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Original Article



Purification and characterization of plantaricin K-2 from Lactiplantibacillus plantarum K-2 isolated from locally fermented cabbage

Khonsuluv A. Sohibnazarova, Muzaffar Muminov, Iskandar Yakubov, Azimjon Abdunabiev, Shakhnoza Umarova, Jakhongirbek Gulomov, Yulduz Abduvokhidova, Urmonalieva Shakhlo, Ibragimova Shakhnoza, Akmal M. Asrorov, Fazliddin Kobilov, Bozorov Soyibjon, Dilbar Dalimova, Shakhlo Miralimova.



Abstract
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Bacteriocins are considered to be safe food preservatives, which have great potential to replace antibiotics due to their high efficacy against multidrug-resistant pathogens. In this work, the bacteriocin plantaricin K-2 was purified by three-stage purification – cation exchange chromatography, hydrophobic chromatography, and reversed-phase high-performance liquid chromatography with the purpose of establishing its practical value. The molecular weight of the peptide was 3937.05 Da by mass spectrometric analysis (Quadrupole Time-of-Flight mass spectrometry). The bacteriocin plantaricin K-2 was identified to belong to Class IIa and its physico-biochemical parameters were determined, and the 16S ribosomal DNA sequence analysis confirmed that the strain synthesizing it was Lactiplantibacillus plantarum. Plantaricin K-2 did not show antimicrobial activity when treated with proteases, but showed high thermal stability at high temperatures (121°C, 30 min). Production of plantaricin K-2 reached 6400 AU/mL during the stationary growth phase of L. plantarum K-2 cultivated in MRS at 37°C for 48 h. Although plantaricin K-2 is usually classified as a narrow-spectrum Class IIa bacteriocin, it showed relatively broad activity against food microbes and pathogenic microorganisms. The results of the study show that plantaricin K-2, belonging to a Class IIa bacteriocin, is a promising natural and safe biological object that could be used for preserving food as an antibiotic-resistant means in clinical applications.

Key words: bacteriocins, plantaricin, Lactiplantibacillus plantarum, antimicrobial peptides, food spoilage







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