Functional Expression and Characterization of Acetyl Xylan Esterases CE Family 7 from Lactobacillus antri and Bacillus halodurans
| العنوان: | Functional Expression and Characterization of Acetyl Xylan Esterases CE Family 7 from Lactobacillus antri and Bacillus halodurans |
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| المؤلفون: | Min-Jeong Kim, Heeji Shin, Gyeong-Hwa Nam, Jeong-Rok Song, Tae-Jip Kim, Myoung-Uoon Jang |
| المصدر: | Journal of Microbiology and Biotechnology. 30:155-162 |
| بيانات النشر: | Journal of Microbiology and Biotechnology, 2020. |
| سنة النشر: | 2020 |
| مصطلحات موضوعية: | chemistry.chemical_classification, biology, Chemistry, food and beverages, General Medicine, biology.organism_classification, medicine.disease_cause, Applied Microbiology and Biotechnology, Xylan, Esterase, Enzyme, Biochemistry, medicine, Xylanase, Bacillus halodurans, Escherichia coli, Thermotoga neapolitana, Biotechnology, Deacetylase activity |
| الوصف: | Acetyl xylan esterase (AXE; E.C. 3.1.1.72) 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 50°C, 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. |
| تدمد: | 1738-8872 1017-7825 |
| DOI: | 10.4014/jmb.2001.01004 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_________::a43b49e7f41b6281103538180d95bbe7 https://doi.org/10.4014/jmb.2001.01004 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi...........a43b49e7f41b6281103538180d95bbe7 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 17388872 10177825 |
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| DOI: | 10.4014/jmb.2001.01004 |