Comparison study on the interaction mechanisms of B. amyloliquefaciens amylase with PEG-400 and TEPA and the properties of enzyme

Wang, Feng; Shao, Lin-Lin; Zhang, Xuan

doi:10.1016/j.molstruc.2014.10.066

Cited by 8 publications

(1 citation statement)

References 61 publications

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“…The reason for the enhancement of thermostability was attributed to the interactions between the PEG and the protein which might stabilize its native tertiary structure . Additionally, the residual activity of amylase from Bacillus amyloliquefaciens was also increased by the addition of PEG 400 according to the investigations of Wang …”

Section: Introductionmentioning

confidence: 99%

A close look on the effect of polyethylene glycol on the levansucrase thermostability: a case study of Brenneria sp. levansucrase

Zhang

Guang

et al. 2019

J Sci Food Agric

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BACKGROUND To increase the low residual activity of levansucrase during long‐time processing, an enhancement of its weak thermostability is needed. Here, the effect of metal ions and polyethylene glycol (PEG) on the thermostability of levansucrase from Brenneria sp. EniD312 were studied and evaluated. The residual activity was determined and the protein structure was evaluated by circular dichroism spectrum, fluorescence intensity (FI), and surface hydrophobicity (S0). RESULTS As a result of incubation with 10% (w/v) PEG 4000, the enzyme activity was increased by 1.24‐fold. After incubation with 5% PEG 4000 for 6 h, the residual activity at 35 and 45 °C was decreased to 55% and 60% of the initial activity, with an increase of 1.2‐ and 3.3‐fold than the wild‐type enzyme. Furthermore, the random coil content of enzyme was decreased from 53% of the wild‐type enzyme to 33.9% of the PEG pre‐incubated enzyme. Additionally, the FI was maximally increased and the S0 was decreased from 117 to 69. CONCLUSION All of these results suggested that after incubation with PEG 4000, the secondary and tertiary structure of wild‐type enzyme could be greatly maintained and then its thermostability could be increased. This study was the first report on the enhancement of levansucrase thermostability by PEG incubation and might be a good guideline to other researches on levansucrase. © 2019 Society of Chemical Industry

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Section: Introductionmentioning

confidence: 99%

A close look on the effect of polyethylene glycol on the levansucrase thermostability: a case study of Brenneria sp. levansucrase

Zhang

Guang

et al. 2019

J Sci Food Agric

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Site-specific immobilization of papain on DDI-modified polystyrene beads for the oligo(γ-ethyl-L-glutamate) synthesis

Wang

et al. 2022

Applied Catalysis A: General

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Spectroscopic and mechanistic analysis of the interaction between Jack bean urease and polypseudorotaxane fabricated with bis-thiolated poly(ethylene glycol) and α-cyclodextrin

Zhao

Fang

et al. 2019

Colloids and Surfaces B: Biointerfaces

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Comparison study on the interaction mechanisms of B. amyloliquefaciens amylase with PEG-400 and TEPA and the properties of enzyme

Cited by 8 publications

References 61 publications

A close look on the effect of polyethylene glycol on the levansucrase thermostability: a case study of Brenneria sp. levansucrase

A close look on the effect of polyethylene glycol on the levansucrase thermostability: a case study of Brenneria sp. levansucrase

Site-specific immobilization of papain on DDI-modified polystyrene beads for the oligo(γ-ethyl-L-glutamate) synthesis

Spectroscopic and mechanistic analysis of the interaction between Jack bean urease and polypseudorotaxane fabricated with bis-thiolated poly(ethylene glycol) and α-cyclodextrin

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