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1.
An extracellular xylanase produced by a Mexican Aspergillus strain was purified and characterized. Aspergillus sp. FP-470 was able to grow and produce extracellular xylanases on birchwood xylan, oat spelt xylan, wheat straw, and corncob, with higher production observed on corncob. The strain also produced enzymes with cellulase, amylase, and pectinase activities on this substrate. A 22-kDa endoxylanase was purified 30-fold. Optimum temperature and pH were 60 degrees C and 5.5, respectively, and isoelectric point was 9.0. The enzyme has good stability from pH 5.0 to 10.0, retaining >80% of its original activity within this range. Half-lives of 150 min at 50 degrees C and 6.5 min at 60 degrees C were found. K(m) and activation energy values were 3.8 mg/mL and 26 kJ/mol, respectively, using birchwood xylan as substrate. The enzyme showed a higher affinity for 4-O-methyl-D-glucuronoxylan with a K(m) of 1.9 mg/mL. The enzyme displayed no activity toward other polysaccharides, including cellulose. Baking trials were conducted using the crude filtrate and purified enzyme. Addition of both preparations improved bread volume. However, addition of purified endoxylanase caused a 30% increase in volume over the crude extract. 相似文献
2.
Terran E. Bergdale Stephen R. Hughes Sookie S. Bang 《Applied biochemistry and biotechnology》2014,172(7):3488-3501
A thermophilic strain, Geobacillus sp. DC3, capable of producing hemicellulolytic enzymes was isolated from the 1.5-km depth of the former Homestake gold mine in Lead, South Dakota. The DC3 strain expressed a high level of extracellular endoxylanase at 39.5 U/mg protein with additional hemicellulases including β-xylosidase (0.209 U/mg) and arabinofuranosidase (0.230 U/mg), after the bacterium was grown in xylan for 24 h. Partially purified DC3 endoxylanase exhibited a molecular mass of approximately 43 kDa according to zymography with an optimal pH of 7 and optimal temperature of 70 °C. The kinetic constants, K m and V max, were 13.8 mg/mL and 77.5 μmol xylose/min·mg xylan, respectively. The endoxylanase was highly stable and maintained 70 % of its original activity after 16 h incubation at 70 °C. The thermostable properties and presence of three different hemicellulases of Geobacillus sp. DC3 strain support its potential application for industrial hydrolysis of renewable biomass such as lignocelluloses. 相似文献
3.
Damaso Mônica C. T. Andrade Carolina M. M. C. Pereira Nei 《Applied biochemistry and biotechnology》2000,84(1-9):821-834
The production of cellulase-free end oxylanase by the thermophilic fungus Thermomyces lanuginosus was investigated insemisolid fermentation and liquid fermentation. Different process variables were investigated in semisolid
fermentation, employing corncobas the carbon source. The best results were with the following conditions: grain size=4.5 mm,
solid:liquid ratio=1:2, and inoculum size=20% (v/v). Corncob, xylan, and xylose were the best inducers for endoxylanase production.
Additionally, organic nitrogen sources were necessary for the production of high endoxylanase activities. The crude enzyme
had optimum activity at pH 6.0 and 75°C, displaying a high thermostability. The apparent K
25 and V
max were 1.77 mg of xylan/mL and 21.5 U/mg of protein, respectively. 相似文献
4.
Javier D. Breccia Nelson Torto Lo Gorton Faustino Siñeriz Rajni Hatti-Kaul 《Applied biochemistry and biotechnology》1998,69(1):31-40
A thermostable xylanase purified from a strain of Bacillus amyloliquefaciens MIR 32 was characterized with respect to its
substrate specificity and mode of hydrolytic action. The enzyme was highly specific for xylans as substrate and displayed
no activity toward other polysaccharides, including cellulose. The enzyme exhibited Km and Vmax of 4.5 mg/mL and 0.58 mmol/min/mg, respectively, with birchwood xylan as the substrate. Microdialysis sampling with anion
exchange chromatography and integrated pulsed electrochemical detection were used for rapid on-line monitoring of products
during hydrolysis of oat spelt and bagasse xylan, and xylooligosaccharides. Xylobiose and xylotriose were the main end products.
Xylotetraose was the smallest oligosaccharide to be acted on by the xylanase. The product pattern confirmed that the enzyme
was an endoxylanase. 相似文献
5.
Selig MJ Knoshaug EP Decker SR Baker JO Himmel ME Adney WS 《Applied biochemistry and biotechnology》2008,146(1-3):57-68
The gene encoding a glycosyl hydrolase family 3 xylan 1,4-beta-xylosidase, xlnD, was successfully cloned from Aspergillus niger strain ATCC 10864. The recombinant product was expressed in Aspergillus awamori, purified by column chromatography, and verified by matrix-assisted laser desorption ionization, tandem time of flight (MALDI-TOF/TOF)
mass spectroscopy of tryptic digests. The T
max was determined using differential scanning microcalorimetry (DSC) to be 78.2 °C; the K
m and k
cat were found to be 255 μM and 13.7 s−1, respectively, using pNP-β-d-xylopyranoside as substrate. End-product inhibition by d-xylose was also verified and shown to be competitive; the K
i for this inhibition was estimated to be 3.3 mM. XlnD was shown to efficiently hydrolyze small xylo-oligomers to monomeric
xylose, making it a critical hydrolytic activity in cases where xylose is to be recovered from biomass conversion processes.
In addition, the presence of the XlnD was shown to synergistically enhance the ability of an endoxylanase, XynA from Thermomyces lanuginosus, to convert xylan present in selected pretreated lignocellulosic substrates. Furthermore, the addition of the XynA/XlnD complex
was effective in enhancing the ability of a simplified cellulase complex to convert glucan present in the substrates. 相似文献
6.
Valquiria B. Damiano Richard Ward Eleni Gomes Heloiza Ferreira Alves-Prado Roberto Da Silva 《Applied biochemistry and biotechnology》2006,129(1-3):289-302
The alkalophilic bacteria Bacillus licheniformis 77-2 produces significant quantities of thermostable cellulase-free xylanases. The crude xylanase was purified to apparent
homogeneity by gel filtration (G-75) and ionic exchange chromatography (carboxymethyl sephadex, Q sepharose, and Mono Q),
resulting in the isolation of two xylanases. The molecular masses of the enzymes were estimated to be 17 kDa (X-I) and 40
kDa (X-II), as determined by SDS-PAGE. The K
m and V
max values were 1.8 mg/mL and 7.05 U/mg protein (X-I), and 1.05 mg/mL and 9.1 U/mg protein (X-II). The xylanases demonstrated
optimum activity at pH 7.0 and 8.0–10.0 for xylanase X-I and X-II, respectively, and, retained more than 75% of hydrolytic
activity up to pH 11.0. The purified enzymes were most active at 70 and 75°C for X-I and X-II, respectively, and, retained
more than 90% of hydrolytic activity after 1 h of heating at 50°C and 60°C for X-I and X-II, respectively. The predominant
products of xylan hydrolysates indicated that these enzymes were endoxylanases. 相似文献
7.
Dengeti Shrinivas Gunashekaran Savitha Kumar Raviranjan Gajanan Ramchandra Naik 《Applied biochemistry and biotechnology》2010,162(7):2049-2057
A highly thermostable alkaline xylanase was purified to homogeneity from culture supernatant of Bacillus sp. JB 99 using DEAE-Sepharose and Sephadex G-100 gel filtration with 25.7-fold increase in activity and 43.5% recovery.
The molecular weight of the purified xylanase was found to be 20 kDA by SDS-PAGE and zymogram analysis. The enzyme was optimally
active at 70 °C, pH 8.0 and stable over pH range of 6.0–10.0.The relative activity at 9.0 and 10.0 were 90% and 85% of that
of pH 8.0, respectively. The enzyme showed high thermal stability at 60 °C with 95% of its activity after 5 h. The K
m and V
max of enzyme for oat spelt xylan were 4.8 mg/ml and 218.6 μM min−1 mg−1, respectively. Analysis of N-terminal amino acid sequence revealed that the xylanase belongs to glycosyl hydrolase family
11 from thermoalkalophilic Bacillus sp. with basic pI. Substrate specificity showed a high activity on xylan-containing substrate and cellulase-free nature. The hydrolyzed product
pattern of oat spelt xylan on thin-layer chromatography suggested xylanase as an endoxylanase. Due to these properties, xylanase
from Bacillus sp. JB 99 was found to be highly compatible for paper and pulp industry. 相似文献
8.
A psychrotrophic fungus identified as Trichoderma sp. SC9 produced 36.7 U/ml of xylanase when grown on a medium containing corncob xylan at 20 °C for 6 days. The xylanase
was purified 37-fold with a recovery yield of 8.2%. The purified xylanase appeared as a single protein band on SDS-PAGE with
a molecular mass of approximately 20.5 kDa. The enzyme had an optimal pH of 6.0, and was stable over pH 3.5–9.0. The optimal
temperature of the xylanase was 42.5 °C and it was stable up to 35 °C at pH 6.0 for 30 min. The xylanase was thermolabile
with a half-life of 23.9 min at 45 °C. The apparent K
m
values of the xylanase for birchwood, beechwood, and oat-spelt xylans were found to be 3, 2.1, and 16 mg/ml respectively.
The xylanase hydrolyzed beechwood xylan and birchwood xylan to yield mainly xylobiose as end products. The enzyme-hydrolysed
xylotriose, xylotetraose, and xylopentose to produce xylobiose, but it hardly hydrolysed xylobiose. A xylanase gene (xynA) with an open reading frame of 669 nucleotide base pairs (bp), encoding 222 amino acids, from the strain was cloned and sequenced.
The deduced amino acid sequence of XynA showed 85% homology with Xyn2 from a mesophilic strain of Trichoderma viride. 相似文献
9.
An extracellular exoinulinase was purified from the crude extract of Aspergillus fumigatus by ammonium sulfate precipitation, followed by successive chromatographies on DEAE-Sephacel, Sephacryl S-200, concanavalin
A-linked amino-activated silica, and Sepharose 6B columns. The enzyme was purified 25-fold, and the specific activity of the
purified enzyme was 171 IU/mg of protein. Gel filtration chromatography revealed a molecular weight of about 200 kDa, and
native polyacrylamide gel electrophoresis (PAGE) showed an electrophoretic mobility corresponding to a molecular weight of
about 176.5 kDa. Sodium dodecyl sulfate-PAGE analysis revealed three closely moving bands of about 66, 62.7, and 59.4 kDa,
thus indicating the heterotrimeric nature of this enzyme. The purified enzyme appeared as a single band on isoelectric focusing,
with a pI of about 8.8. The enzyme activity was maximum at pH 5.5 and was stable over a pH range of 4.0–9.5, and the optimum temperature
for enzyme activity was 60°C. The purified enzyme retained 35.9 and 25.8% activities after 4 h at 50 and 55°C, respectively.
The inulin hydrolysis activity was completely abolished with 1 mM Hg++, whereas EDTA inhibited about 63% activity. As compared to sucrose, stachyose, and raffinose, the purified enzyme had lower
K
m
(0.25 mM) and higher V
max (333.3 IU/mg) values for inulin. 相似文献
10.
Jeffrey A. Mertens Jay D. Braker Douglas B. Jordan 《Applied biochemistry and biotechnology》2010,162(8):2415-2213
Catalytic properties of two glucoamylases, AmyC and AmyD, without starch binding domains from Rhizopus oryzae strain 99-880 are determined using heterologously expressed enzyme purified to homogeneity. AmyC and AmyD demonstrate pH
optima of 5.5 and 6.0, respectively, nearly one unit higher than the Rhizopus AmyA glucoamylase enzyme. Optimal initial activities are at 60 and 50 °C for AmyC and AmyD, respectively. Inactivation of
both enzymes occurs at 50 °C following 30 min pre-incubation. The two enzymes demonstrate substantially slower catalytic rates
toward soluble starch relative to AmyA. AmyC has similar k
cat and K
m for oligosaccharides to other Rhizopus and Aspergillus glucoamylases; however, the enzyme has a 2-fold lower K
mmaltose. AmyD has a 3-fold higher K
m and lower k
cat for maltooligosaccharides than AmyC and other glucoamylases. AmyC (but not AmyD) exhibits substrate inhibition. K
i for substrate inhibition decreases with increasing length of the oligosaccharides. Data from pre-steady-state binding of
AmyC to maltose and maltotriose and pre-steady-state to steady-state catalytic turnover experiments of AmyC acting on maltotriose
were used to interrogate models of substrate inhibition. In the preferred model, AmyC accumulates an enzyme-maltose-maltotriose
dead-end complex in the steady state. 相似文献
11.
Rey MW Brown KM Golightly EJ Fuglsang CC Nielsen BR Hendriksen HV Butterworth A Xu F 《Applied biochemistry and biotechnology》2003,111(3):153-166
Thielavia terrestris is a soil-borne thermophilic fungus whose molecular/cellular biology is poorly understood. Only a few genes have been cloned
from the Thielavia genus. We detected an extracellular glucoamylase in culture filtrates of T. terrestris and cloned the corresponding glaA gene. The coding region contains five introns. Based on the amino acid sequence, the glucoamylase was 65% identical to Neurospora crassa glucoamylase. Sequence comparisons suggested that the enzyme belongs to the glycosyl hydrolase family 15. The T. terrestris glaA gene was expressed in Aspergillus oryzae under the control of an A. oryzae α-amylase promoter and an Aspergillus niger glucoamylase terminator. The 75-kDa recombinant glucoamylase showed a specific activity of 2.8 μmol/(min·mg) with maltose
as substrate. With maltotriose as a substrate, the enzyme had an optimum pH of 4.0 and an optimum temperature of 60°C. The
enzyme was stable at 60°C for 30 min. The K
m
and k
cat
of the enzyme for maltotriose were determined at various pHs and temperatures. At 20°C and pH 4.0, the enzyme had a K
m
of 0.33±0.07 mM and a k
cat
of (5.5±0.5)×103 min−1 for maltotriose. The temperature dependence of k
cat
/K
m
indicated an activation free energy of 2.8 kJ/mol across the range of 20–70°C. Overall, the enzyme derived from the thermophilic
fungus exhibited properties comparable with that of its homolog derived from mesophilic fungi. 相似文献
12.
Wanzeng Ren Feng Zhang Xinyi Yang Shukun Tang Hong Ming Enmin Zhou Yirui Yin Yuanming Zhang Wenjun Li 《Cellulose (London, England)》2013,20(4):1947-1955
An extracellular xylanase from halophilic Streptomonospora sp. YIM 90494 was purified to homogeneity from a fermentation broth by ammonium sulphate precipitation, gel filtration chromatography and ion exchange chromatography. The purified xylanase appeared as a single protein band on SDS-PAGE with a molecular mass of approximately 50 kDa. The xylanase had maximum activity at pH 7.5 and 55 °C. The enzyme was stable over a broad pH range (pH 4.0–10.0) and showed good thermal stability when being incubated at 60 °C for 2 h. Kinetic experiments indicated that the enzyme had K m and V max values of 19.24 mg/mL and 6.1 μmol/min/mg, respectively, using birch wood xylan as substrate. The inhibitory effects of various metal ions and chemical agents on the xylanase activity were investigated. It is greatly interesting to note that Ag+ ion and SDS, which strongly inhibited most xylanases reported previously increases the xylanase activity in this study. These characteristics suggest that the enzyme with new properties has considerable potential in industrial applications. 相似文献
13.
Taibi Z Saoudi B Boudelaa M Trigui H Belghith H Gargouri A Ladjama A 《Applied biochemistry and biotechnology》2012,166(3):663-679
An extracellular thermostable xylanase from a newly isolated thermophilic Actinomadura sp. strain Cpt20 was purified and characterized. Based on matrix-assisted laser desorption–ionization time-of-flight mass
spectrometry analysis, the purified enzyme is a monomer with a molecular mass of 20,110.13 Da. The 19 residue N-terminal sequence
of the enzyme showed 84% homology with those of actinomycete endoxylanases. The optimum pH and temperature values for xylanase
activity were pH 10 and 80 °C, respectively. This xylanase was stable within a pH range of 5–10 and up to a temperature of
90 °C. It showed high thermostability at 60 °C for 5 days and half-life times at 90 °C and 100 °C were 2 and 1 h, respectively.
The xylanase was specific for xylans, showing higher specific activity on soluble oat-spelt xylan followed by beechwood xylan.
This enzyme obeyed the Michaelis–Menten kinetics, with the K
m and k
cat values being 1.55 mg soluble oat-spelt xylan/ml and 388 min−1, respectively. While the xylanase from Actinomadura sp. Cpt20 was activated by Mn2+, Ca2+, and Cu2+, it was, strongly inhibited by Hg2+, Zn2+, and Ba2+. These properties make this enzyme a potential candidate for future use in biotechnological applications particularly in
the pulp and paper industry. 相似文献
14.
Sangeeta Yadav Pramod Kumar Yadav Dinesh Yadav Kapil Deo Singh Yadav 《Applied biochemistry and biotechnology》2009,159(1):270-283
An indigenously isolated fungal strain identified as Aspergillus terricola with assigned fungal strain number MTCC 7588 has been used as source for pectin lyase production. The extracellular pectin
lyase was purified to homogeneity from the culture filtrate of A. terricola by ion exchange and gel filtration chromatography. The determined molecular weight was 35 ± 01 kDa. The K
m and k
cat (turnover) values of the purified enzyme at 37 °C using citrus pectin as the substrate were found to be 1.0 mg/ml and 110.0 s−1, respectively. The pH and temperature optima of the enzyme were 8.0 and 50 °C, respectively. The retting ability of the purified
pectin lyase for natural fibers viz. Cannabis sativa and Linum usitatissimum has been demonstrated for the first time. 相似文献
15.
The gene encoding a glycoside hydrolase family 39 xylosidase (BH1068) from the alkaliphile Bacillus halodurans strain C-125 was cloned with a C-terminal His-tag, and the recombinant gene product termed BH1068(His)6 was expressed in Escherichia coli. Of the artificial substrates tested, BH1068(His)6 hydrolyzed nitrophenyl derivatives of β-d-xylopyranose, α-l-arabinofuranose, and α-l-arabinopyranose. Deviation from Michaelis−Menten kinetics at higher substrate concentrations indicative of transglycosylation
was observed, and k
cat and K
m values were measured at both low and high substrate concentrations to illuminate the relative propensities to proceed along
this alternate reaction pathway. The pH maximum was 6.5, and under the conditions tested, maximal activity was at 47°C, and
thermal instability occurred above 45°C. BH1068(His)6 was inactive on arabinan, hydrolyzed xylooligosaccharides, and released only xylose from oat, wheat, rye, beech, and birch
arabinoxylan, and thus, can be classified as a xylosidase with respect to natural substrate specificity. The enzyme was not
inhibited by up to 200 mM xylose. The oligomerization state was tetrameric under the size-exclusion chromatography conditions
employed. 相似文献
16.
Sucharita Sen Lalitagauri Ray Parimal Chattopadhyay 《Applied biochemistry and biotechnology》2012,167(7):1938-1953
A fungal strain isolated from rotten banana and identified as Aspergillus alliaceus was found capable of producing thermostable extracellular ??-galactosidase enzyme. Optimum cultural conditions for ??-galactosidase production by A. alliaceus were as follows: pH?4.5; temperature, 30?°C; inoculum age, 25?h; and fermentation time, 144?h. Optimum temperature, time, and pH for enzyme substrate reaction were found to be 45?°C, 20?min, and 7.2, respectively, for crude and partially purified enzyme. For immobilized enzyme?Csubstrate reaction, these three variable, temperature, time, and pH were optimized at 50?°C, 40?min, and 7.2, respectively. Glucose was found to inhibit the enzyme activity. The K m values of partially purified and immobilized enzymes were 170 and 210?mM, respectively. Immobilized enzyme retained 43?% of the ??-galactosidase activity of partially purified enzyme. There was no significant loss of activity on storage of immobilized beads at 4?°C for 28?days. Immobilized enzyme retained 90?% of the initial activity after being used four times. 相似文献
17.
M. Costa-Ferreira A. Dias C. Maximo M. J. Morgado G. Sena-Martins J. Cardoso Duarte 《Applied biochemistry and biotechnology》1994,44(3):231-242
Production of xylanolytic enzymes by anAspergillus niger CCMI 850 isolate was investigated in batch cultures. The effect of the composition of a fermentation medium that did not
include chemical inducers, on β-xylanase, β-xylosidase, α-l-arabinofuranosidase, and total cellulase activity was studied. With 4% xylan as the carbon source, about 65 U/mL of β-xylanase
was obtained, whereas the total cellulase activity was undetectable, under the specified conditions. This β-xylanase activity
represents the highest reported for a wild-type strain ofA. niger. The effect of pH and temperature on the activity of β-xylanase was studied. Partial characterization of the β-xylanase showed
that with insoluble birchwood as substrate theK
m
andV
max were 0.3 mM and 19 μmol/min, respectively. Aspects of using the crude β-xylanase preparation for applications in the pulp and paper industry
were discussed. 相似文献
18.
To obtain extracellular and high-level expression of the Dictyoglomus thermophilum Rt46B.1 xylanase B gene, this gene was integrated into the α-amylase gene site of a host strain of Bacillus subtilis WB800. The extreme thermophile xylanase gene was successfully integrated and expressed in the host, measured at 24 ± 0.4 XUs/mL
in the Luria broth medium supernatant. The recombinant enzyme was purified by ammonium sulfate precipitation, anion exchange
chromatography, and gel filtration. The molecular mass and pI value of xylanase were estimated to be 24 kDa and 4.3, respectively. The optimal pH level and temperature of the purified
enzyme were 6.5 and 85 °C, respectively. Xylanase showed reasonable activity at temperatures up to 95 °C and remained stable
at 4 °C for 1 week. The purified enzyme retained most of its activity in 1 mM ethylenediaminetetraacetic acid or dithiothreitol
and 0.1% Tween-20 or Triton X-100. However, strong inhibition was observed in the presence of 5 mM Mn2+, 0.5% sodium dodecyl sulfate, Tween-20, or Triton X-100; a strong stimulating effect was also observed in the presence of
Fe2+. The K
m and V
max values of the recombinant xylanase for birchwood xylan were calculated to be 2.417 ± 0.36 mg/mL and 325 ± 41 μmol/min mg,
respectively. Xylanase was found to be useful in the prebleaching process of paper pulps. 相似文献
19.
Carvalho Andrade Carolina M. M. Aguiar Wilson Bucker Antranikian Garo 《Applied biochemistry and biotechnology》2001,91(1-9):655-669
Xylanases (EC3.2.1.8) catalyze the hydrolysis of xylan, the major constituent of hemicellulose. The use of these enzymes could
greatly improve the overall economics of processing lignocellulosic materials for the generation of liquid fuels and chemicals.
The hyperthermophilic archaeon Pyrodictium abyssi, which was originally isolated from marine hot abyssal sites, grows optimally at 97°C and is a prospective source of highly
thermostable xylanase. Its endoxylanase was shown to be highly thermostable (over 100 m in at 105°C) and active even at 110°C.
The growth of the deep-sea archaeon P. abyssi was investigated using different culture techniques. Among the carbohydrates used, beech wood xylan, birch wood glucuronoxylan
and the arabinoxylan from oats pelt appeared to be good inducers for endoxylanase and β-xylosidase production. The highest
production of arabinofuranosidase, however, was detected in the cell extracts after growth on xylose and pyruvate, indicating
that the intermediate of the tricarboxylic acid cycle acted as a nonrepressing carbon source for the production of thi enzyme.
Electron microscopic studies did not show a significant difference in the cell surface (e.g., xylanosomes) when P. abyssi cells were grown on different carbohydrates. The main kinetic parameters of the organism have been determined. The cell yield
was shown to be very low owing to incomplete substrate utilization, but a very high maximal specific growth rate was determined
(μmax=0.0195) at 90°C and pH 6.0. We also give information on the problems that arise during the fermentation of this hyperthermophilic
archaeon at elevated temperatures. 相似文献
20.
Maalej I Belhaj I Masmoudi NF Belghith H 《Applied biochemistry and biotechnology》2009,158(1):200-212
A thermostable xylanase from a newly isolated thermophilic fungus Talaromyces thermophilus was purified and characterized. The enzyme was purified to homogeneity by ammonium sulfate precipitation, diethylaminoethyl
cellulose anion exchange chromatography, P-100 gel filtration, and Mono Q chromatography with a 23-fold increase in specific
activity and 17.5% recovery. The molecular weight of the xylanase was estimated to be 25kDa by sodium dodecyl sulfate–polyacrylamide
gel electrophoresis and gel filtration. The enzyme was highly active over a wide range of pH from 4.0 to 10.0. The relative
activities at pH5.0, 9.0, and 10.0 were about 80%, 85.0%, and 60% of that at pH7.5, respectively. The optimum temperature
of the purified enzyme was 75°C. The enzyme showed high thermal stability at 50°C (7days) and the half-life of the xylanase
at 100°C was 60min. The enzyme was free from cellulase activity. K
m and V
max values at 50°C of the purified enzyme for birchwood xylan were 22.51mg/ml and 1.235μmol min−1 mg−1, respectively. The enzyme was activated by Ag+, Co2+, and Cu2+; on the other hand, Hg2+, Ba2+, and Mn2+ inhibited the enzyme. The present study is among the first works to examine and describe a secreted, cellulase-free, and
highly thermostable xylanase from the T. thermophilus fungus whose application as a pre-bleaching aid is of apparent importance for pulp and paper industries. 相似文献