Antibacterial activity of lactic acid bacteria isolated from vacuum‐packaged meats

Ahn, Changwoo; Stiles, Michael E.

doi:10.1111/j.1365-2672.1990.tb01520.x

Cited by 124 publications

(68 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Spectrum of Activity-The antimicrobial spectrum was determined using a deferred inhibition assay described previously by Ahn and Stiles (23). Briefly, the producer strain was spotted onto TSA plates and incubated 24 h at 30°C.…”

Section: Methodsmentioning

confidence: 99%

Isolation, Structural Characterization, and Properties of Mattacin (Polymyxin M), a Cyclic Peptide Antibiotic Produced byPaenibacillus kobensis M

Martin

Moake

et al. 2003

Journal of Biological Chemistry

103

View full text Add to dashboard Cite

Mattacin is a nonribosomally synthesized, decapeptide antibiotic produced by Paenibacillus kobensis M. The producing strain was isolated from a soil/manure sample and identified using 16 S rRNA sequence homology along with chemical and morphological characterization. An efficient production and isolation procedure was developed to afford pure mattacin. Structure elucidation using a combination of chemical degradation, multidimensional NMR studies (COSY, HMBC, HMQC, ROESY), and mass spectrometric (MALDI MS/MS) analyses showed that mattacin is identical to polymyxin M, an uncommon antibiotic reported previously in certain Bacillus species by Russian investigators. Mattacin (polymyxin M) is cyclic and possesses an amide linkage between the C-terminal threonine and the side chain amino group of the diaminobutyric acid residue at position 4. It contains an (S)-6-methyloctanoic acid moiety attached as an amide at the N-terminal amino group, one D-leucine, six L-␣,␥-diaminobutyric acid, and three L-threonine residues. Transfer NOE experiments on the conformational preferences of mattacin when bound to lipid A and microcalorimetry studies on binding to lipopolysaccharide showed that its behavior was very similar to that observed in previous studies of polymyxin B (a commercial antibiotic), suggesting an identical mechanism of action. It was capable of inhibiting the growth of a wide variety of Gram-positive and Gramnegative bacteria, including several human and plant pathogens with activity comparable with purified polymyxin B. The biosynthesis of mattacin was also examined briefly using transpositional mutagenesis by which 10 production mutants were obtained, revealing a set of genes involved in production.

show abstract

Section: Methodsmentioning

confidence: 99%

Isolation, Structural Characterization, and Properties of Mattacin (Polymyxin M), a Cyclic Peptide Antibiotic Produced byPaenibacillus kobensis M

Martin

Moake

et al. 2003

Journal of Biological Chemistry

103

View full text Add to dashboard Cite

show abstract

“…C. piscicola LV17C was used as a sensitive indicator strain for CbnA, while L. sakei DSM 20017 was used as a sensitive indicator for both CbnA and EntB. Immunity was tested by deferred inhibition assay (Ahn & Stiles, 1990) with C. piscicola LV17A or the EntB producer Enterococcus faecalis ATCC 19433 containing plasmid pCMAP03 (Franz et al, 1999) as producer strains, and strains containing immunity genes as indicators.…”

Section: Methodsmentioning

confidence: 99%

Characterization of the genetic locus responsible for production and immunity of carnobacteriocin A: the immunity gene confers cross-protection to enterocin B The GenBank/EMBL/DDBJ accession number for the sequence reported in this paper is AF207838

et al. 2000

View full text Add to dashboard Cite

Carnobacteriocin A (CbnA) is a regulated bacteriocin produced by Carnobacterium piscicola LV17A that is encoded on a 72 kb plasmid. A 10 0 kb fragment from this plasmid that contained information necessary for bacteriocin production and immunity was cloned and sequenced. Genetic analysis showed the presence of the previously sequenced structural gene for CbnA, as well as genes encoding proteins homologous to dedicated bacteriocin transport proteins and proteins of three-component signal transduction systems. The induction factor (CbnX) was chemically synthesized and induced CbnA production at 10 N11 M or higher in a C. piscicola LV17A culture that had lost the ability to produce bacteriocin as a result of dilution. The gene cbiA for the immunity protein is not located in typical close proximity to the structural gene for CbnA and is encoded in the opposite orientation. CbiA has homology with EniB, the immunity protein for enterocin B that is also encoded in the opposite orientation to the bacteriocin gene. CbiA and EniB cross-protected against the corresponding bacteriocins.

show abstract

“…This paper aims to study potential antimicrobial acid tolerant LAB and protease activities during Green Cacao fermentation in West Sumatra. Strain selected acid tolerant and potential antimicrobial is important to the next further study of antimicrobial Bacteriocin of amino acid structure, physiology and molecular DNA of LAB for new Probiotic and application in food preservative [5,12].…”

Section: Introductionmentioning

confidence: 99%

Antimicrobial Properties and Lactase Activities from Selected Probiotic Lactobacillus brevis Associated With Green Cacao Fermentation in West Sumatra, Indonesia

Syukur¹

2013

J Prob Health

View full text Add to dashboard Cite

Lactase activity is very important enzyme for Lactose Intolerant people. The lactic acid bacteria selected for use as Probiotic bacteria should be able to tolerate many organotoxic or heavy metal toxicities in intestine at least for 90 minute, attach to the epithelium, and grow in the lower intestinal tract before they can start providing any health benefits. The Green varieties of cacao fruits were used for cacao bean fermentation. The cacao bean covers with white pulp containing fructose, e.g. 42 mg/g, glucose 24 mg/g and sucrose 21 mg/g, as carbon source of Lactic Acid Bacteria (LAB). Screening of LAB was carried out after 24-36 h during spontaneous fermentation. This paper aims to find potential LAB resistant acid pH and producing potential antimicrobial and showing high protease/lactase activities. The medium of de Man, Ragosa, and Sharpe (MRS) were used to screen LAB, and 63 colonies were found. The screening of isolates is based on LAB survival growth in acid pH ranges (2.0; 2.5 and 3.0) and body temperature (37°C). For Antimicrobial experiments were used pathogen bacterial E. coli and Salmonela (Unand Collection) as indicator strain. Six isolate were conformed as strong antimicrobial and selected as potential for producing protease (lactase) using specific Triple Sugar Iron Agar (TSIA) medium. The isolate G3 and G6 were selected for further enzyme protease delivered with 2% Skim Milk as a protein subsrate. The results showed, the maximum amount of protease activity potential from isolate G6 in acid pH (3.0) were calculated as 0.0088 and protease activity 1.1795 Unit/mL, while the optimum of protease activity was found at pH (6.0) calculated protease activity 3.150 Unit/mL. This study could explain the possibility of using potential isolate G6 LAB as Probiotic for dairy or food Industry and supplement tablet. There is no report so far concerning this topic and potential isolate G6, with high antimicrobial or wide pH of protease. The study will continue to purify antimicrobial Bacteriocin and amino acid structure determination. The G6 isolate was 95% polymorphism with Lactobacillus brevis.

show abstract

Antibacterial activity of lactic acid bacteria isolated from vacuum‐packaged meats

Cited by 124 publications

References 20 publications

Isolation, Structural Characterization, and Properties of Mattacin (Polymyxin M), a Cyclic Peptide Antibiotic Produced byPaenibacillus kobensis M

Isolation, Structural Characterization, and Properties of Mattacin (Polymyxin M), a Cyclic Peptide Antibiotic Produced byPaenibacillus kobensis M

Characterization of the genetic locus responsible for production and immunity of carnobacteriocin A: the immunity gene confers cross-protection to enterocin B The GenBank/EMBL/DDBJ accession number for the sequence reported in this paper is AF207838

Antimicrobial Properties and Lactase Activities from Selected Probiotic Lactobacillus brevis Associated With Green Cacao Fermentation in West Sumatra, Indonesia

Contact Info

Product

Resources

About