Production of xylitol by expressing xylitol dehydrogenase and alcohol dehydrogenase from Gluconobacter thailandicus and co-biotransformation of whole cells

Zhang, Huanhuan; Yun, Jimmy; Zabed, Hossain M.; Yang, Miaomiao; Zhang, Guoyan; Qi, Yilin; Guo, Qi; Qi, Xianghui

doi:10.1016/j.biortech.2018.02.095

Cited by 34 publications

(9 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…However, the optimum pH and temperature for the oxidation activity of the NAD-dependent xylitol dehydrogenase 2 were observed to be slightly higher than those reported in earlier studies for the same reaction of xylitol dehydrogenases isolated from different strains of G. oxydans. The reason for this variation in the optimum pH and temperature for xylitol dehydrogenase activity could be due to different source strains from which the enzymes were isolated.…”

Section: Discussionmentioning

confidence: 99%

“…With regard to the substrate specificity of xylitol dehydrogenases, xylitol dehydrogenase from G. oxydans ATCC 621 has been noted to present a higher catalytic activity toward sorbitol and xylitol, whereas xylitol dehydrogenase from Gluconobacter thailandicus CGMCC1.3748 has been demonstrated to exhibit catalytic activity toward xylitol, d -sorbitol, d -mannitol, and d -fructose . Besides, while most of the known xylitol dehydrogenases have been reported to be dependent on cofactor NAD + , an NADP + -dependent xylitol dehydrogenase has been found to increase ethanol production from xylose in recombinant Saccharomyces cerevisiae though protein engineering …”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Identification of NAD-Dependent Xylitol Dehydrogenase from Gluconobacter oxydans WSH-003

Liu

Zeng

et al. 2019

ACS Omega

View full text Add to dashboard Cite

Gluconobacter oxydans plays an important role in the conversion of d-sorbitol to l-sorbose, which is an essential intermediate for the industrial-scale production of vitamin C. In the fermentation process, some d-sorbitol could be converted to d-fructose and other byproducts by uncertain dehydrogenases. Genome sequencing has revealed the presence of diverse genes encoding dehydrogenases in G. oxydans. However, the characteristics of most of these dehydrogenases remain unclear. Therefore, the analyses of these unknown dehydrogenases could be useful for identifying those related to the production of d-fructose and other byproducts. Accordingly, dehydrogenases in G. oxydans WSH-003, an industrial strain used for vitamin C production, were examined. A nicotinamide adenine dinucleotide (NAD)-dependent dehydrogenase, which was annotated as xylitol dehydrogenase 2, was identified, codon-optimized, and expressed in Escherichia coli BL21 (DE3) cells. The enzyme exhibited a high preference for NAD+ as the cofactor, while no activity with nicotinamide adenine dinucleotide phosphate, flavin adenine dinucleotide, or pyrroloquinoline quinone was noted. Although this enzyme presented high similarity with NAD-dependent xylitol dehydrogenase, it showed high activity to catalyze d-sorbitol to d-fructose. Unlike the optimum temperature and pH for most of the known NAD-dependent xylitol dehydrogenases (30–40 °C and about 6–8, respectively), those for the identified enzyme were 57 °C and 12, respectively. The values of Km and Vmax of the identified dehydrogenase toward l-sorbitol were 4.92 μM and 196.08 μM/min, respectively. Thus, xylitol dehydrogenase 2 can be useful for the cofactor-reduced nicotinamide adenine dinucleotide regeneration under alkaline conditions, or its knockout can improve the conversion ratio of d-sorbitol to l-sorbose.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Identification of NAD-Dependent Xylitol Dehydrogenase from Gluconobacter oxydans WSH-003

Liu

Zeng

et al. 2019

ACS Omega

View full text Add to dashboard Cite

show abstract

“…Due to strong expression and misfolding of BAAI during induction process, recombinant BAAI formed inclusion bodies as also reported for L-AI of C. hylemonae (Nguyen et al, 2018). To dissolve inclusion bodies and get BBAI in soluble form, cells were harvested by centrifugation at 8,000 rpm (4 • C) for 15 min and washed twice with 100 mM sodium phosphate buffer (pH 7.4) as described earlier (Qi et al, 2016;Zhang et al, 2018). Thereafter, cells were re-suspended in the lysis buffer (50 mM Tris-Cl, 100 mM NaCl, 1% Triton X) and disrupted by sonication (350 W; 1.5 s working time, 2 s interval, for 20 mins, at 4 • C), and centrifuged at 10,000 rpm (4 • C) for 10 min (Qi et al, 2017).…”

Section: Expression and Purification Of Recombinant Baaimentioning

confidence: 99%

Exploring a Highly D-Galactose Specific L-Arabinose Isomerase From Bifidobacterium adolescentis for D-Tagatose Production

Zhang

Parvez

et al. 2020

Front. Bioeng. Biotechnol.

Self Cite

View full text Add to dashboard Cite

D-Galactose-specific L-arabinose isomerase (L-AI) would have much potential for the enzymatic conversion of D-Galactose into D-tagatose, while most of the reported L-AIs are L-arabinose specific. This study explored a highly D-Galactose-specific L-AI from Bifidobacterium adolescentis (BAAI) for the production of D-tagatose. In the comparative protein-substrate docking for D-Galactose and L-arabinose, BAAI showed higher numbers of hydrogen bonds in D-Galactose-BAAI bonding site than those found in L-arabinose-BAAI bonding site. The activity of BAAI was 24.47 U/mg, and it showed good stability at temperatures up to 65 • C and a pH range 6.0-7.5. The K m , V max , and K cat /K m of BAAI were found to be 22.4 mM, 489 U/mg and 9.3 mM −1 min −1 , respectively for D-Galactose, while the respective values for L-arabinose were 40.2 mM, 275.1 U/mg, and 8.6 mM −1 min −1 . Enzymatic conversion of D-Galactose into D-tagatose by BAAI showed 56.7% conversion efficiency at 55 • C and pH 6.5 after 10 h.

show abstract

“…Corn cob is the secondary agricultural residue in the world; more than 70 million metric tons of corn cob was produced by USA and China in 2008. , It is rich in hemicellulose and can easily be hydrolyzed to obtain corn cob hydrolysate with d- xylose, d- glucose, and l -arabinose as its utilizable sugars. , However, corn cob hydrolysate has not been effectively utilized recently. In China, corn cob hydrolysate is mainly used to prepare d- xylose, which is used to produce xylitol through chemical reduction. − The annual production of xylitol is expected to be about 2.4 × 10 5 tons by 2020. , With the increasing yield of maize, the corn cob production has exceeded the demands of the xylitol industry and is becoming an environmental pollutant due to the lack of its effective utilization …”

Section: Introductionmentioning

confidence: 99%

“…6−8 The annual production of xylitol is expected to be about 2.4 × 10 5 tons by 2020. 9,10 With the increasing yield of maize, 11 the corn cob production has exceeded the demands of the xylitol industry and is becoming an environmental pollutant due to the lack of its effective utilization. 12 D-Xylonate is a five-carbon organic acid that can be used as a chelator, dispersant, and precursor for various platform chemicals, such as 3,4-dihydroxybutanal, 3,4-dihydroxybutyrate, 1,2,4-butantriol, and 1,4-butanediol.…”

Section: ■ Introductionmentioning

confidence: 99%

Production of d-Xylonate from Corn Cob Hydrolysate by a Metabolically Engineered Escherichia coli Strain

Zhang

Guo

Wang

et al. 2018

ACS Sustainable Chem. Eng.

View full text Add to dashboard Cite

Corn cob is the secondary agricultural residue that can be easily hydrolyzed into hydrolysate with abundant d-xylose. Besides d-xylose, d-glucose, and l-arabinose are also utilizable sugars in corn cob hydrolysate. Here, we established a coutilization system through which recombinant Escherichia coli can use d-glucose and l-arabinose supporting its growth and convert d-xylose in corn cob hydrolysate into d-xylonate. First, biosynthetic pathway of d-xylonate was overexpressed and two xylonate dehydratases were knocked out in E. coli W3110 to enhance d-xylonate production from d-xylose. Then, the genes responsible for acetate, ethanol, and lactate synthesis were knocked out to decrease these byproducts production during the growth of the recombinant strain. Three successive strategies were employed to enhance the d-xylonate productionusing lactose as the inducer, eliminating carbon catabolite repression, and inactivating the lactose degradation. Finally, 108.2 g/L d-xylonate was produced with a yield of 1.09 g of d-xylonate/g of d-xylose using d-xylose as the substrate and d-glucose as the carbon source through fed-batch fermentation. When corn cob hydrolysate was used, 91.2 g/L d-xylonate was produced with a specific productivity of 1.52 g/[L·h]. This study is valuable not only for producing d-xylonate but also for providing a coutilization system to obtain other important chemicals from corn cob hydrolysate.

show abstract

Production of xylitol by expressing xylitol dehydrogenase and alcohol dehydrogenase from Gluconobacter thailandicus and co-biotransformation of whole cells

Cited by 34 publications

References 30 publications

Identification of NAD-Dependent Xylitol Dehydrogenase from Gluconobacter oxydans WSH-003

Identification of NAD-Dependent Xylitol Dehydrogenase from Gluconobacter oxydans WSH-003

Exploring a Highly D-Galactose Specific L-Arabinose Isomerase From Bifidobacterium adolescentis for D-Tagatose Production

Production of d-Xylonate from Corn Cob Hydrolysate by a Metabolically Engineered Escherichia coli Strain

Contact Info

Product

Resources

About