Cloning, expression and activity optimization of trehalose synthase from Thermus thermophilus HB27

Li, Yan; Sun, Xinxiao; Feng, Yue; Yuan, Qipeng

doi:10.1016/j.ces.2015.02.034

Cited by 17 publications

(13 citation statements)

References 26 publications

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“…Fusion protein expression is a common strategy to obtain enzyme proteins. Due to the convenience of purification using Ni-chelating affinity chromatography, histidine tags are widely used for enzyme protein expression [18,19]. Nickel ions modified materials for enzyme purification and immobilization were developed which are based on the affinity of nickel ions and histidine labels [20][21][22].…”

Section: Introductionmentioning

confidence: 99%

Fast Immobilization of Human Carbonic Anhydrase II on Ni-Based Metal-Organic Framework Nanorods with High Catalytic Performance

Jiao

Sun

et al. 2020

Catalysts

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Carbonic anhydrase (CA) has received considerable attention for its ability to capture carbon dioxide efficiently. This study reports a simple strategy for immobilizing recombinant carbonic anhydrase II from human (hCA II) on Ni-based MOFs (Ni-BTC) nanorods, which was readily achieved in a one-pot immobilization of His-tagged hCA II (His-hCA II). Consequently, His-hCA II from cell lysate could obtain an activity recovery of 99% under optimal conditions. After storing for 10 days, the immobilized His-hCA II maintained 40% activity while the free enzyme lost 91% activity. Furthermore, during the hydrolysis of p-nitrophenyl acetic acid, immobilized His-hCA II exhibited excellent reusability and still retained more than 65% of the original activity after eight cycles. In addition, we also found that Ni-BTC had no fixation effect on proteins without histidine-tag. These results show that the Ni-BTC MOFs have a great potential with high efficiency for and specific binding of immobilized enzymes.

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Section: Introductionmentioning

confidence: 99%

Fast Immobilization of Human Carbonic Anhydrase II on Ni-Based Metal-Organic Framework Nanorods with High Catalytic Performance

Jiao

Sun

et al. 2020

Catalysts

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“…By the end of fermentation (25 h), the OD 600 of E. coli and TtTreS activity of fermentation broth reached 40 and 24,666 U/L, respectively. The fermentation time was decreased to 25 h from 30 h, which was needed for fermentation in flasks [ 10 ]. The TtTreS activity of unit fermentation broth was also improved after fermentation scale-up by fermenter.…”

Section: Resultsmentioning

confidence: 99%

“…In the present study, we are reporting the continuation of our former report describing trehalose production by recombinant TtTreS [ 10 ]. In this study, we used a 2.5 L fermenter to scale up the production of recombinant TtTreS.…”

Section: Introductionmentioning

confidence: 82%

“…E. coli BL21(DE3) harboring pET-22b-tttreS and pCS27-sigma-32-GroeL-GroeS-DnaK-DnaJ was constructed in our previous study [ 10 ]. Luria–Bertani (LB) medium and Terrific Broth (TB) were used for pre-cultures in shake flasks and fermentation cultures in a 2.5-L fermenter (INFORS HT minifors, Switzerland), respectively.…”

Section: Methodsmentioning

confidence: 99%

“…TreS is efficient, practical, and low-cost for the industrial production of trehalose, since it involves only one step to convert maltose into trehalose by intramolecular rearrangement in vitro [ 8 , 9 ]. Recently, TreS derived from Thermus thermophiles (TtTreS) was successfully expressed in Escherichia coli to produce trehalose [ 10 ]. Our recent research indicated that the activity of TtTreS could be further improved by adding the C-terminal domain [ 11 ].…”

Section: Introductionmentioning

confidence: 99%

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Improvement of Trehalose Production by Immobilized Trehalose Synthase from Thermus thermophilus HB27

Sun

Wang

et al. 2018

Molecules

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Trehalose is a non-reducing disaccharide with a wide range of applications in the fields of food, cosmetics, and pharmaceuticals. In this study, trehalose synthase derived from Thermus thermophilus HB27 (TtTreS) was immobilized on silicalite-1-based material for trehalose production. The activity and the stability of TtTreS against pH and temperature were significantly improved by immobilization. Enzyme immobilization also led to a lower concentration of byproduct glucose, which reduces byproduct inhibition of TtTreS. The immobilized TtTreS still retained 81% of its initial trehalose yield after 22 cycles of enzymatic reactions. The immobilized TtTreS exhibited high operational stability and remarkable reusability, indicating that it is promising for industrial applications.

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Potential Microbial Bioresources for Functional Sugar Molecules

Patel

Sharma

Singh

et al. 2023

Microbial Bioreactors for Industrial Molecules

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Cloning, expression and activity optimization of trehalose synthase from Thermus thermophilus HB27

Cited by 17 publications

References 26 publications

Fast Immobilization of Human Carbonic Anhydrase II on Ni-Based Metal-Organic Framework Nanorods with High Catalytic Performance

Fast Immobilization of Human Carbonic Anhydrase II on Ni-Based Metal-Organic Framework Nanorods with High Catalytic Performance

Improvement of Trehalose Production by Immobilized Trehalose Synthase from Thermus thermophilus HB27

Potential Microbial Bioresources for Functional Sugar Molecules

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