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Analytical pyrolysis of acid precipitable polymeric lignin (APPL) from the solid-state fermentation of wheat biomass with Streptomyces ipomoeae

AutorArias, María E.; Blánquez, Alba; Hernández. Manuel; Rodríguez, Juana; González-Pérez, José Antonio ; Jiménez Morillo, N. T. ; González-Vila, Francisco Javier
Fecha de publicación2-nov-2016
EditorSociedad Española de Cromatografía y Técnicas Afines
CitaciónAdvances in Chromatography and Related Techniques: Book of Absracts pág. 212 (2016)
ResumenStreptomycetes produce enzymes able to depolymerize lignin in solid-state fermentation (SFF) conditions and therefore are of interest for biopulping purposes. In recent studies a thermostable lacease (SiIA) produced by Streptomyces ipomoeae CECT 3341 presenting both physico-chemical and structural characteristics usually uncommon among microbial laceases was isolated that opened up the biotechnological interest of this enzyme i.e. high resistance to alkaline conditions and to high concentrations of sodium chloride [1]. For this study, the wild strain (SiIA) and a laccase-negative mutant (SiIA-) obtained through gene disruption were grown on wheat straw as substrate under SSF conditions. In addition, a non-inoculated substrate was used as control. After 7 days of incubation the APPL extracted with water were quantified and studied by Py-GC/MS at moderate temperature (350 oC). The APPL yield was 12 times and 6 times higher for the wild-type strain (SiIA) than for the control and mutant strain (SiIA-), respectively. Under the chromatographic conditions used [i.e. 2], the chromatograms could be divided in three parts where main biogenic compounds elute; a first part (min 2-5) dominated by polysaccharide-derived compounds, from min 5-14 lignin-derived compounds and from min 14 to the end of the chromatogram lipid compounds including fatty acids (FA14, 16 & 18), long chain alkanes (C27-C33) and sterols. Polysaccharides were the main pyrolysis compounds detected in the control (89.0 %) and SiIA- mutant strain (60.9 %) APPLs, being a minor component in the SilA strain (5.4 %) that was dominated by lignin derived compounds (77.3 %). The pyrolysates from the wild SilA and SilA- strains present a similar distribution of lignin subunits (H, G, S) and an equivalent degree of oxidation. In control APPL there was an absence of H and dominance of G type subunits and higher relative abundance of non-oxidized alkyl phenols. However, a shortening of lignin propyl side chains and a higher relative abundance of oxidized moieties (ketones and acids) where the predominant features of SilA and SiIA- APPLs. This result indicates the occurrence of oxidative Ca-C~ cleavage of propyl side chains in lignin by both strains. In conclusion, S. ipomoeae has high lignin solubilizing activity in SSF conditions. Although lacease is the main enzyme involved, other oxidative enzymes are likely to contribute. The behaviour of the laccase-negative mutant (SilA-) could indicate the presence of alternative oxidative enzymes which affects/modify the lignin in a similar manner than lacease but with lower efficiency. [1] J.M. Molina Guijarro et al., Int. Microbiol. 12 (2009) 13-21 [2] J.A. González-Pérez, N.T. Jiménez-Morillo, J.M. de La Rosa Arranz, G. Almendros, F.J. González-Vila, J. Sci. Food Agric. 96 (2016) 948-953
DescripciónVI Reunión Científica de la Sociedad Española de Cromatografía y Técnicas Afines SECyTA, 2-4 Noviembre (2016) Sevilla, España
Versión del editorhttp://digital.csic.es/handle/10261/139608
Identificadoresuri: http://hdl.handle.net/10261/139608
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