2020 ; Vol.30-2: 155~162
|Author||Min-Jeong Kim, Myoung-Uoon Jang, Gyeong-Hwa Nam, Heeji Shin, Jeong-Rok Song, Tae-Jip Kim|
|Place of duty||Division of Animal, Horticultural and Food Sciences, Graduate School of Chungbuk National University, Cheongju 28644, Republic of Korea|
|Title||Functional Expression and Characterization of Acetyl Xylan Esterases CE Family 7 from Lactobacillus antri and Bacillus halodurans|
J. Microbiol. Biotechnol.2020 ;
|Abstract||Acetyl xylan esterase (AXE; E.C. 220.127.116.11) is one of the accessory enzymes for xylan
degradation, which can remove the terminal acetate residues from xylan polymers. In this
study, two genes encoding putative AXEs (LaAXE and BhAXE) were cloned from Lactobacillus
antri DSM 16041 and Bacillus halodurans C-125, and constitutively expressed in Escherichia coli.
They possess considerable activities towards various substrates such as p-nitrophenyl acetate,
4-methylumbelliferyl acetate, glucose pentaacetate, and 7-amino cephalosporanic acid. LaAXE
and BhAXE showed the highest activities at pH 7.0 and 8.0 at 50oC, respectively. These
enzymes are AXE members of carbohydrate esterase (CE) family 7 with the cephalosporine-C
deacetylase activity for the production of antibiotics precursors. The simultaneous treatment
of LaAXE with Thermotoga neapolitana β-xylanase showed 1.44-fold higher synergistic
degradation of beechwood xylan than the single treatment of xylanase, whereas BhAXE
showed no significant synergism. It was suggested that LaAXE can deacetylate beechwood
xylan and enhance the successive accessibility of xylanase towards the resulting substrates.
The novel LaAXE originated from a lactic acid bacterium will be utilized for the enzymatic
production of D-xylose and xylooligosaccharides.|
|Key_word||Acetyl xylan esterases, carbohydrate esterase (CE) family 7, synergistic xylan degradation, Lactobacillus antri, Bacillus halodurans|
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