PMID- 35891899
OWN - NLM
STAT- PubMed-not-MEDLINE
LR  - 20220729
IS  - 1880-7291 (Electronic)
IS  - 1344-7882 (Print)
IS  - 1344-7882 (Linking)
VI  - 69
IP  - 2
DP  - 2022
TI  - Acetylated Xylan Degradation by Glycoside Hydrolase Family 10 and 11 Xylanases 
      from the White-rot Fungus Phanerochaete chrysosporium.
PG  - 35-43
LID - 10.5458/jag.jag.JAG-2021_0017 [doi]
AB  - Endo-type xylanases are key enzymes in microbial xylanolytic systems, and 
      xylanases belonging to glycoside hydrolase (GH) families 10 or 11 are the major 
      enzymes degrading xylan in nature. These enzymes have typically been 
      characterized using xylan prepared by alkaline extraction, which removes acetyl 
      sidechains from the substrate, and thus the effect of acetyl groups on xylan 
      degradation remains unclear. Here, we compare the ability of GH10 and 11 
      xylanases, PcXyn10A and PcXyn11B, from the white-rot basidiomycete Phanerochaete 
      chrysosporium to degrade acetylated and deacetylated xylan from various plants. 
      Product quantification revealed that PcXyn10A effectively degraded both 
      acetylated xylan extracted from Arabidopsis thaliana and the deacetylated xylan 
      obtained by alkaline treatment, generating xylooligosaccharides. In contrast, 
      PcXyn11B showed limited activity towards acetyl xylan, but showed significantly 
      increased activity after deacetylation of the xylan. Polysaccharide analysis 
      using carbohydrate gel electrophoresis showed that PcXyn11B generated a broad 
      range of products from native acetylated xylans extracted from birch wood and 
      rice straw, including large residual xylooligosaccharides, while non-acetylated 
      xylan from Japanese cedar was readily degraded into xylooligosaccharides. These 
      results suggest that the degradability of native xylan by GH11 xylanases is 
      highly dependent on the extent of acetyl group substitution. Analysis of 31 
      fungal genomes in the Carbohydrate-Active enZymes database indicated that the 
      presence of GH11 xylanases is correlated to that of carbohydrate esterase (CE) 
      family 1 acetyl xylan esterases (AXEs), while this is not the case for GH10 
      xylanases. These findings may imply co-evolution of GH11 xylanases and CE1 AXEs.
CI  - 2022 by The Japanese Society of Applied Glycoscience.
FAU - Kojima, Keisuke
AU  - Kojima K
AD  - 1 Department of Biomaterial Sciences, The University of Tokyo.
FAU - Sunagawa, Naoki
AU  - Sunagawa N
AD  - 1 Department of Biomaterial Sciences, The University of Tokyo.
FAU - Yoshimi, Yoshihisa
AU  - Yoshimi Y
AD  - 2 Department of Biochemistry, University of Cambridge.
FAU - Tryfona, Theodora
AU  - Tryfona T
AD  - 2 Department of Biochemistry, University of Cambridge.
FAU - Samejima, Masahiro
AU  - Samejima M
AD  - 1 Department of Biomaterial Sciences, The University of Tokyo.
AD  - 3 Faculty of Engineering, Shinshu University.
FAU - Dupree, Paul
AU  - Dupree P
AD  - 2 Department of Biochemistry, University of Cambridge.
FAU - Igarashi, Kiyohiko
AU  - Igarashi K
AD  - 1 Department of Biomaterial Sciences, The University of Tokyo.
LA  - eng
PT  - Journal Article
DEP - 20220525
PL  - Japan
TA  - J Appl Glycosci (1999)
JT  - Journal of applied glycoscience
JID - 101167786
PMC - PMC9276525
OTO - NOTNLM
OT  - Phanerochaete chrysosporium
OT  - acetylated xylan
OT  - biomass utilization
OT  - glycoside hydrolase
OT  - xylanase
EDAT- 2022/07/28 06:00
MHDA- 2022/07/28 06:01
PMCR- 2022/05/25
CRDT- 2022/07/27 02:15
PHST- 2021/12/27 00:00 [received]
PHST- 2022/02/28 00:00 [accepted]
PHST- 2022/07/27 02:15 [entrez]
PHST- 2022/07/28 06:00 [pubmed]
PHST- 2022/07/28 06:01 [medline]
PHST- 2022/05/25 00:00 [pmc-release]
AID - 10.5458/jag.jag.JAG-2021_0017 [doi]
PST - epublish
SO  - J Appl Glycosci (1999). 2022 May 25;69(2):35-43. doi: 
      10.5458/jag.jag.JAG-2021_0017. eCollection 2022.