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• W129553657 abstract "In this study, eight Lactic Acid Bacteria (LAB) isolated from Ikan Rebus(steamed fish) were screened for bacteriocin production using spot-on-lawn, flipstreak plate and agar-well diffusion methods. Seven out of eight LAB isolates wereconfirmed to be able to produce bacteriocin. However, only the highest bacteriocinproducer, RW 18, was selected for further studies. The carbohydrate fermentationpattern of RW 18 isolate exhibited 83.4% similarity to Laetoeoeeus laetis subsp.laetis by the API CHL 50 test kit and hence designated as Le. laetis subsp. laetisRW 18. Bacteriocin production by Le. laetis subsp. laetis RW 18 was detected duringmid log phase and reached a maximum level of 200 Au/ml during the earlystationary phase. Bacteriocin of Le. laetis subsp. laetis RW 18 was able to toleratewide pH range (pH 3.0 to pH 7.0) but it was unstable when the incubationtemperature was increased above 90°C at pH 6.5. The bacteriocin demonstrated a broad-spectrum antagonistic activity against gram-positive bacteria includingListeria monocytogenes, Enterococcus jaecalis, Enterococcus jaecium, Pediococcusacidilactici and Lactobacillus pentosus but it was not active against gram-negativebacteria. Results obtained in the study on the effect of hydrolytic enzymes indicatedthat the bacteriocin was a proteinaceous compound and most likely to containlipolytic and glycolytic moieties. The bacteriocin was purified to homogeneity by aprocedure involving 0-60% ammonium sulfate precipitation, cation-exchangechromatography and gel filtration chromatography with a yield of 0.9% andpurification fold of 3210. The molecular mass of purified bacteriocin was estimatedto be 3.9 kDa and 4.0 kDa using the Tricine sodium dodecyl sulphatepolyacrylamidegel electrophoresis (Tricine SDS-PAGE) and gel filtrationchromatography respectively. The isoelectric point of the purified bacteriocin wasestimated to be more than 9.30 by Isoelectric focusing-PAGE and hence itdemonstrated a strong basic (cationic) characteristic. The stability of purifiedbacteriocin could be improved by adding either BSA or glycerol. A 100%increment of relative activity was obtained by adding 10-40 µg of BSA, whereas ahighest relative activity of 300% was achieved when 10% and 15% of glycerolwere added respectively. The purified bacteriocins have less antagonistic activitycompared to crude bacteriocins. Partially purified bacteriocin pooled from theResource-S chromatography exhibited enhanced biological activity against LAB,whereas reduced biological activity was observed for purified bacteriocin pooledafter superose- 12 gel filtration chromatography. NisA gene was detected in Lc. lactissubsp. lactis RW 18 by PCR amplification using a pair of nisA structural genespecific primers. The RAPD-PCR fingerprinting analysis revealed that Lc. lactis subsp. lac tis RW 18 was genotypically different from nisin producer, Le. lactis subsp.lactis ATCC 11454. Nevertheless, evidence obtained in this study could not provethat the bacteriocin produced by Le. lactis subsp. lactis RW18 was nisin, regardlessof the fact that nisA gene was detected in the Le. lactis subsp. lactis RW18. Theactual amino acid sequence of the purified bacteriocin has to be determined in orderto ascertain whether bacteriocin produced by Le. lactis subsp. lactis RW 18 is nisin." @default.
• W129553657 created "2016-06-24" @default.
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• W129553657 date "2002-01-01" @default.
• W129553657 modified "2023-09-27" @default.
• W129553657 title "Purification and Characterisation of Bacteriocin Produced by Lactococcus Lactis Subsp. Lactis RW18 Isolated From Steamed Fish (Rastrelliger Sp.)" @default.
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