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Table 3 Comparison of Xyn10A with known enzymes with bifunctional xylanase/cellulase activities

From: A novel thermostable GH10 xylanase with activities on a wide variety of cellulosic substrates from a xylanolytic Bacillus strain exhibiting significant synergy with commercial Celluclast 1.5 L in pretreated corn stover hydrolysis

Properties Main xylanase activity Main cellulase activity
Proteinsa: XynA Cex MFC XynT-6 Mxyn10 CbXyn10C Xyl10A rBhcell-xyl CtCel5E CbGH5 EG I-CD EG I
Sourceb This study C. fimi A. crossean B. stearothermophilus Demequina sp. C. bescii S. olivaceoviridis B. halodurans C. thermocellum Chryseobacterium sp. T. reesei T. reesei
Length (aa), identityc 408, – 312, 18% 395, 30% 107, 14% 471, 14% 339, 17% 453, 17% 561, 11% 403, 9% 576, 11% 404, 8% –, –
Domain architecture GH10 GH10 GH10 GH10 GH10 + CBM2 GH10 GH10 GH5 + CBM12 GH5 GH5 GH7 GH7
Xylanase activityd
 Activity for
  Xylans Yes Yes Yes Yes Yes Yes Yes Yes Yes Yes Yes Yes
  pNPX Yes Yes Yes Yes No No
  X3–X6 Yes Yes Yes
  X2 No No No No
Cellulase activityd
 Activity for
  CMC Yes Yes Yes Yes Yes Yes Yes Yes Yes Yes
  MCC Yes No Yes Yes Yes No Yes
  G3–G6 Yes Yes Yes
  G2 Yes No No No
  pNPC Yes Yes Yes Yes No Yes Yes Yes
  pNPG Yes Yes Yes Yes No Yes Yes No
References This study [8] [9] [10, 11] [12] [13] [29] [31] [32] [33] [34] [35, 36]
  1. MCC microcrystalline cellulose substrates
  2. aThe GenBank accession numbers for related enzymes are: XynA (MK064556), Cex (2HIS_A), MFC (ACC86116), XynT-6 (P40943), Mxyn10 (ACM41799), CbXyn10C (5OFL_A), Xyl10A (WP_003978188), rBhcell-xyl (ALL28250), CtCel5E (4U3A_B), CbGH5 (ANQ80467), and EG I-CD (AAA34212). EG I has only been partial sequenced, so full amino sequence is not available
  3. bSource: C. fimi, Cellulomonas fimi. A. crossean, Ampullaria crossean. B. stearothermophilus, Bacillus stearothermophilus T-6. C. bescii, Caldicellulosiruptor bescii DSM 6725. S. olivaceoviridis, Streptomyces olivaceoviridis E-86. B. halodurans, Bacillus halodurans TSLV1. C. thermocellum, Clostridium thermocellum. T. reesei, Trichoderma reesei
  4. cThe values for amino acid sequence identity were obtained using CLUSTAL W (https://www.genome.jp/tools-bin/clustalw)
  5. d –: the information is not available in the reference