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Tropical Journal of Pharmaceutical Research
Pharmacotherapy Group, Faculty of Pharmacy, University of Benin, Benin City, Nigeria
ISSN: 1596-5996
EISSN: 1596-5996
Vol. 14, No. 6, 2015, pp. 989-995
Bioline Code: pr15129
Full paper language: English
Document type: Research Article
Document available free of charge

Tropical Journal of Pharmaceutical Research, Vol. 14, No. 6, 2015, pp. 989-995

 en Purification, Characterization and Antibacterial Mechanism of Bacteriocin from Lactobacillus Acidophilus check for this species in other resources XH1
Zhao, Ruixiang; Duan, Gaili; Yang, Tianyou; Niu, Shengyang & Wang, Ying


Purpose: To carry out the extraction, purification and biological characterization, and assess the antibacterial activity of bacteriocin from Lactobacillus acidophilus check for this species in other resources XH1.
Methods: Chloroform extraction method was used for bacterioc in extraction while characterization of bacteriocin was carried out by flat-dug well agar diffusion assay. The antibacterial mechanisms of bacteriocin were examined by scanning electron microscopy and atomic emission spectroscopy. The molecular weight of l actobacillin XH1 was measured using Tricine-SDS-PAGE electrophoresis.
Results: The bacteriocin (lactobacillin XH1) inhibited Escherichia coli check for this species in other resources , Staphylococcus aureus check for this species in other resources and Bacillus anthracis check for this species in other resources . It showed a wide range of antimicrobial activity at pH 1.0-5.0 while at 37 – 120 °C, it was sensitive to trypsin, pepsin and papain, but insensitive to proteinase K and neutral protease. The intracellular UV-absorbing substances, namely, lactate dehydrogenase macromolecules, K+ and ATP of E. coli, decreased rapidly. The molecular weight of lactobacillin XH1 was approximately 16 kDa.
Conclusion: Lactobacillin XH1 is a broad-spectrum antimicrobial substance that is thermostable. Its antibacterial mechanism on Escherichia coli is similar to that of bacteriocins on Gram-positive bacteria. The agent is a hydrophobic protein with more acidic groups.

Lactobacillus acidophilus; Lactobacillin; Bacteriocin; Purification; Antibacterial mechanism; Atomic emission spectroscopy

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