Isolation of lactic acid bacteria exhibiting high scavenging activity for environmental hydrogen peroxide from fermented foods and its two scavenging enzymes for hydrogen peroxide
Autor: | Sanae Okada, Yasuhiro Hamada, Akira Abe, Shinya Kimata, Junichi Nakagawa, Junichi Satoh, Masataka Uchino, Akio Watanabe, Naoto Tanaka, Kouji Takeda, Takashi Matsumoto, Youichi Niimura, Chiaki Kaneko |
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Rok vydání: | 2016 |
Předmět: |
0301 basic medicine
Applied Microbiology and Biotechnology Microbiology Raphanus 03 medical and health sciences chemistry.chemical_compound Vegetables Food microbiology Amino Acid Sequence Cloning Molecular NADH peroxidase Hydrogen peroxide Pediococcus pentosaceus biology Chemistry food and beverages Oryza Hydrogen Peroxide Catalase biology.organism_classification Culture Media Lactic acid 030104 developmental biology Peroxidases Biochemistry Fermentation Food Microbiology biology.protein Oxidation-Reduction Bacteria Peroxidase |
Zdroj: | The Journal of General and Applied Microbiology. 62:75-82 |
ISSN: | 1349-8037 0022-1260 |
DOI: | 10.2323/jgam.62.75 |
Popis: | To obtain lactic acid bacteria that scavenge environmental hydrogen peroxide, we developed a specialized enrichment medium and successfully isolated Pediococcus pentosaceus Be1 strain from a fermented food. This strain showed vigorous environmental hydrogen peroxide scavenging activity over a wide range of hydrogen peroxide concentrations. High Mn-catalase and NADH peroxidase activities were found in the cell-free extract of the P. pentosaceus Be1 strain, and these two hydrogen peroxide scavenging enzymes were purified from the cell-free extract of the strain. Mn-catalase has been purified from several microorganisms by several researchers, and the NADH peroxidase was first purified from the original strain in this report. After cloning the genes of the Mn-catalase and the NADH peroxidase, the deduced amino acid sequences were compared with those of known related enzymes. |
Databáze: | OpenAIRE |
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