A family 30 glucurono-xylanase from Bacillus subtilis LC9: Expression, characterization and its application in Chinese bread making

Guo, Yalan; Gao, Zhen; Xu, Jiaxing; Chang, Siyuan; Wu, Bin; He, Bingfang

doi:10.1016/j.ijbiomac.2018.05.143

Cited by 19 publications

(11 citation statements)

References 31 publications

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“…B. subtilis WB800 used as host in the present study is a protease‐deficient strain that was employed to avoid degradation of the target protein by host proteases [13] . Additionally, the strength of the promoter can affect the expression of recombinant proteins in B. subtilis , and strategies such as tandem promoters can prove useful [14] .…”

Section: Resultsmentioning

confidence: 99%

“…Integrated Expression of Dextranase in B. subtilis B. subtilis WB800 used as host in the present study is a protease-deficient strain that was employed to avoid degradation of the target protein by host proteases. [13] Additionally, the strength of the promoter can affect the expression of recombinant proteins in B. subtilis, and strategies such as tandem promoters can prove useful. [14] In the present work, we truncated the 4 -54 bp region in the codon-optimized DEX coding gene which was predicted as a signal peptide by SignalP-5.0 (http://www.cbs.dtu.dk/services/SignalP/).…”

Section: Resultsmentioning

confidence: 99%

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Food‐Grade Expression and Characterization of a Dextranase from Chaetomium gracile Suitable for Sugarcane Juice Clarification

Zhao

Wang

Wei

et al. 2020

Chemistry & Biodiversity

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The microbial production of dextranase using cheap carbon sources is beneficial to solve the economic loss caused by the accumulation of dextran in syrup. A food-grade microbial cell factory was constructed by introducing the dextranase encoding gene DEX from Chaetomium gracile to the chromosome of Bacillus subtilis, and the antibiotic resistance marker gene was subsequently deleted via the Cre/loxP strategy. The dual-promoter system with a sequentially arranged constitutive P43 promoter resulted in an 85 % increase in DEX expression. Under the optimal fermentation conditions of 10 g/L maltose, 15 g/L casein, 1 g/L Na 2 HPO 4 , 1 g/L FeSO 4 and 8 g/ L NaCl, DEX activity was increased from 2.625 to 64.34 U/mL. Recombinant DEX was purified 5.98-fold with a recovery ratio of 26.67 % and specific activity of 3935.02 U/mg. Enzyme activity was optimal at 55°C and pH 5.0 and remained 80.34 % and 71.36 % of the initial activity at 55°C and pH 4.0 after 60 min, respectively. The enzyme possessed high activity in the presence of Co 2 + , while Ag + showed the strongest inhibition ability. The optimal substrate was 20 g/L dextran T-2000. The findings could facilitate the low-cost, large-scale production of food-grade DEX for use in the sugar industry.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Food‐Grade Expression and Characterization of a Dextranase from Chaetomium gracile Suitable for Sugarcane Juice Clarification

Zhao

Wang

Wei

et al. 2020

Chemistry & Biodiversity

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“…Glucuronoxylanases generally do not cleave linear XOs, and only a very high enzyme loadings lead to a weak hydrolysis [9,21,22]. On the contrary, linear XOs were good substrates for xylobiohydrolases HcXyn30A and AaXyn30A, glucuronoxylanases/xylobiohydrolases TcXyn30B, TtXyn30A from Thermothelomyces thermophila, as well as for nonspecific GH30-7 xylanases TlXyn30A, TcXyn30C, TpXyn30A, and GH30-8 xylanases CaXyn30A and CpXyn30A (Figure 5, Tables 1 and 2).…”

Section: Discussionmentioning

confidence: 99%

Catalytic Diversity of GH30 Xylanases

et al. 2021

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Catalytic properties of GH30 xylanases belonging to subfamilies 7 and 8 were compared on glucuronoxylan, modified glucuronoxylans, arabinoxylan, rhodymenan, and xylotetraose. Most of the tested bacterial GH30-8 enzymes are specific glucuronoxylanases (EC 3.2.1.136) requiring for action the presence of free carboxyl group of MeGlcA side residues. These enzymes were not active on arabinoxylan, rhodymenan and xylotetraose, and conversion of MeGlcA to its methyl ester or its reduction to MeGlc led to a remarkable drop in their specific activity. However, some GH30-8 members are nonspecific xylanases effectively hydrolyzing all tested substrates. In terms of catalytic activities, the GH30-7 subfamily is much more diverse. In addition to specific glucuronoxylanases, the GH30-7 subfamily contains nonspecific endoxylanases and predominantly exo-acting enzymes. The activity of GH30-7 specific glucuronoxylanases also depend on the presence of the MeGlcA carboxyl, but not so strictly as in bacterial enzymes. The modification of the carboxyl group of glucuronoxylan had only weak effect on the action of predominantly exo-acting enzymes, as well as nonspecific xylanases. Rhodymenan and xylotetraose were the best substrates for exo-acting enzymes, while arabinoxylan represented hardly degradable substrate for almost all tested GH30-7 enzymes. The results expand current knowledge on the catalytic properties of this relatively novel group of xylanases.

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“…Given these unique features, as well as other beneficial effects on health, e.g. prevention of colon cancer (Aachary et al, 2015), XOS have been incorporated in several functional foods and animal feed, nutraceuticals and cosmetics (Moure et al, 2006;Ayyappan et al, 2016;Gao et al, 2017;Gupta and Mehra, 2017;Abasubong et al, 2018;Guo et al, 2018;Ferrão et al, 2018;Zhang et al, 2018). Furthermore, XOS are also reported to present other beneficial effects, namely in the prevention of diabetes (Yang et al, 2015), neurotoxicity (Krishna et al, 2015) and colon inflammation (Femia et al, 2010;Lin et al, 2016), which have gained attention from the medical and pharmaceutical industries (Fig.…”

Section: Biological Propertiesmentioning

confidence: 99%

From lignocellulosic residues to market: Production and commercial potential of xylooligosaccharides

Amorim

Silvério

Prather

et al. 2019

Biotechnology Advances

205

108

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The updated definition of prebiotic expands the range of potential applications in which emerging xylooligosaccharides (XOS) can be used. It has been demonstrated that XOS exhibit prebiotic effects at lower amounts compared to others, making them competitively priced prebiotics. As a result, the industry is focused on developing alternative approaches to improve processes efficiency that can meet the increasing demand while reducing costs. Recent advances have been made towards greener and more efficient processes, by applying process integration strategies to produce XOS from costless lignocellulosic residues and using genetic engineering to create microorganisms that convert these residues to XOS. In addition, collecting more in vivo data on their performance will be key to achieve regulatory claims, greatly increasing XOS commercial value.

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A family 30 glucurono-xylanase from Bacillus subtilis LC9: Expression, characterization and its application in Chinese bread making

Cited by 19 publications

References 31 publications

Food‐Grade Expression and Characterization of a Dextranase from Chaetomium gracile Suitable for Sugarcane Juice Clarification

Food‐Grade Expression and Characterization of a Dextranase from Chaetomium gracile Suitable for Sugarcane Juice Clarification

Catalytic Diversity of GH30 Xylanases

From lignocellulosic residues to market: Production and commercial potential of xylooligosaccharides

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