Efficient secretion of xylanase in Escherichia coli for production of prebiotic xylooligosaccharides. (1st June 2022)
- Record Type:
- Journal Article
- Title:
- Efficient secretion of xylanase in Escherichia coli for production of prebiotic xylooligosaccharides. (1st June 2022)
- Main Title:
- Efficient secretion of xylanase in Escherichia coli for production of prebiotic xylooligosaccharides
- Authors:
- Wang, Jiapeng
Zhang, Susu
Li, Chunhai
Liu, Xinli
Xu, Zhenshang
Wang, Ting - Abstract:
- Abstract: The N-terminal 20 amino acid of Lactobacillus amylovorus feruloyl esterase (N20) was used as a signal peptide for fusion expression with a novel xylanase Xyl derived from Bacillus paralicheniformis . Results showed that N20-Xyl could be effectively secreted out of E. coli BL21(DE3) cells. Enzymatic characterization indicated that Xyl and N20-Xyl exhibited similar properties with the optimal pH of 8.0 and temperature of 50 °C. Furthermore, xylooligosaccharides were prepared through simultaneous xylanase secretion and xylan degradation by using E. coli . The final extracellular reducing sugar content reached 8.79 ± 0.10 g/L based on 40 g/L xylan, and the main products were xylobiose, xylotriose, and xylotetraose. Moreover, it was found that Levilactobacillus brevis 217-168, Enterococcus faecium 217-169, Pediococcus acidilactici 217-112, and Weissella confusa 217-162 could efficiently utilize these xylooligosaccharides for growth. Therefore, this study provided a method for the production of prebiotic xylooligosaccharides via simultaneous fermentation by using E. coli . Highlights: A novel xylanase Xyl derived from B. paralicheniformis was expressed in E. coli. The N20 of Lactobacillus amylovorus feruloyl esterase was used as signal peptide. Xylooligosaccharides were prepared via simultaneous N20-Xyl secretion and xylan degradation. The main products were xylobiose, xylotriose, and xylotetraose. The produced xylooligosaccharides could be used as prebiotic for LABAbstract: The N-terminal 20 amino acid of Lactobacillus amylovorus feruloyl esterase (N20) was used as a signal peptide for fusion expression with a novel xylanase Xyl derived from Bacillus paralicheniformis . Results showed that N20-Xyl could be effectively secreted out of E. coli BL21(DE3) cells. Enzymatic characterization indicated that Xyl and N20-Xyl exhibited similar properties with the optimal pH of 8.0 and temperature of 50 °C. Furthermore, xylooligosaccharides were prepared through simultaneous xylanase secretion and xylan degradation by using E. coli . The final extracellular reducing sugar content reached 8.79 ± 0.10 g/L based on 40 g/L xylan, and the main products were xylobiose, xylotriose, and xylotetraose. Moreover, it was found that Levilactobacillus brevis 217-168, Enterococcus faecium 217-169, Pediococcus acidilactici 217-112, and Weissella confusa 217-162 could efficiently utilize these xylooligosaccharides for growth. Therefore, this study provided a method for the production of prebiotic xylooligosaccharides via simultaneous fermentation by using E. coli . Highlights: A novel xylanase Xyl derived from B. paralicheniformis was expressed in E. coli. The N20 of Lactobacillus amylovorus feruloyl esterase was used as signal peptide. Xylooligosaccharides were prepared via simultaneous N20-Xyl secretion and xylan degradation. The main products were xylobiose, xylotriose, and xylotetraose. The produced xylooligosaccharides could be used as prebiotic for LAB strains. … (more)
- Is Part Of:
- Lebensmittel-Wissenschaft + Technologie =. Volume 162(2022)
- Journal:
- Lebensmittel-Wissenschaft + Technologie =
- Issue:
- Volume 162(2022)
- Issue Display:
- Volume 162, Issue 2022 (2022)
- Year:
- 2022
- Volume:
- 162
- Issue:
- 2022
- Issue Sort Value:
- 2022-0162-2022-0000
- Page Start:
- Page End:
- Publication Date:
- 2022-06-01
- Subjects:
- Xylanase -- Atyptical signal peptide -- Secretory expression -- Escherichia coli -- Xylooligosaccharides
Food industry and trade -- Periodicals
Food -- Composition -- Periodicals
Microbiology -- Periodicals
Nutrition -- Periodicals
664.005 - Journal URLs:
- http://www.sciencedirect.com/science/journal/00236438 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.lwt.2022.113481 ↗
- Languages:
- English
- ISSNs:
- 0023-6438
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3983.070000
British Library DSC - BLDSS-3PM
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- 21896.xml