Solution scattering studies of conformation stability of xylanase XYNII from <i>Trichoderma longibrachiatum</i>

Kozak, Maciej

doi:10.1002/bip.20531

Cited by 9 publications

(14 citation statements)

References 45 publications

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“…The stability of the xylanase molecule shape in solution at 158C and in wide range of pH values (3-10) was studied in Ref. 15, where it was found that it remained relatively unchanged and similar to that implied by the crystal structure. The model of the XYNII molecule obtained from the SAXS data collected at 308C and presented in Figure 4a has also a shape similar to that implied by the crystal structure and that earlier proposed for xylanase in solution.…”

Section: Resultsmentioning

confidence: 91%

“…This value is close to that obtained in our earlier study of native xylanase XYNII in solution (pH 6.0). 15,35 At 508C, so at the temperature optimum for enzymatic activity of xylanase XYNII, 22 the shape of the function p(r) slightly changes, which can suggest a possible change in the conformation of the xylanase molecule. Conformational changes and open-close movements of XYNII active site have been previously suggested on the basis of the X-ray crystallographic and molecular dynamic studies.…”

Section: Resultsmentioning

confidence: 97%

“…The model of the XYNII molecule obtained from the SAXS data collected at 308C and presented in Figure 4a has also a shape similar to that implied by the crystal structure and that earlier proposed for xylanase in solution. 15 The typical model is characterized by R G ¼ 1.57-1.61 nm and D max ¼ 4.5-4.6 nm).…”

Section: Resultsmentioning

confidence: 99%

“…15 Till recently, a number of attempts at improving the activity and stability of xylanases in an alkaline medium and at high temperatures have been reported. 16 The thermal stability of xylanases from the family 11 has been studied for Bacillus circulans 17 Streptomyces sp.…”

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confidence: 99%

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Synchrotron radiation small angle scattering studies of thermal stability of xylanase XYNII from Trichoderma longibrachiatum

Kozak¹

2006

Biopolymers

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Xylanase XYNII from Trichoderma longibrachiatum is a small protein of the molecular weight 21 kDa, belonging to the family 11 of glycosyl hydrolases, which catalyses hydrolysis of xylan. This article reports thermal stability study of xylanase XYN II conformation in the temperature range 15-65 degrees C by the small angle synchrotron radiation scattering. The study has been performed at different pH conditions: at pH 4.0 (below the physiological optimum of the enzyme activity) at pH 5.8 close to the optimum for enzymatic activity and at pH 8.0. The radius of gyration and the pair distance distribution function p(r) have been analyzed to characterize the changes of the enzyme conformation on heating. In the environment of the pH close to that of the optimum for the enzymatic activity, xylanase shows the greatest thermal stability and undergoes denaturation only above 55 degrees C. In the acidic and basic environments, the enzyme stability is much lower and denaturation begins at 45 degrees C. On the basis of the SAXS data, the shape of the xylanase molecule in solution in different temperatures has been reconstructed using ab initio method and program DAMMIN. The shape of the xylanase molecule at room temperature is similar to the right hand, which is typically observed for xylanase crystal structure. In higher temperatures (close to the enzyme activity optimum), the conformation of the right hand is loosened and half opened.

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Section: Resultsmentioning

confidence: 91%

Section: Resultsmentioning

confidence: 97%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

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Synchrotron radiation small angle scattering studies of thermal stability of xylanase XYNII from Trichoderma longibrachiatum

Kozak¹

2006

Biopolymers

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“…The β-jelly-roll fold is better conserved than its sequence and it can hold several functions. Such structure makes GH11 xylanases be a dense globular proteins, whose gyration radius is nearly closed to 17 Å [20]. It may be one of the reasons for GH11 xylanases be the smallest which is similar to a monomeric enzyme.…”

Section: High-level Structure Analysis Of the Xynbmentioning

confidence: 98%

Cloning and expression of a broad pH stable GH11 xylanase from Aspergillus niger C71 / Aspergillus niger C71 den geniş pH aralığında dengeli olan GH11 xylanaz klonlaması ve ekspresyonu

Nie

Zhang

Shan

et al. 2015

Turkish Journal of Biochemistry

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Aspergillus niger C71 den geniş pH aralığında dengeli olan GH11 xylanaz klonlaması ve ekspresyonu Abstract: Objective: To clone a full-length cDNA sequence of xynB, encoding endo-1,4-β-xylanase of Aspergillus niger C71 and express in Escherichia coli BL21(DE3).Methods: The xynB was cloned using rapid amplification of cDNA ends (RACE) methods. The sequenced DNA was compared with the available sequences from GenBank using the BLASTX program, and the phylogenetic tree of the xylanases was then constructed using MEGA version 5.0. The amino acid sequences of XYNB were submitted to the ESyPred3D Web Server 1.0 for Homology modeling. The XYNB was purified by MonoQ an ion exchange chromatography and analyzed by SDS-PAGE.Results: The results showed that xynB is 678 bp in length, and encodes a 18 amino acid signal peptide as well as a 22 amino acid mature peptide with a calculated molecular weight of 24.127 kDa. Phylogenetic analysis of xynB, three-dimensional structure and overlap analysis of XYNB demonstrated that XYNB has a β-jelly-roll architecture, which is more conversation in the catalytic domain of GH11 xylanases, belonging to the family 11 of glycosyl hydrolases. A maximum enzyme activity of 62,242.33 U•ml -1 was obtained from XYNB. The XYNB with MW of 41 kDa demonstrated a broad pH stability from pH 3.0 to pH 12. 0.5 mM of Fe 2+ could greatly enhance activity of XYNB to 567.02%. The mainly hydrolysis products of beechwood xylan were xylobiose. The hydrolysis products of XYNB effecting on beechwood xylan were analysed by HPLC.Conclusion: The xynB had been successfully expressed in Escherichia coli BL21, with high enzyme activity and a broad pH stability, and it would be a very good application prospect as the feed enzyme.

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Continuous microbial fuel cell using a photoautotrophic cathode and a fermentative anode

Mitra

Hill

2011

Can J Chem Eng

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A complete microbial fuel cell (MFC) operating under continuous flow conditions and using Chlorella vulgaris at the cathode and Saccharomyces cerevisiae at the anode was investigated for the production of electricity. The MFC was loaded with different resistances to characterise its power capabilities and voltage dynamics. A cell recycle system was also introduced to the cathode to observe the effect of microalgae cell density on steady‐state power production and dynamic voltage profiles. At the maximum microalgae cell density of 2140 mg/L, a maximum power level of 0.6 mW/m2 of electrode surface area was achieved. The voltage difference between the cathode and anode decreased as the resistance decreased within the closed circuit, with a maximum open circuit voltage (infinite resistance) of 220 mV. The highest current flow of 1.0 mA/m2 of electrode surface area was achieved at an applied resistance of 250 Ω.

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Solution scattering studies of conformation stability of xylanase XYNII from Trichoderma longibrachiatum

Cited by 9 publications

References 45 publications

Synchrotron radiation small angle scattering studies of thermal stability of xylanase XYNII from Trichoderma longibrachiatum

Synchrotron radiation small angle scattering studies of thermal stability of xylanase XYNII from Trichoderma longibrachiatum

Cloning and expression of a broad pH stable GH11 xylanase from Aspergillus niger C71 / Aspergillus niger C71 den geniş pH aralığında dengeli olan GH11 xylanaz klonlaması ve ekspresyonu

Continuous microbial fuel cell using a photoautotrophic cathode and a fermentative anode

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