Isolation, purification, characterization, mode of action, and amino acid sequence of bifidocin B and lactococcin R
Başlık çevirisi mevcut değil.
- Tez No: 400650
- Danışmanlar: PROF. DR. MICHEAL G. JOHNSON
- Tez Türü: Doktora
- Konular: Mikrobiyoloji, Microbiology
- Anahtar Kelimeler: Belirtilmemiş.
- Yıl: 1998
- Dil: İngilizce
- Üniversite: University of Arkansas
- Enstitü: Yurtdışı Enstitü
- Ana Bilim Dalı: Belirtilmemiş.
- Bilim Dalı: Belirtilmemiş.
- Sayfa Sayısı: 100
Özet
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Özet (Çeviri)
Ten dairy products and ten fresh vegetables products were researched for bacteria that produce bacteriocins. Also, Bifidobacteria species from ATCC (11863, 29521), and NCFB (1453, 1454, 1455) were examined for possible production of bacteriocins. Only Bifidobacterium bifidum NCFB 1454 and a radish isolate, Lactococcus lactis subsp. cremoris R, produced bacteriocins designated bifidocin B (BB) and lactococcin R (LR), respectively. BB and LR were sensitive to some proteolytic enzymes tested. Both bacteriocins were resistant to organic solvents, pH, or heating (90-121°C) and were active against Listeria, Enterococcus, Bacillus, Micrococcus, LacwbaciUus, Leuconostoc and Pediococcus species tested. Also, LR was inhibitory to Clostridium, Staphylococcus and Streptococcus species. Their activity (1,280 AU/ml) on L. monocytogenes was bactericidal, reducing colony counts by 99.9% in 3-h. BB and LR were purified to homogeneity by a simple purification procedure including freeze-drying, Micro-Cel adsorption/desorpcion and cation«exchangeT chromatography. These bacteriocins caused sensitive cells to lose intracellular K+ ions, UV-absorbing materials and become more permeable to ONPG. Bacteriocins adsorbed to the gram-positive bacteria but not gram-negative bacteria tested. Several salts inhibited their binding. Also, addition of purified lipoteichoic acid to sensitive cells and methanol:chloroform plus hot 20% TCA treatment on cell wall preparations blocked bacteriocin adsorption. The N-terminal amino acid sequence of BB yielded
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