobacterales: A MALDI-TOF Mass Spectrometry-Based Approach

2019 ◽  
Vol 6 (Supplement_2) ◽  
pp. S731-S731
Author(s):  
Carlos Correa-Martinez ◽  
Evgeny A Idelevich ◽  
Karsten Becker
Keyword(s):  
Mass Spectrometry ◽  
Molecular Weight ◽  
Gold Standard ◽  
Sodium Dodecylsulfate ◽  
Resistant Bacteria ◽  
Maldi Tof Ms ◽  
Maldi Tof ◽  
Carbapenem Resistant ◽  
Sds Page ◽  
Tof Ms

Abstract Background The accurate identification of carbapenem resistance mechanisms is decisive for the appropriate selection of antibiotic regimens. Numerous methods can detect carbapenemase-producing carbapenem-resistant bacteria (CPCR). However, non-CPCR (NCPCR) are routinely assumed to display porin loss as a diagnosis of exclusion. No further confirmatory tests are performed since the gold standard (sodium dodecylsulfate polyacrylamide gel electrophoresis, SDS–PAGE) is laborious and time consuming. We propose a test for rapid and easy detection of porin loss by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). Methods Clinical meropenem-resistant Enterobacterales strains (10 CPCR, 10 NCPCR) and control strains recommended by EUCAST (5 carbapenemase-producing, one with porin loss, one-negative control) were analyzed. Membrane proteins were extracted by successive centrifugation of bacterial suspensions (McFarland 0.5) and addition of ethanol, formic acid and acetonitrile. MALDI-TOF MS of the protein extracts was performed on a 96-spot target (Bruker Daltonics, Germany). Peaks between 35 and 40 kDa were analyzed for the presence of porins and compared with the bands observed in the SDS–PAGE of the protein extracts. Results Within the molecular weight range of 35–40 kDa, the MALDI-TOF MS-based method revealed peaks in all CPCR isolates corresponding to those observed in the carbapenemase-producing control strains. In contrast, the control strain with porin loss as well as all CNCR isolates showed a lower quantity of peaks in this range. All peaks observed correlated with the bands observed in the SDS–PAGE of the protein extracts at the corresponding molecular weight (Figure 1). Conclusion Yielding results that reliably correspond to the current gold standard, we propose a method for accelerated detection of porin loss as an alternative to the diagnosis of exclusion usually made in routine settings. With a processing time of approximately 20 minutes, the method can be easily implemented in the clinical setting. Applying this MALDI-TOF MS-based approach, valuable information will be provided about a resistance mechanism that otherwise remains unexplained. Disclosures All authors: No reported disclosures.

Bacteriocin ST91KM, produced by Streptococcus gallolyticus subsp. macedonicus ST91KM, is a narrow-spectrum peptide active against bacteria associated with mastitis in dairy cattle

2008 ◽  
Vol 54 (7) ◽  
pp. 525-531 ◽  
Author(s):  
Reneé Pieterse ◽  
Svetoslav D. Todorov ◽  
Leon M.T. Dicks
Keyword(s):  
Staphylococcus Aureus ◽  
Antimicrobial Activity ◽  
Streptococcus Agalactiae ◽  
Staphylococcus Epidermidis ◽  
Mode Of Action ◽  
Proteolytic Enzymes ◽  
Streptococcus Dysgalactiae ◽  
Streptococcus Gallolyticus ◽  
Streptococcus Uberis ◽  
Sds Page

Streptococcus gallolyticus subsp. macedonicus ST91KM produces a bacteriocin (macedocin ST91KM) active against Streptococcus agalactiae , Streptococcus dysgalactiae subsp. dysgalactiae , Streptococcus uberis , Staphylococcus aureus , and Staphylococcus epidermidis . Macedocin ST91KM is, according to tricine-SDS PAGE, between 2.0 and 2.5 kDa in size. Antimicrobial activity remained unchanged after 2 h of incubation at pH 2.0–10.0 and after 100 min at 100 °C. The peptide was inactivated after 20 min at 121 °C and when treated with proteolytic enzymes. Treatment with α-amylase had no effect on activity, suggesting that the mode of action does not depend on glycosylation. Amplification of the genome of strain ST91KM with primers designed from the macedocin precursor gene (mcdA) produced 2 fragments (approximately 375 and 220 bp) instead of one 150-bp fragment, as recorded for macedocin produced by Streptococcus gallolyticus subsp. macedonicus ACA-DC 198. Strain ACA-DC 198 was not available. However, DNA amplified from strain LMG 18488 (ACA-DC 206), genetically closely related to strain ACA-DC 198, revealed 99% homology to the mcdA of strain ACA-DC 198 (accession No. DQ835394). Macedocin ST91KM may thus be a second putative bacteriocin described for Streptococcus gallolyticus subsp. macedonicus.

scholarly journals Characterization of Reutericyclin Produced by Lactobacillus reuteri LTH2584

2000 ◽  
Vol 66 (10) ◽  
pp. 4325-4333 ◽  
Author(s):  
Michael G. Gänzle ◽  
Alexandra Höltzel ◽  
Jens Walter ◽  
Günther Jung ◽  
Walter P. Hammes
Keyword(s):  
Staphylococcus Aureus ◽  
Antimicrobial Activity ◽  
Culture Supernatant ◽  
Lactobacillus Reuteri ◽  
Gel Filtration ◽  
Reversed Phase ◽  
Exchange Chromatography ◽  
Growth Media ◽  
Dependent Manner ◽  
Cell Extracts

ABSTRACT Lactobacillus reuteri LTH2584 exhibits antimicrobial activity that can be attributed neither to bacteriocins nor to the production of reuterin or organic acids. We have purified the active compound, named reutericyclin, to homogeneity and characterized its antimicrobial activity. Reutericyclin exhibited a broad inhibitory spectrum including Lactobacillus spp., Bacillus subtilis, B. cereus, Enterococcus faecalis, Staphylococcus aureus, and Listeria innocua. It did not affect the growth of gram-negative bacteria; however, the growth of lipopolysaccharide mutant strains ofEscherichia coli was inhibited. Reutericyclin exhibited a bactericidal mode of action against Lactobacillus sanfranciscensis, Staphylococcus aureus, and B. subtilis and triggered the lysis of cells of L. sanfranciscensis in a dose-dependent manner. Germination of spores of B. subtilis was inhibited, but the spores remained unaffected under conditions that do not permit germination. The fatty acid supply of the growth media had a strong effect on reutericyclin production and its distribution between producer cells and the culture supernatant. Reutericyclin was purified from cell extracts and culture supernatant of L. reuteri LTH2584 cultures grown in mMRS by solvent extraction, gel filtration, RP-C8 chromatography, and anion-exchange chromatography, followed by rechromatography by reversed-phase high-pressure liquid chromatography. Reutericyclin was characterized as a negatively charged, highly hydrophobic molecule with a molecular mass of 349 Da. Structural characterization (A. Höltzel, M. G. Gänzle, G. J. Nicholson, W. P. Hammes, and G. Jung, Angew. Chem. Int. Ed. 39:2766–2768, 2000) revealed that reutericyclin is a novel tetramic acid derivative. The inhibitory activity of culture supernatant of L. reuteri LTH2584 corresponded to that of purified as well as synthetic reutericyclin.

scholarly journals Expression of Lon-like Protease Gene from Lactobacillus plantarum IIA-1A5 in Escherichia coli BL21(DE3)

2019 ◽  
Vol 19 (2) ◽  
pp. 149-158
Author(s):  
Olfa Mega ◽  
Cece Sumantri ◽  
Irma Isnafia Arief ◽  
Cahyo Budiman
Keyword(s):  
Molecular Weight ◽  
Lactobacillus Plantarum ◽  
Expression System ◽  
Gc Content ◽  
Whole Genome Sequence ◽  
Protease Gene ◽  
Iptg Induction ◽  
E Coli ◽  
Sds Page ◽  
Index Value

Proteases are one of most important and abundant enzymes produced by the biotechnology industry, for scientific, physiological and industrial application and dominates of the whole enzyme market. Lactobacillus plantarum IIA-1A5 is an Indonesian lactic acid bacteria (LAB) isolated from beef Peranakan Ongole cattle. Preliminary analysis on its whole genome sequence indicated that this strain harbours some genes involved in protein degradation and might be promising to be further applied. This study aims to optimize the gene sequence of a lon-like protease of L. plantarum IIA-1A5 for heterologous expression system. The Lon-like gene expression system is made using genes that have been optimized first in silico.  pET-28a(+), E. coli BL21(DE3), Nde1 and BamH1 were used in this study as a expression vector, a host and retriction enzyme, respectively.  Molecular weight was validated using SDS-PAGE and expasy.org software. The results showed that optimization increased codon adaptation index value (CAI) and GC content to 0.97 and 56.57%, respectively, which were suitable for the E. coli expression system. The Lon-like IIA gene was successfully expressed in the cell cytoplasm by induction of 1 mM Isopropyl β-D-1-thiogalactopyranoside (IPTG) at 37 °C.  As many as 88% of Lon-like IIA codons were distributed in the 91-100 quality group. Lon-like IIA was successfully expressed in a host cell induced with 1 mM IPTG at 37oC . IPTG induction was performed at the 3rd hour of incubation with OD600 0.59. In addition, Lon-like IIA molecular weight was detected approximately 43 kDa.

scholarly journals POTENSI BAKTERI ASAM LAKTAT DALAM MENGHASILKAN BAKTERIOSIN SEBAGAI ANTIMIKROBA DAN PENGUKURAN BERAT MOLEKULNYA DENGAN SDS-PAGE DARI ISOLAT FERMENTASI KAKAO

2015 ◽  
Vol 1 (2) ◽  
pp. 126
Author(s):  
Urnemi ◽  
Sumaryati Syukur ◽  
Endang Purwati ◽  
Sanusi Ibrahim ◽  
Jamsari
Keyword(s):  
Staphylococcus Aureus ◽  
Antimicrobial Activity ◽  
Bacillus Subtilis ◽  
Lactic Acid ◽  
Lactic Acid Bacteria ◽  
Pathogenic Bacteria ◽  
Inhibition Zone ◽  
Sds Page ◽  
Inhibition Zones ◽  
And Staphylococcus Aureus

ABSTRACT Lactic acid bacteria (LAB) were isolated from of cocoa beans fermentation Forestero variety from West Sumatera, that were eleven isolates. The isolates were tested to antimicrobial activity against pathogenic bacteria E.coli NBRC 14237, Staphylococcus aureus NBRC 13276, Bacillus subtilis BTCCB 612, listeria m. dan S. Typhii. Results the research showed that, isolates had inhibition zone to pathogenic bacteria, that were 7 mm till 12 mm at 48 hours observation. R2.4 isolate was most potential to inhibition zones growth pathogenic bacteria, that was 11mm till 12 mm to five pathogens. R2.4 isolates was the highest to against pathogenic bacteria (Bacillus subtilis BTCCB, Listeria monocytogenesis and Staphylococcus aureus NBRC) had inhibition zones, that was 12.00 mm till 48 hours. Listeria monocytogenesis had been known as pest bacterium of food born, so that R2.4 isolate can be used as food biopreservative. Crude of R2.4 isolate molecular weight was 10 kDa by SDS-PAGE.  Key words: Lactic acid bacteria, Antimicrobial activity, SDS-PAGE, Cocoa fermentation and food biopreservative                                                      

scholarly journals New Exfoliative Toxin Produced by a Plasmid-Carrying Strain of Staphylococcus hyicus

1999 ◽  
Vol 67 (8) ◽  
pp. 4014-4018 ◽  
Author(s):  
Hisaaki Sato ◽  
Takao Watanabe ◽  
Yasuko Murata ◽  
Ayumi Ohtake ◽  
Mayumi Nakamura ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Staphylococcus Aureus ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
The Other ◽  
Exfoliative Toxin ◽  
Sds Page ◽  
Serotype B

ABSTRACT A new serotype of Staphylococcus hyicus exfoliative toxin (SHET), serotype B, was isolated from the culture filtrate of a plasmid-carrying strain of S. hyicus. The new SHET was purified by precipitation with 70% saturated ammonium sulfate, gel filtration on a Sephadex G-75 column, column chromatography on DEAE–Cellulofine A-500, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The new SHET caused exfoliation of the epidermis as determined by the so-called Nikolsky sign when inoculated into 1-day-old chickens. The new SHET was serologically different fromStaphylococcus aureus exfoliative toxins (ETs) (ETA, ETB, and ETC) and from the SHET from the plasmidless strain but showed the same molecular weight as the other serotypes of toxins on SDS-PAGE. It was thermolabile and lost its toxicity after being heated at 60°C for 30 min. We propose that the new SHET be designated SHETB and that the SHET produced by the plasmidless strain be designated SHETA.

scholarly journals In-vitro and In-silico approach for characterization of antimicrobial-peptide from probiotics against Staphylococcus aureus and Escherichia coli

2021 ◽  
Author(s):  
Amrutha Bindu ◽  
Lakshmidevi N
Keyword(s):  
Escherichia Coli ◽  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Lactobacillus Plantarum ◽  
Exchange Chromatography ◽  
Proteinase K ◽  
Kinetic Assay ◽  
Wide Range

Abstract The present aim was to determine the characteristic feature and stability of antimicrobial compound (AMC) produced by probiotic strains of Enterococcus durans MCC4243, Lactiplantibacillus plantarum (Basanym: Lactobacillus plantarum MCC4246) and Limosilactobacillus fermentum (Basonym: Lactobacillus fermentum MCC4233) against Staphylococcus aureus MTCC96 and Escherichia coli MTCC118. Growth kinetic assay revealed 24h of incubation to be optimum for bacteriocin production. Ammonium sulphate precipitation-dialysis was found to be favorable method for extraction of AMC compared to other methods employed. The partially purified compound after ion-exchange chromatography was found to be thermo-resistant upto 90°C and stable under wide range of pH. The compound was sensitive to proteinase-K, but resistant to trypsin, α-amylase and lipase. The apparent molecular weight of AMC from MCC4243 and MCC4246 was found to be 3.5KDa. PCR confirmed the presence of plantaricinA gene in MCC4246. Translated partial amino acid sequence of plnA gene of MCC4246 displayed 48 amino acid sequence which had 100% similarity with plantaricinA of Lactobacillus plantarum (WP 0036419). The sequence revealed 7 β sheets, 6 α sheets, 6 predicted coils and 9 predicted turns and functions on cytoplasm with 10.82 isoelectric point and 48.6% hydrophobicity. From the study, the amino acid sequence “KSSAYSLQMGATAIKQVKKLFKKWGW” of peptide was predicted to be responsible for antimicrobial activity.

scholarly journals Plantaricin IIA-1A5 from Lactobacillus plantarum IIA-1A5 displays bactericidal activity against Staphylococcus aureus

2015 ◽  
Vol 6 (4) ◽  
pp. 603-613 ◽  
Author(s):  
I. Isnafia Arief ◽  
C. Budiman ◽  
B. Sri Laksmi Jenie ◽  
E. Andreas ◽  
A. Yuneni
Keyword(s):  
Staphylococcus Aureus ◽  
Cell Membrane ◽  
Lactobacillus Plantarum ◽  
Histidine Kinase ◽  
Mode Of Action ◽  
Apparent Size ◽  
Gene Encoding ◽  
Disulphide Bonds ◽  
Sds Page ◽  
Quorum Sensor

Plantaricin IIA-1A5 is a bacteriocin produced by Lactobacillus plantarum IIA-1A5 isolated from Indonesian beef. This research aimed to identify the genes involved in plantaricin IIA-1A5 production and examine its mode of action against Staphylococcus aureus. It has been reported that a bacteriocin structural gene, plnW, is present in genome of L. plantarum IIA-1A5. Here, we reported the presence of additional genes responsible for plantaricin precursor (plnA and plnEF) and a gene encoding the quorum sensor of histidine kinase (plnB). It indicates that genes involved in production of plantaricin IIA-1A5 are organized in at least two bacteriocin operons (plnABCD, plnEFI) and a structural plnW gene. Purified plantaricin IIA-1A5 yielded a single band in SDS-PAGE with apparent size of 6.4 kDa. Amino acid composition of purified plantaricin IIA-1A5 was mainly composed of cationic glutamic acid and cysteine that allowed the formation of disulphide bonds, suggesting plantaricin IIA-1A5 belongs to the pediocin-subclass of class II bacteriocins. Plantaricin IIA-1A5 displayed remarkable antibacterial activity against S. aureus, which was initiated by the adsorption of plantaricin IIA-1A5 onto the cell membrane of S. aureus. The adsorption is hypothesised to be facilitated by non-ionic interactions as it is reduced by the presence of organic solvents or detergents. This adsorption promoted leakage of cellular metabolites through the cell membrane of S. aureus, as indicated by the release of genetic and proteinaceous material of S. aureus observed at 260 and 280 nm, respectively. The leakage also promoted the release of divalent (Ca2+, Mg2+) and monovalent (K+) cations. The release of these intracellular components might be due to pores formed in the cell membrane of S. aureus by plantaricin IIA-1A5 as shown by scanning electron microscopy. Altogether, the mode of action of plantaricin IIA-1A5 against S. aureus seems to be bactericidal as indicated by lysis of the cell membrane.

scholarly journals Antimicrobial Activities of Ellagitannins against Clostridiales perfringens, Escherichia coli, Lactobacillus plantarum and Staphylococcus aureus

Molecules ◽  
2020 ◽  
Vol 25 (16) ◽  
pp. 3714
Author(s):  
Elina Puljula ◽  
Gemma Walton ◽  
Martin J. Woodward ◽  
Maarit Karonen
Keyword(s):  
Escherichia Coli ◽  
Staphylococcus Aureus ◽  
Antimicrobial Activity ◽  
Growth Inhibition ◽  
Lactobacillus Plantarum ◽  
Molecular Size ◽  
Antimicrobial Effects ◽  
E Coli ◽  
Inhibition Effect ◽  
And Staphylococcus Aureus

In this study, we tested the growth inhibition effect of 22 individual ellagitannins and of pentagalloylglucose on four bacterial species, i.e., Clostridiales perfringens, Escherichia coli, Lactobacillus plantarum and Staphylococcus aureus. All tested compounds showed antimicrobial effects against S. aureus, and almost all against E. coli and C. perfringens. For L. plantarum, no or very weak growth inhibition was detected. The level of inhibition was the greatest for S. aureus and the weakest for C. perfringens. For S. aureus, the molecular size or flexibility of ellagitannins did not show a clear relationship with their antimicrobial activity, even though rugosins E and D and pentagalloylglucose with four or five free galloyl groups had a stronger growth inhibition effect than the other ellagitannins with glucopyranose cores but with less free galloyl groups. Additionally, our results with S. aureus showed that the oligomeric linkage of ellagitannin might have an effect on its antimicrobial activity. For E. coli, the molecular size, but not the molecular flexibility, of ellagitannins seemed to be an important factor. For C. perfringens, both the molecular size and the flexibility of ellagitannin were important factors. In previous studies, corilagin was used as a model for ellagitannins, but our results showed that other ellagitannins are much more efficacious; therefore, the antimicrobial effects of ellagitannins could be more significant than previously thought.

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