A novel l-arabinose isomerase from Lactobacillus fermentum CGMCC2921 for d-tagatose production: Gene cloning, purification and characterization

Xu, Zheng; Qing, Yujia; Li, Sha; Feng, Xiaohai; Xu, Hong; Ouyang, Pingkai

doi:10.1016/j.molcatb.2011.01.010

Cited by 63 publications

(53 citation statements)

References 32 publications

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“…1,9,42 The low affinity for l -arabinose is comparable with the enzyme from Pediococcus pentosaceus PC-5, which shows no activity for this substrate. 10 …”

Section: Resultsmentioning

confidence: 87%

“…2 This low-calorie sweetener has numerous health and medical benefits, including prevention of dental caries, regulation of intestinal flora, and reduction of symptoms of type 2 diabetes. 1 The sweetness of d -tagatose is comparable to that of sucrose, and it has received “generally recognized as safe” (GRAS) status from the U.S. Food and Drug Administration. 3 d -Tagatose can be produced from d -galactose by a chemical method using a calcium catalyst, but this process has some disadvantages including complex purification steps and the formation of chemical waste and byproducts.…”

Section: Introductionmentioning

confidence: 99%

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l-Arabinose Isomerase and d-Xylose Isomerase from Lactobacillus reuteri: Characterization, Coexpression in the Food Grade Host Lactobacillus plantarum, and Application in the Conversion of d-Galactose and d-Glucose

Staudigl

Haltrich

Peterbauer

2014

J. Agric. Food Chem.

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The l-arabinose isomerase (l-AI) and the d-xylose isomerase (d-XI) encoding genes from Lactobacillus reuteri (DSMZ 17509) were cloned and overexpressed in Escherichia coli BL21 (DE3). The proteins were purified to homogeneity by one-step affinity chromatography and characterized biochemically. l-AI displayed maximum activity at 65 °C and pH 6.0, whereas d-XI showed maximum activity at 65 °C and pH 5.0. Both enzymes require divalent metal ions. The genes were also ligated into the inducible lactobacillal expression vectors pSIP409 and pSIP609, the latter containing a food grade auxotrophy marker instead of an antibiotic resistance marker, and the l-AI- and d-XI-encoding sequences/genes were coexpressed in the food grade host Lactobacillus plantarum. The recombinant enzymes were tested for applications in carbohydrate conversion reactions of industrial relevance. The purified l-AI converted d-galactose to d-tagatose with a maximum conversion rate of 35%, and the d-XI isomerized d-glucose to d-fructose with a maximum conversion rate of 48% at 60 °C.

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“…1,9,42 The low affinity for l -arabinose is comparable with the enzyme from Pediococcus pentosaceus PC-5, which shows no activity for this substrate. 10 …”

Section: Resultsmentioning

confidence: 87%

Section: Introductionmentioning

confidence: 99%

l-Arabinose Isomerase and d-Xylose Isomerase from Lactobacillus reuteri: Characterization, Coexpression in the Food Grade Host Lactobacillus plantarum, and Application in the Conversion of d-Galactose and d-Glucose

Staudigl

Haltrich

Peterbauer

2014

J. Agric. Food Chem.

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“…Furthermore, we found that D-glucose in the conversion mixtures could be completely consumed by a Saccharomyces cerevisiae strain (purchased from Angel Yeast Co. Ltd, Yichang, China) to form ethanol, which could be easily eliminated by evaporation (data not shown). Referring to the previously reported method [8], the D-tagatose-borate complex was separated from D-galactose and lactose through a Ca 2+ Amberlite column, and borate could be removed as methyl borate under vacuum [23][24][25]. As a low-calorie functional sweetener, however, the D-tagatose market is currently limited due to its high price.…”

Section: Discussionmentioning

confidence: 99%

“…D-tagatose could be manufactured by chemical and biological methods, selectively using lactose or whey as the starting material thermophilic, and hyperthermophilic bacteria [2]. More particularly, the thermo-AIs which exhibited optimum temperatures at 60-70°C were approved to be extremely suitable for industrialization of D-tagatose [7,8]. Under this circumstance, the highest yield of Dtagatose was reported to be 370 gl −1 with a conversion rate of 74% (w/w) from Dgalactose by isomerization of a purified thermo-AI [9].…”

Section: Introductionmentioning

confidence: 99%

Production of d-tagatose, a Functional Sweetener, Utilizing Alginate Immobilized Lactobacillus fermentum CGMCC2921 Cells

Feng-gen

et al. 2011

Appl Biochem Biotechnol

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D-tagatose is a ketohexose that can be used as a novel functional sweetener in foods, beverages, and dietary supplements. This study was aimed at developing a high-yielding D-tagatose production process using alginate immobilized Lactobacillus fermentum CGMCC2921 cells. For the isomerization from D-galactose into D-tagatose, the immobilized cells showed optimum temperature and pH at 65 °C and 6.5, respectively. The alginate beads exhibited a good stability after glutaraldehyde treatment and retained 90% of the enzyme activity after eight cycles (192 h at 65 °C) of batch conversion. The addition of borate with a molar ratio of 1.0 to D-galactose led to a significant enhancement in the D-tagatose yield. Using commercial β-galactosidase and immobilized L. fermentum cells, D-tagatose was successfully obtained from lactose after a two-step biotransformation. The relatively high conversion rate and productivity from D-galactose to D-tagatose of 60% and 11.1 g l⁻¹ h⁻¹ were achieved in a packed-bed bioreactor. Moreover, lactobacilli have been approved as generally recognized as safe organisms, which makes this L. fermentum strain an attracting substitute for recombinant Escherichia coli cells among D-tagatose production progresses.

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“…15 Generally, a major consideration in biotransformation processes is the development suitable biological catalysts. 16,17 L-AI from various prokaryotic microbes have been identified, including those from Escherichia coli, 18 Lactobacillus plantarum, 19,20 Lactobacillus fermentum, 21 Arthrobacter sp., 22 Lactobacillus sakei, 23 Bifidobacterium longum, 24 and Thermus sp. Strain.…”

Section: Introductionmentioning

confidence: 99%

D-Tagatose production by Lactococcus lactis NZ9000 Cells Harboring Lactobacillus plantarum L-arabinose Isomerase

Yao¹,

Fan²,

Hu³

et al. 2017

IJPER

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D-tagatose is a functional sweetener present in medicine, food, and dairy products and with broad market prospects, and L-arabinose isomerase gene (araA) can mediate the bioconversion of D-galactose into D-tagatose. In this study, a Lactococcus lactis NZ9000 strain harboring exogenous L-arabinose isomerase was constructed to produce D-tagatose. Lactobacillus plantarum CGMCC 8198 exhibits L-arabinose isomerase activity and its genome has been sequenced. The araA gene of Lactobacillus plantarum CGMCC 8198 encoding L-arabinose isomerase was identified by sequence analysis and was successfully cloned and expressed in Lactococcus lactis NZ9000. The D-tagatose production by the whole cell of the recombinant strain was optimized. The optimal condition for conversion reaction was at 50°C, pH 7.0 and with 300 mmol/L Mn 2+ and 60 g/L galactose added. The D-tagatose yield and conversion rate at the optimal condition was determined and reached 40.2 g/L and 67%, respectively.

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A novel l-arabinose isomerase from Lactobacillus fermentum CGMCC2921 for d-tagatose production: Gene cloning, purification and characterization

Cited by 63 publications

References 32 publications

l-Arabinose Isomerase and d-Xylose Isomerase from Lactobacillus reuteri: Characterization, Coexpression in the Food Grade Host Lactobacillus plantarum, and Application in the Conversion of d-Galactose and d-Glucose

l-Arabinose Isomerase and d-Xylose Isomerase from Lactobacillus reuteri: Characterization, Coexpression in the Food Grade Host Lactobacillus plantarum, and Application in the Conversion of d-Galactose and d-Glucose

Production of d-tagatose, a Functional Sweetener, Utilizing Alginate Immobilized Lactobacillus fermentum CGMCC2921 Cells

D-Tagatose production by Lactococcus lactis NZ9000 Cells Harboring Lactobacillus plantarum L-arabinose Isomerase

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