Characterization of Clostridium thermocellum (B8) secretome and purified cellulosomes for lignocellulosic biomass degradation

Publication date: Available online 8 November 2016 Source:Enzyme and Microbial Technology Author(s): Karen O. Osiro, Brenda R. de Camargo, Rachel Satomi, Pedro Ricardo V. Hamann, Jéssica Pinheiro Silva, Marcelo Valle de Sousa, Betania F. Quirino, Elaine N. Aquino, Carlos R. Felix, André Melro Murad, Eliane F. Noronha The main goal of the present study was a complete proteomic characterization of total proteins eluted from residual substrate-bound proteins (RSBP), and cellulosomes secreted by Clostridium thermocellum B8 during growth in the presence of microcrystalline cellulose as a carbon source. The second goal was to evaluate their potential use as enzymatic blends for hydrolyzing agro-industrial residues to produce fermentable sugars. Protein identification through LC-MS/MS mass spectrometry showed that the RSBP sample, in addition to cellulosomal proteins, contains a wide variety of proteins, including those without a well-characterized role in plant cell wall degradation. The RSBP subsample defined as purified cellulosomes (PC) consists mainly of glycoside hydrolases grouped in families 5, 8, 9, 10 and 48. Dynamic light scattering, DLS, analysis of PC resulted in two protein peaks (pi1 and pi2) presenting molecular masses in agreement with those previously described for cellulosomes and polycellulosomes. These peaks weren’t detected after PC treatment with 1.0% Tween. PC and RSBP presented maximal activities at temperatures ranging from 60° to 70°C an...
Source: Enzyme and Microbial Technology - Category: Biotechnology Source Type: research
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