Stability and activity of Dictyoglomus thermophilum GH11 xylanase and its disulphide mutant at high pressure and temperature

Li, He; Voutilainen, Sanni; Ojamo, Heikki; Turunen, Ossi

doi:10.1016/j.enzmictec.2014.12.011

Cited by 17 publications

(6 citation statements)

References 44 publications

(57 reference statements)

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“…We previously studied the effect of a high temperature on the behaviour and kinetic parameters of extremophilic xylanases (Li et al 2015 ). In D. thermophilum GH11 xylanase, which has an apparent temperature optimum at 90 °C, the K m value increased 5-fold in response to a shift in temperature from 90 to 100 °C.…”

Section: Discussionmentioning

confidence: 99%

“…Monosaccharides and oligosaccharides are known to inhibit cellulases, which can be a significant problem in the hydrolysis of lignocellulose (Collins et al 2005 ). A study of extremophilic xylanase reported weaker binding of short sugar compounds at higher temperatures (Li et al 2015 ). Therefore, when highly thermophilic xylanase enzymes are needed for biocatalytic processes under extreme conditions having also multiple inhibiting factors in the reaction mixture, the T. maritima GH10 xylanase appears to be a promising enzyme (Jia et al 2012 ).…”

Section: Discussionmentioning

confidence: 99%

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Hyperthermostable Thermotoga maritima xylanase XYN10B shows high activity at high temperatures in the presence of biomass-dissolving hydrophilic ionic liquids

Anbarasan

Wang

et al. 2016

Extremophiles

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The gene of Thermotoga maritima GH10 xylanase (TmXYN10B) was synthesised to study the extreme limits of this hyperthermostable enzyme at high temperatures in the presence of biomass-dissolving hydrophilic ionic liquids (ILs). TmXYN10B expressed from Pichia pastoris showed maximal activity at 100 °C and retained 92 % of maximal activity at 105 °C in a 30-min assay. Although the temperature optimum of activity was lowered by 1-ethyl-3-methylimidazolium acetate ([EMIM]OAc), TmXYN10B retained partial activity in 15–35 % hydrophilic ILs, even at 75–90 °C. TmXYN10B retained over 80 % of its activity at 90 °C in 15 % [EMIM]OAc and 15–25 % 1-ethyl-3-methylimidazolium dimethylphosphate ([EMIM]DMP) during 22-h reactions. [EMIM]OAc may rigidify the enzyme and lower Vmax. However, only minor changes in kinetic parameter Km showed that competitive inhibition by [EMIM]OAc of TmXYN10B is minimal. In conclusion, when extended enzymatic reactions under extreme conditions are required, TmXYN10B shows extraordinary potential.Electronic supplementary materialThe online version of this article (doi:10.1007/s00792-016-0841-y) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Hyperthermostable Thermotoga maritima xylanase XYN10B shows high activity at high temperatures in the presence of biomass-dissolving hydrophilic ionic liquids

Anbarasan

Wang

et al. 2016

Extremophiles

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“…Ultrasound may alter the secondary structure of the enzyme, thereby exposing the active site of the enzyme to a better extent (Subhedar and Gogate, 2014). The changes of secondary structure of proteins can be analyzed by CD spectroscopy, which calculates the α-helix, β-strand (β-Sheet and β-turn) and random coiling of xylanase, and the relationship between enzyme activity and secondary structure is determined (Li et al, 2015). A typical characteristic of all natural enzyme structure cd spectra is that the XynB spectrum has a fixed minimum peak at 209 nm and a positive peak at 195 nm, which is essentially the same as the native zymogram seen from early researches (You et al, 2010).…”

Section: Effect Of Ultrasonic Treatment On Xylanase Structure (Cd Spectra Analysis)mentioning

confidence: 99%

Ultrasound-Assisted Production of Xylo-Oligosaccharides From Alkali-Solubilized Corncob Bran Using Penicillium janthinellum XAF01 Acidic Xylanase

Zhou

Fan

Xia

et al. 2021

Front. Bioeng. Biotechnol.

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A novel treatment involving enzymatic hydrolysis using an acidic xylanase coupled with ultrasound was performed to improve the xylo-oligosaccharides (XOS) yield from corncob bran. The acidic xylanase (XynB) was purified to a most suitable pH, temperature, and operational parameters for ultrasound-assisted hydrolysis were determined. A preliminary mechanistic investigation was performed through circular dichroism (CD) spectroscopy, scanning electron microscope (SEM) and a laser particle size analyzer, and the effects of ultrasound on enzyme (XynB) and substrate (corncob bran) were assessed. The results show that the maximum XOS yield was 20.71% when the reaction pH and temperature were 4.3 and 50°C, the ultrasonic parameters were 50 kHz and 0.40 W/cm2, which was 2.55 fold higher than that obtained using a non-ultrasound-assisted enzymatic preparation. Mechanism studies indicated that ultrasonic pretreatment could reduce the β-fold content and increase the random coil content. Changes in structure and size of substrate were observed. The specific surface area of the XAC molecules is easy to carry out enzymatic reaction, which is beneficial to the production of XOS.

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“…Among the most thermostable enzymes reported subsequently have been those from anaerobic thermophiles such as Caldicellulosiruptor saccharolyticus [28] and C. bescii [29]. The half-life of inactivation of xylanase from Dictyoglomus thermophilum at 80°C and 500 MPa has been over 30 h [30]. The observed two active bands, one strong and one weak, in the zymogram of the culture supernatant revealed the synthesis of several enzyme forms observed also by other authors [31].…”

Section: Xylanase Produced By Anoxybacillus Flavithermus Bcmentioning

confidence: 53%

“…The xylanase showed high thermostability comparable to most thermostable enzymes -it retained 100% of its activity after 40 h at 70°C in six-fold concentrated enzyme supernatant [25]. The half-life of inactivation of xylanase from Dictyoglomus thermophilum at 80°C and 500 MPa has been over 30 h [30]. Bataillon et al [27] have observed maintenance of activity after 4 h at 70°C of the thermostable enzyme from Bacillus sp.…”

Section: Xylanase Produced By Anoxybacillus Flavithermus Bcmentioning

confidence: 96%

Thermostable enzymes and polysaccharides produced by thermophilic bacteria isolated from Bulgarian hot springs

Kambourova

2018

Engineering in Life Sciences

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Thermostable enzymes (thermozymes) have been recognized as extremophilic compounds with a greatest biotechnological importance in different industrial areas. Quite recently exopolysaccharides (EPSs) synthesized by thermophiles became an object of increased research interest due to their unique properties appropriate for some specific industrial needs. Thermophilic producers of biotechnologically valuable enzymes and novel EPS were isolated by our group from Bulgarian thermal springs with a diverse geotectonic origin and different water properties. Laboratory reactor processes for their production were developed in batch and continuous cultures. Some of the synthesized thermostable enzymes were among the first described in their groups, for example, the single known thermostable gellan lyase that demonstrated specific activity higher than that of the mesophilic enzymes. Isolated by us thermostable xylanase was able to degrade more than 60% of beechwood xylan in a coprocess with an archaeal β‐xylosidase. Lipase purified by us was active between 55 and 90°C with an optimum at 75–80°C in a large pH range. It was able to degrade a broad range of substrates. Isolates from Bulgarian hot springs synthesized EPS with novel composition and high thermostability. Thus, Bulgarian hot springs harbor a wide set of thermophilic producers of novel enzymes and EPS with potential for a large number of biotechnological applications.

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Stability and activity of Dictyoglomus thermophilum GH11 xylanase and its disulphide mutant at high pressure and temperature

Cited by 17 publications

References 44 publications

Hyperthermostable Thermotoga maritima xylanase XYN10B shows high activity at high temperatures in the presence of biomass-dissolving hydrophilic ionic liquids

Hyperthermostable Thermotoga maritima xylanase XYN10B shows high activity at high temperatures in the presence of biomass-dissolving hydrophilic ionic liquids

Ultrasound-Assisted Production of Xylo-Oligosaccharides From Alkali-Solubilized Corncob Bran Using Penicillium janthinellum XAF01 Acidic Xylanase

Thermostable enzymes and polysaccharides produced by thermophilic bacteria isolated from Bulgarian hot springs

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