PMID- 32671051
OWN - NLM
STAT- PubMed-not-MEDLINE
LR  - 20200928
IS  - 2296-4185 (Print)
IS  - 2296-4185 (Electronic)
IS  - 2296-4185 (Linking)
VI  - 8
DP  - 2020
TI  - Functional Validation of Two Fungal Subfamilies in Carbohydrate Esterase Family 1 
      by Biochemical Characterization of Esterases From Uncharacterized Branches.
PG  - 694
LID - 10.3389/fbioe.2020.00694 [doi]
LID - 694
AB  - The fungal members of Carbohydrate Esterase family 1 (CE1) from the CAZy database 
      include both acetyl xylan esterases (AXEs) and feruloyl esterases (FAEs). AXEs 
      and FAEs are essential auxiliary enzymes to unlock the full potential of 
      feedstock. They are being used in many biotechnology applications including food 
      and feed, pulp and paper, and biomass valorization. AXEs catalyze the hydrolysis 
      of acetyl group from xylan, while FAEs release ferulic and other hydroxycinnamic 
      acids from xylan and pectin. Previously, we reported a phylogenetic analysis for 
      the fungal members of CE1, establishing five subfamilies (CE1_SF1-SF5). 
      Currently, the characterized AXEs are in the subfamily CE1_SF1, whereas CE1_SF2 
      contains mainly characterized FAEs. These two subfamilies are more related to 
      each other than to the other subfamilies and are predicted to have evolved from a 
      common ancestor, but target substrates with a different molecular structure. In 
      this study, four ascomycete enzymes from CE1_SF1 and SF2 were heterologously 
      produced in Pichia pastoris and characterized with respect to their biochemical 
      properties and substrate preference toward different model and plant biomass 
      substrates. The selected enzymes from CE1_SF1 only exhibited AXE activity, 
      whereas the one from CE1_SF2 possessed dual FAE/AXE activity. This dual activity 
      enzyme also showed broad substrate specificity toward model substrates for FAE 
      activity and efficiently released both acetic acid and ferulic acid ( approximately 50%) from 
      wheat arabinoxylan and wheat bran which was pre-treated with a commercial 
      xylanase. These fungal AXEs and FAEs also showed promising biochemical 
      properties, e.g., high stability over a wide pH range and retaining more than 80% 
      of their residual activity at pH 6.0-9.0. These newly characterized fungal AXEs 
      and FAEs from CE1 have high potential for biotechnological applications. In 
      particular as an additional ingredient for enzyme cocktails to remove the 
      ester-linked decorations which enables access for the backbone degrading enzymes. 
      Among these novel enzymes, the dual FAE/AXE activity enzyme also supports the 
      evolutionary relationship of CE1_SF1 and SF2.
CI  - Copyright (c) 2020 Li, Griffin, Langeveld, Frommhagen, Underlin, Kabel, de Vries 
      and Dilokpimol.
FAU - Li, Xinxin
AU  - Li X
AD  - Fungal Physiology, Westerdijk Fungal Biodiversity Institute, Fungal Molecular 
      Physiology, Utrecht University, Utrecht, Netherlands.
FAU - Griffin, Kelli
AU  - Griffin K
AD  - Fungal Physiology, Westerdijk Fungal Biodiversity Institute, Fungal Molecular 
      Physiology, Utrecht University, Utrecht, Netherlands.
FAU - Langeveld, Sandra
AU  - Langeveld S
AD  - Fungal Physiology, Westerdijk Fungal Biodiversity Institute, Fungal Molecular 
      Physiology, Utrecht University, Utrecht, Netherlands.
FAU - Frommhagen, Matthias
AU  - Frommhagen M
AD  - Laboratory of Food Chemistry, Wageningen University & Research, Wageningen, 
      Netherlands.
FAU - Underlin, Emilie N
AU  - Underlin EN
AD  - Laboratory of Food Chemistry, Wageningen University & Research, Wageningen, 
      Netherlands.
AD  - Department of Chemistry, Technical University of Denmark, Lyngby, Denmark.
FAU - Kabel, Mirjam A
AU  - Kabel MA
AD  - Laboratory of Food Chemistry, Wageningen University & Research, Wageningen, 
      Netherlands.
FAU - de Vries, Ronald P
AU  - de Vries RP
AD  - Fungal Physiology, Westerdijk Fungal Biodiversity Institute, Fungal Molecular 
      Physiology, Utrecht University, Utrecht, Netherlands.
FAU - Dilokpimol, Adiphol
AU  - Dilokpimol A
AD  - Fungal Physiology, Westerdijk Fungal Biodiversity Institute, Fungal Molecular 
      Physiology, Utrecht University, Utrecht, Netherlands.
LA  - eng
PT  - Journal Article
DEP - 20200626
PL  - Switzerland
TA  - Front Bioeng Biotechnol
JT  - Frontiers in bioengineering and biotechnology
JID - 101632513
PMC - PMC7332973
OTO - NOTNLM
OT  - CAZy subfamilies
OT  - acetyl xylan esterase
OT  - carbohydrate esterase
OT  - ferulic acid
OT  - feruloyl esterase
OT  - fungi
OT  - plant biomass degradation
EDAT- 2020/07/17 06:00
MHDA- 2020/07/17 06:01
PMCR- 2020/01/01
CRDT- 2020/07/17 06:00
PHST- 2020/03/13 00:00 [received]
PHST- 2020/06/03 00:00 [accepted]
PHST- 2020/07/17 06:00 [entrez]
PHST- 2020/07/17 06:00 [pubmed]
PHST- 2020/07/17 06:01 [medline]
PHST- 2020/01/01 00:00 [pmc-release]
AID - 10.3389/fbioe.2020.00694 [doi]
PST - epublish
SO  - Front Bioeng Biotechnol. 2020 Jun 26;8:694. doi: 10.3389/fbioe.2020.00694. 
      eCollection 2020.