PMID- 27770795
OWN - NLM
STAT- MEDLINE
DCOM- 20170623
LR  - 20181113
IS  - 1472-6750 (Electronic)
IS  - 1472-6750 (Linking)
VI  - 16
IP  - 1
DP  - 2016 Oct 22
TI  - Replacement of carbohydrate binding modules improves acetyl xylan esterase 
      activity and its synergistic hydrolysis of different substrates with xylanase.
PG  - 73
LID - 73
AB  - BACKGROUND: Acetylation of the xylan backbone was a major obstacle to enzymatic 
      decomposition. Removal of acetyl groups by acetyl xylan esterases (AXEs) is 
      essential for completely enzymatic hydrolysis of xylan. Appended carbohydrate 
      binding modules (CBMs) can promote the enzymatic deconstruction of plant cell 
      walls by targeting and proximity effects. Fungal acetyl xylan esterases are 
      strictly appended to cellulose-specific CBM1. It is still unclear whether 
      xylan-specific CBMs have a greater advantage than CBM1 in potentiating the 
      activity of fungal deacetylating enzymes and its synergistic hydrolysis of 
      different substrates with xylanase. RESULTS: Three recombinant AXE1s fused with 
      different xylan-specific CBMs, together with wild-type AXE1 with CBM1 and 
      CBM1-deleted mutant AXE1dC, were constructed in this study. The optimal 
      temperature and pH of recombinant AXE1s was 50  degrees C and 8.0 (except AXE1dC-CBM6), 
      respectively. Cellulose-specific CBM1 in AXE1 obviously contributed to its 
      catalytic action against substrates compared with AXE1dC. However, replacement of 
      CBM1 with xylan-specific CBM4-2 significantly enhanced AXE1 thermostability and 
      catalytic activity against soluble substrate 4-methylumbelliferyl acetate. 
      Whereas replacements with xylan-specific CBM6 and CBM22-2 were more effective in 
      enzymatic release of acetic acid from destarched wheat bran, NaClO(2)-treated 
      wheat straw, and water-insoluble wheat arabinoxylan compared to AXE1. Moreover, 
      replacement with CBM6 and CBM22-2 also resulted in higher degree releases of 
      reducing sugar and acetic acid from different substrates when simultaneous 
      hydrolysis with xylanase. A good linear relationship exists between the acetic 
      acid and reducing sugar release. CONCLUSIONS: Our findings suggested that the 
      replacement with CBM6 and CBM22-2 not only significantly improved the catalysis 
      efficiency of AXE1, but also increased its synergistic hydrolysis of different 
      substrates with xylanase, indicating the significance of targeting effect in AXE1 
      catalysis mediated by xylan-specific CBMs.
FAU - Liu, Shiping
AU  - Liu S
AD  - College of Chemical Engineering, Nanjing Forestry University, Nanjing, 210037, 
      Jiangsu, China.
FAU - Ding, Shaojun
AU  - Ding S
AUID- ORCID: 0000-0002-8359-9252
AD  - College of Chemical Engineering, Nanjing Forestry University, Nanjing, 210037, 
      Jiangsu, China. dshaojun@hotmail.com.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20161022
PL  - England
TA  - BMC Biotechnol
JT  - BMC biotechnology
JID - 101088663
RN  - 0 (Carbohydrates)
RN  - 0 (Multienzyme Complexes)
RN  - 0 (Xylans)
RN  - EC 3.1.1.6 (Acetylesterase)
RN  - EC 3.1.1.72 (acetylxylan esterase)
RN  - EC 3.2.1.8 (Endo-1,4-beta Xylanases)
SB  - IM
MH  - Acetylation
MH  - Acetylesterase/*chemistry/*genetics
MH  - Carbohydrates/genetics
MH  - Endo-1,4-beta Xylanases/*chemistry/*genetics
MH  - Enzyme Activation/genetics
MH  - Enzyme Stability
MH  - Gene Regulatory Networks/genetics
MH  - Hydrolysis
MH  - Multienzyme Complexes
MH  - Protein Engineering/*methods
MH  - Substrate Specificity
MH  - Xylans/*chemistry
PMC - PMC5075172
OTO - NOTNLM
OT  - Acetyl xylan esterase
OT  - Carbohydrate-binding module
OT  - Fusion enzyme
OT  - Synergism
OT  - Xylan
OT  - Xylan-specific
EDAT- 2016/10/25 06:00
MHDA- 2017/06/24 06:00
PMCR- 2016/10/22
CRDT- 2016/10/25 06:00
PHST- 2016/06/01 00:00 [received]
PHST- 2016/10/13 00:00 [accepted]
PHST- 2016/10/25 06:00 [pubmed]
PHST- 2017/06/24 06:00 [medline]
PHST- 2016/10/25 06:00 [entrez]
PHST- 2016/10/22 00:00 [pmc-release]
AID - 10.1186/s12896-016-0305-6 [pii]
AID - 305 [pii]
AID - 10.1186/s12896-016-0305-6 [doi]
PST - epublish
SO  - BMC Biotechnol. 2016 Oct 22;16(1):73. doi: 10.1186/s12896-016-0305-6.