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Koh, Sukhoon; Shin, Hyun‐Jae; Kim, Joong Su; Lee, Dae-Sil; Lee, Se Young

doi:10.1023/a:1005342921339

Cited by 30 publications

(7 citation statements)

References 11 publications

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“…The trehalose synthase catalyzes two competing reactions: the formation of trehalose is maltose rearrangement by trehalose synthase, which is related to intramolecular transglycosylation. The formation of glucose resulted from the attack of water molecules on the catalytic pockets of the enzyme, which leads to the transformation of a maltose molecule into two glucose molecules . The formation of glucose during the process has been shown to be irreversible and thus could lead to a decline in trehalose yield .…”

Section: Resultsmentioning

confidence: 99%

“…The formation of glucose resulted from the attack of water molecules on the catalytic pockets of the enzyme, which leads to the transformation of a maltose molecule into two glucose molecules . The formation of glucose during the process has been shown to be irreversible and thus could lead to a decline in trehalose yield . The presence of glucose in the reaction mixture could further hamper trehalose synthesis by acting as a competitive inhibitor …”

Section: Resultsmentioning

confidence: 99%

“…This pathway allows one-step formation of trehalose, and an inexpensive substrate, maltose, is employed, which provides a simple, fast, and low-cost method for the future industrial production of trehalose. Various TSases from different species have been isolated and characterized. − …”

Section: Introductionmentioning

confidence: 99%

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Integrated Biocatalytic Process for Trehalose Production and Separation from Maltose

Song

Tang

Jiang

et al. 2016

Ind. Eng. Chem. Res.

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To develop cost-effective, biobased, industrial trehalose production from maltose, an integrated bioprocess for trehalose production and separation from maltose with recombinant trehalose synthase in permeabilized cells is proposed in this study. We have successfully established an efficient production system for recombinant trehalose synthase (TreS) (9234 U/mL) in a 50 L fermentor and efficient processes for separation and purification to achieve comprehensive utilization of the raw material and products. The trehalose conversion rate of 75% at 30 °C can be reached with 6% glucose generated as byproduct using maltose syrup (30 wt %) as substrate in the bioreactor system via whole-cell biocatalysis. After two-stage simulated moving bed chromatography (SMB), the trehalose could be successfully separated, crystallized, and identified with a 97.6% purity and 95.9% recovery yield, respectively. The yield of trehalose produced was 0.675 g per gram of maltose consumed in the whole process within 80.5 h.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Integrated Biocatalytic Process for Trehalose Production and Separation from Maltose

Song

Tang

Jiang

et al. 2016

Ind. Eng. Chem. Res.

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“…Maltose can be easily prepared from starch by β-amylase and pullulanase. A number of treS genes from different bacteria have been identified and characterized, and some have been applied in trehalose production. ,− However, treS -containing bacteria produce trehalose from maltose with a very low yield. Thus, treS genes were cloned from those bacteria, overexpressed in Escherichia coli, purified, and used as free enzymes or biocatalysts to convert maltose to trehalose at yields of 40–70%. − The E.…”

Section: Introductionmentioning

confidence: 99%

Integrated Approach To Producing High-Purity Trehalose from Maltose by the Yeast Yarrowia lipolytica Displaying Trehalose Synthase (TreS) on the Cell Surface

Li¹,

Wang

Li³

et al. 2016

J. Agric. Food Chem.

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An alternative strategy that integrated enzyme production, trehalose biotransformation, and bioremoval in one bioreactor was developed in this study, thus simplifying the traditional procedures used for trehalose production. The trehalose synthase gene from a thermophilic archaea, Picrophilus torridus, was first fused to the YlPir1 anchor gene and then inserted into the genome of Yarrowia lipolytica, thus yielding an engineered yeast strain. The trehalose yield reached 73% under optimal conditions. The thermal and pH stabilities of the displayed enzyme were improved compared to those of its free form purified from recombinant Escherichia coli. After biotransformation, the glucose byproduct and residual maltose were directly fermented to ethanol by a Saccharomyces cerevisiae strain. Ethanol can be separated by distillation, and high-purity trehalose can easily be obtained from the fermentation broth. The results show that this one-pot procedure is an efficient approach to the economical production of trehalose from maltose.

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“…Because this pathway allows one-step formation of trehalose and an inexpensive substrate, maltose, is employed, this pathway is capable of industrial manufacture of trehalose. Up to now, about six TSases have been reported from different species and characterized for their biochemical properties ( − ). However, the three TSases from Pimelobacter sp.…”

Section: Introductionmentioning

confidence: 99%

Gene Cloning, Expression, and Biochemical Characterization of a Recombinant Trehalose Synthase from Picrophilus torridus in Escherichia coli

Chen

Lee

Shaw

2006

J. Agric. Food Chem.

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A trehalose synthase (TSase) gene from a hyperacidophilic, thermophilic archaea, Picrophilus torridus, was synthesized using overlap extension PCR and transformed into Escherichia coli for expression. The purified recombinant P. torridus TSase (PTTS) showed an optimum pH and temperature of 6.0 and 45 degrees C, respectively, and the enzyme maintained high activity at pH 5.0 and 60 degrees C. Kinetic analysis showed that the enzyme has a 2.5-fold higher catalytic efficiency (k(cat)/K(M)) for maltose than for trehalose, indicating maltose as the preferred substrate. The maximum conversion rate of maltose into trehalose by the enzyme was independent of the substrate concentration, tended to increase at lower temperatures, and reached approximately 71% at 20 degrees C. Enzyme activity was inhibited by Hg2+, Al3+, and SDS. Five amino acid residues that are important for alpha-amylase family enzyme catalysis were shown to be conserved in PTTS (Asp203, Glu245, Asp311, His106, and His310) and required for its activity, suggesting this enzyme might employ a similar hydrolysis mechanism.

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Cited by 30 publications

References 11 publications

Integrated Biocatalytic Process for Trehalose Production and Separation from Maltose

Integrated Biocatalytic Process for Trehalose Production and Separation from Maltose

Integrated Approach To Producing High-Purity Trehalose from Maltose by the Yeast Yarrowia lipolytica Displaying Trehalose Synthase (TreS) on the Cell Surface

Gene Cloning, Expression, and Biochemical Characterization of a Recombinant Trehalose Synthase from Picrophilus torridus in Escherichia coli

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