Title
Purification and characterization of thermophilin T, a novel bacteriocin produced by Streptococcus thermophilus ACA-DC 0040
Author
Aktypis, A.
Kalantzopoulos, G.
Huis in't Veld, J.H.J.
ten Brink, B.
Centraal Instituut voor Voedingsonderzoek TNO
Publication year
1998
Abstract
ACA-DC 0040 produced an antimicrobial agent, which was named thermophilin T, active against several lactic acid bacteria strains of different species and food spoilage bacteria, such as Clostridium sporogenes C22/10 and Cl. tyrobutyricum NCDO-1754. The crude antimicrobial compound is sensitive to proteolytic enzymes and α-amylase, heat-stable (100 °C for 30 min), resistant to pH exposure at pH 1-12 and demonstrates a bactericidal mode of action against the sensitive strain Lactococcus cremoris CNRZ-117. The production of bacteriocin was optimized approximately 10-fold in an aerobic fermenter held at constant pH 5.8 and 6.2. Ultrafiltration experiments with culture supernatant fluids containing the bacteriocin, and further estimation of molecular weight with gel filtration chromatography, revealed that bacteriocin in the native form has a molecular weight in excess of 300 kDa. SDS-gel electrophoresis of partially purified thermophilin T showed that bacteriocin activity was associated with a protein band of approximately 2.5 kDa molecular mass.
Subject
Nutrition
Amylase
Bacteriocin
Proteinase
Thermophilin t
Unclassified drug
Bactericidal activity
Clostridium sporogenes
Gel filtration chromatography
Lactococcus
Molecular weight
Nonhuman
Polyacrylamide gel electrophoresis
Protein analysis
Protein purification
Streptococcus thermophilus
Ultrafiltration
Bacteriocins
Cheese
Electrophoresis, Polyacrylamide Gel
Food Microbiology
Hydrogen-Ion Concentration
Lactococcus
Streptococcus
Temperature
Time Factors
Clostridium sporogenes
Lactococcus
Lactococcus lactis subsp. cremoris
Posibacteria
Streptococcus thermophilus
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TNO identifier
234497
ISSN
1364-5072
Source
Journal of Applied Microbiology, 84 (4), 568-576
Document type
article