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MOESM1 of A novel GH10 xylanase from Penicillium sp. accelerates saccharification of alkaline-pretreated bagasse by an enzyme from recombinant Trichoderma reesei expressing Aspergillus β-glucosidase

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posted on 2017-11-21, 05:00 authored by Nozomu Shibata, Mari Suetsugu, Hiroshi Kakeshita, Kazuaki Igarashi, Hiroshi Hagihara, Yasushi Takimura
Additional file 1: Figure S1. Multiple alignments and phygogenetic tree of PspXyn10, PspXyn10 orthologs and TrXyn3. (a) Multiple alignments of the PspXyn10, PspXyn10 orthologs and TrXyn3. The amino acid sequence of PspXyn10 was compared with those of endo-1,4-beta-xylanase from Penicillium brasilianum (OOQ87260), endo-1,4-beta-xylanase D from Penicillium subrubescens (OKO90312), endo-1,4-beta-xylanase from Rasamsonia emersonii CBS 393.64 (XP_013330999), hypothetical protein PENANT_c053G02808 from Penicillium antarcticum (OQD79351), endo-1,4-beta-xylanase Xyl10A from Talaromyces cellulolyticus (GAM37231) and TrXyn3 from Trichoderma reesei (BAA89465) by multiple alignment. The alignment was created using ClustalW2 on Genetyx Version 12 software (Genetyx). Amino acid numbers are shown on the left and right. Black boxes indicate invariant residues. Gray boxes indicate the residues conserved in more than half of aligned sequences. (b) Phylogenetic tree of the PspXyn10, PspXyn10 orthologs and TrXyn3. Phylogenetic tree of the amino acid sequences were created using the NJ method under 1000 times bootstrap conditions using Genetyx Version 12 software (Genetyx).

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New Energy and Industrial Technology Development Organization

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