Extracellular ligninases production and lignin degradation by Paenibacillus polymyxa
Ana Edith Ayala Rodríguez, Silvia Valdés Rodríguez, Víctor Enrique Olalde Mathieu, María Arias Padró, Cuauhtémoc Reyes Moreno, Víctor Olalde Portugal
Te invitamos a leer el artículo "Extracellular ligninases production and lignin degradation by Paenibacillus polymyxa" publicado en "The Journal of General and Applied Microbiology", en el que colaboraron la Dra. Silvia Valdés Rodríguez, María Arias Padro y el Dr. Víctor Olalde Portugal de Cinvestav Irapuato.
Autores:
Ana Edith Ayala Rodríguez, Silvia Valdés Rodríguez, Víctor Enrique Olalde Mathieu, María Arias Padró, Cuauhtémoc Reyes Moreno, Víctor Olalde Portugal
Resumen:
Bacteria represent an attractive source for the isolation and identification of potentially useful microorganisms for lignin depolymerization, a process required for the use of agricultural waste. In this work, ten autochthonous bacteria isolated from straw, cow manure, and composts were characterized for potential use in the biodelignification of the waste. A comparison of the ability to degrade lignin and the efficiency of ligninolytic enzymes was performed in bacteria grown in media with lignin as a sole carbon source (LLM, 3.5g/L lignin-alkali) and in complex media supplemented with All-Ban fiber (FLM, 1.5g/L). Bacterial isolates showed different abilities to degrade lignin, they decreased the lignin concentration from 7.6 to 18.6% in LLM and from 11.1 to 44.8% in FLM. They also presented the activity of manganese peroxidase, lignin peroxidases, and laccases with different specific activities. However, strain 26 identified as Paenibacillus polymyxa by sequencing the 16S rRNA showed the highest activity of lignin peroxidase and the ability to degrade efficiently lignocellulose. In addition, P. polymyxa showed the highest potential (desirability ≥ 0.795) related to the best combination of properties to depolymerize lignin from biomass. The results suggest that P. polymyxa has a coordinated lignin degradation system constituted of lignin peroxidase, manganese peroxidase, and laccase enzymes.