Structural analysis and biochemical properties of laccase enzymes from two Pediococcus species
Autor: | Juanjo Huesa, Alexei S. Soares, Sara Callejón, Patricia Casino, Sergi Ferrer, Isabel Pardo, Robert E. Collins, Ramon Sendra, Isidoro Olmeda |
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Jazyk: | angličtina |
Rok vydání: | 2021 |
Předmět: |
Bioengineering
Applied Microbiology and Biotechnology Biochemistry 03 medical and health sciences chemistry.chemical_compound Pediococcus Research Articles 030304 developmental biology Laccase chemistry.chemical_classification 0303 health sciences ABTS Bacteria biology 030306 microbiology Chemistry Substrate (chemistry) Pediococcus acidilactici food and beverages biology.organism_classification Lactic acid Enzyme Prokaryotic Cells Oxidation-Reduction TP248.13-248.65 Research Article Biotechnology |
Zdroj: | Microbial Biotechnology, Vol 14, Iss 3, Pp 1026-1043 (2021) Microbial Biotechnology |
ISSN: | 1751-7915 |
Popis: | Summary Prokaryotic laccases are emergent biocatalysts. However, they have not been broadly found and characterized in bacterial organisms, especially in lactic acid bacteria. Recently, a prokaryotic laccase from the lactic acid bacterium Pediococcus acidilactici 5930, which can degrade biogenic amines, was discovered. Thus, our study aimed to shed light on laccases from lactic acid bacteria focusing on two Pediococcus laccases, P. acidilactici 5930 and Pediococcus pentosaceus 4816, which have provided valuable information on their biochemical activities on redox mediators and biogenic amines. Both laccases are able to oxidize canonical substrates as ABTS, ferrocyanide and 2,6‐DMP, and non‐conventional substrates as biogenic amines. With ABTS as a substrate, they prefer an acidic environment and show sigmoidal kinetic activity, and are rather thermostable. Moreover, this study has provided the first structural view of two lactic acid bacteria laccases, revealing new structural features not seen before in other well‐studied laccases, but which seem characteristic for this group of bacteria. We believe that understanding the role of laccases in lactic acid bacteria will have an impact on their biotechnological applications and provide a framework for the development of engineered lactic acid bacteria with enhanced properties. Prokaryotic laccases are emergent biocatalysts. However, they have not been broadly found and characterized in bacterial organisms, especially in lactic acid bacteria. Recently, a prokaryotic laccase from the lactic acid bacterium Pediococcus acidilactici 5930, which can degrade biogenic amines, was discovered. Thus, our study aimed to shed light on laccases from lactic acid bacteria focusing on two Pediococcus laccases, P . acidilactici 5930 and Pediococcus pentosaceus 4816, which have provided valuable information on their biochemical activities on redox mediators and biogenic amines. Both laccases are able to oxidize canonical substrates as ABTS, ferrocyanide and 2,6‐DMP, and non‐conventional substrates as biogenic amines. With ABTS as a substrate, they prefer an acidic environment and show sigmoidal kinetic activity, and are rather thermostable. Moreover, this study has provided the first structural view of two lactic acid bacteria laccases, revealing new structural features not seen before in other well‐studied laccases, but which seem characteristic for this group of bacteria. We believe that understanding the role of laccases in lactic acid bacteria will have an impact on their biotechnological applications and provide a framework for the development of engineered lactic acid bacteria with enhanced properties. |
Databáze: | OpenAIRE |
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