3.2.1.8: endo-1,4-beta-xylanase
This is an abbreviated version!
For detailed information about endo-1,4-beta-xylanase, go to the full flat file.
Word Map on EC 3.2.1.8
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3.2.1.8
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xylans
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xylanases
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xylose
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arabinoxylans
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trichoderma
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xylooligosaccharides
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reesei
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xylotriose
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xylanolytic
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birchwood
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spelt
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cellulases
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straw
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carbohydrate-binding
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lignocellulosic
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beta-xylosidase
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xylotetraose
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bran
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hemicellulases
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lanuginosus
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thermomyces
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corncob
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arabinofuranosidase
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bagasse
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cellobiohydrolase
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alpha-l-arabinofuranosidase
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cellulomonas
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saccharification
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cellulose-binding
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avicel
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thermoascus
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degradation
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agriculture
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cellulosome
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paper production
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glucuronoxylans
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lignocellulolytic
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endo-1,4-beta-glucanase
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halodurans
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arabinan
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industry
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xylosidase
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biofuel production
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breadmaking
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analysis
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hemicellulolytic
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nutrition
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cellulolyticus
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longibrachiatum
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taxi
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food industry
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synthesis
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kraft
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biotechnology
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biobleaching
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cellulase-free
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neocallimastix
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water-extractable
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cellulosa
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dockerin
- 3.2.1.8
- xylans
- xylanases
- xylose
- arabinoxylans
- trichoderma
- xylooligosaccharides
- reesei
- xylotriose
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xylanolytic
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birchwood
- spelt
- cellulases
- straw
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carbohydrate-binding
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lignocellulosic
- beta-xylosidase
- xylotetraose
- bran
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hemicellulases
- lanuginosus
- thermomyces
- corncob
- arabinofuranosidase
- bagasse
- cellobiohydrolase
- alpha-l-arabinofuranosidase
- cellulomonas
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saccharification
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cellulose-binding
- avicel
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thermoascus
- degradation
- agriculture
- cellulosome
- paper production
- glucuronoxylans
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lignocellulolytic
- endo-1,4-beta-glucanase
- halodurans
- arabinan
- industry
- xylosidase
- biofuel production
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breadmaking
- analysis
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hemicellulolytic
- nutrition
- cellulolyticus
- longibrachiatum
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taxi
- food industry
- synthesis
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kraft
- biotechnology
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biobleaching
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cellulase-free
- neocallimastix
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water-extractable
- cellulosa
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dockerin
Reaction
Synonyms
(1--> 4)-beta-xylan 4-xylanohydrolase, (1-4)-beta-xylan 4-xylanohydrolase, 1,4-beta-D-xylan xylanohydrolase, 1,4-beta-D-xylan xylanohydrolase 22, 1,4-beta-D-xylan-xylanohydrolase, 1,4-beta-xylan xylanohydrolase, 1,4-beta-xylanase, 34 kDa xylanase, Abf51A, Abf62A-Axe6A, Acel_0180, acidophilic endo-1,4-beta-xylanase, AfXynA, AfXynB, alkaline active xylanase, alkaline xylanase, AMX-4 xylanase, AnxB, AxB8, Axy43A, basic xylanase, Bcx, beta-1, 4-endoxylanase, beta-1,4-D-xylanase, beta-1,4-endoxylanase, beta-1,4-xylan hydrolase, beta-1,4-xylan xylanohydrolase, beta-1,4-xylanase, beta-1,4endoxylanase, beta-D-xylanase, beta-endoxylanase, beta-xylanase, bifunctional cellulase/xylanase, bifunctional endoglucanase/xylanase, bifunctional xylanase/endoglucanase, BlxA, BSX, BSXY, Btx, Calow_0124, ctendo7, Cthe_3012, CTHT_0045780, CtXynGH30, EGXA, endo(1-4)beta-xylanase, endo-(1,4)-beta-xylanase, endo-(1--> 4)-beta-xylanase, endo-1,4-beta-D-xylanase, endo-1,4-beta-xylanase, endo-1,4-beta-xylanase II, endo-1,4-xylanase, endo-acting beta-1,4-xylanase, endo-beta-(1'4)-xylanase, endo-beta-(1,4)-xylanase, endo-beta-1, 4-xylanase, endo-beta-1,4-xylanase, endo-beta-1,4-xylanase 2, endo-beta-1,4-xylanase2, endo-xylanase, endoxylanase, endoxylanase I, endoxylanase NtSymX11, endoxylanase Xys1DELTA, EXY1, family 11 endoxylanase, family 11 xylanase, family 30 glycoside hydrolase subfamily 8 glucuronoxylan endo-beta-1,4-xylanase, family-10 endo-1,4-beta-xylanase, FIA-xylanase, FOTG_15646, G/11 endo-1,4-beta-xylanase, GC25 xylanase, GH 10 xylanase, GH 11 xylanase, GH-10 endo-1,4-beta-xylanase, GH-11 endo-1,4-beta-xylanase, GH10 endo-beta-1,4-xylanase, GH10 xylanase D, GH11 xylanase, GH43B6, GH7 endoglucanase, GHF 10 endoxylanase, GHF 11 endoxylanase, glycoside hydrolase family 11 endoxylanase, glycoside hydrolase family 8 domain protein, GXYN, KRICT PX1, MalAC0309_0409, More, MROS_2090, MROS_2091, MROS_2495, Mxyn10, MYCTH_49824, MYCTH_56237, ORF4, Pedsa_2704, PhX20, PhX33, PsGH10A, pXyl, RrXyn11A, RuCelA, Rut C-30, SCO5931, SipoEnXyn10A, SlxB, SoxB, SSO1354 protein, TAXI, TERTU_4506, Tfu_1213, TLX, TmxB, Tpet_0854, TRX II, TtGH8, Wxl1, X-I, X-II, X34, Xa, Xln-1, xlnA, xlnB, XT6, Xyl, Xyl I, Xyl II, XYL1, Xyl10A, Xyl10B, XYL10C, Xyl11, XYL1p, XYL2, Xyl2090, Xyl2091, Xyl2495, Xyl30, XYLA, xylanase, xylanase 1, xylanase 10A, xylanase 10B, xylanase 10C, xylanase 11 A, xylanase 11A, xylanase 11J, xylanase 2, Xylanase 22, xylanase 43A, xylanase A, xylanase B, xylanase bI, xylanase bII, xylanase C, xylanase I, xylanase II, xylanase III, xylanase J, xylanase LC9, xylanase Xyl10A, xylanase Xyl11A, xylanase XynZF-2, xylanase, endo-1,4-, XylB, XylB8, XylC, XYLD, XylE, XylF2, XylG, xylH, xylM, XylX, XYLY, Xyn II, Xyn III, Xyn-b39, Xyn-Lxy, Xyn1, Xyn10, Xyn10A, Xyn10B, Xyn10E, XYN10G5, XYN10Ks_480, Xyn11, Xyn11A, XYN11F63, XYN11Ks_480, Xyn11NX, Xyn12.2, Xyn162, Xyn2, Xyn3, Xyn30A, Xyn5, XynA, XynA119, XynA19, XynA4, XynAS27, XynAS9, XynB, XynB18, XynBS27, XynC, XynD, XynE15, XynE2, XynG1, XynGH30, XynGR40, XYNII, XynIII, XynJ, XynS14, XynS20, XynSW1, XynSW3, XynT, XynY, XynZ, Xys1, Xys1delta, xysA
ECTree
3.2.1.8 endo-1,4-beta-xylanaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.2.1.8 - endo-1,4-beta-xylanase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E337A
capture of the substrate xylohexaose in the inactivated site
D60N
-
site-directed mutagenesis, the mutant shows an increased pH optimum and over 90% reduced specific activity compared to the wild-type enzyme
D60N/E141A
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site-directed mutagenesis, the mutant shows an increased pH optimum and over 90% reduced specific activity compared to the wild-type enzyme
D60N/Y35W
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site-directed mutagenesis, the mutant shows an increased pH optimum and over 90% reduced specific activity compared to the wild-type enzyme
E141A
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site-directed mutagenesis, the mutant shows an increased pH optimum, slightly reduced thermostability, 50% increase in specific activity at pH 4.0, and an overall increased catalytic efficiency compared to the wild-type enzyme
Y35W
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site-directed mutagenesis, the mutant shows an increased pH optimum and 64% reduced specific activity compared to the wild-type enzyme
Y35W/E141A
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site-directed mutagenesis, the mutant shows an increased pH optimum and 46% reduced specific activity compared to the wild-type enzyme
Q47P/S159R
increase in thermostability and in optimum temperature
T16A/T39I/L176Q
increase in thermostabilityand in optimum temperature
Q127E
-
specific activity is lower than 5% compared to the wild type enzyme
Q127L
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specific activity is lower than 5% compared to the wild type enzyme
T11Y/N12H/N13D/F15Y/F16F
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the mutation increases the enzyme's thermostability
T205C/A52C
the optimum temperature of the mutant enzyme is improved from 45°C to 60°C, and it retains greater than 90.0% activity (wild-type enzyme retains only 50.0% activity) after treatment at 50°C for 85 min. The optimum pH of mutant xylanase is similar to wild-type enzyme (pH 5.0). The pH stability span (5.0-7.0) of the wild-type enzyme is increased to 3.0-9.0 for the mutant enzyme
W9Y
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mutant enzyme is insensitive for Triticum aestivum xylanase inhibitor-II
W9Y/N35D
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increased sensitivity to Triticum aestivum xylanase inhibitor-I and insensitive for Triticum aestivum xylanase inhibitor-II
T11Y/N12H/N13D/F15Y/F16F
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the mutation increases the enzyme's thermostability
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D11F/R122D
the mutant shows highly decreased sensitivity to inhibitor Triticum aestivum xylanase inhibitor compared to wild-type enzyme
F48C
-
mutation increases the half-inactivation temperature by 2-3°C over that of the wild type enzyme
G23R
construction of a XynA mutant with increased pH stability, Computational design-based molecular engineering, overview
Q175K
construction of a XynA mutant with increased pH stability, Computational design-based molecular engineering, overview
T10H
construction of a XynA mutant with increased pH stability, Computational design-based molecular engineering, overview
T44C
-
mutation increases the half-inactivation temperature by 2-3°C over that of the wild type enzyme
T44Y
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mutation increases the half-inactivation temperature by 2-3°C over that of the wild type enzyme
T87D
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mutation increases the half-inactivation temperature by 2-3°C over that of the wild type enzyme
W9H
construction of a XynA mutant with increased pH stability, Computational design-based molecular engineering, overview
Y94C
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mutation increases the half-inactivation temperature by 2-3°C over that of the wild type enzyme
N62D
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XylB mutant with inhibition specificity similar to the wild type enzyme and lower pH optimum
N65D
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XylA mutant with inhibition specificity similar to the wild type enzyme and lower pH optimum
Q144N
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XylA mutant with inhibition specificity similar to the wild type enzyme
S100C/N150C
V169A/I170F/D171N
N38Y/F52W/G56Y/G201L
increase in melting temperature by 14 degrees
D101N/G103F/R132A/R136A
site-directed mutagenesis, the mutant is expressed in inclusion bodies
F48Y
site-directed mutagenesis, the mutant shows increased thermostability and activity compared to the wild-type enzyme
F48Y/R49A/T50V/T147L
site-directed mutagenesis, the half-life of the mutant is 4fold increased compared to the wild-type enzyme
F48Y/T147L
site-directed mutagenesis, the half-life of the mutant is 7.5fold increased compared to the wild-type enzyme
F48Y/T50V
site-directed mutagenesis, the half-life of the mutant is increased compared to the wild-type enzyme
F48Y/T50V/T147L
site-directed mutagenesis, the half-life of the mutant is 15fold increased compared to the wild-type enzyme
G103F
site-directed mutagenesis, the mutation introduced a bulky hydrophobic residue causing a clash with the neighbouring residues that results in destabilization
T147L
site-directed mutagenesis, the mutant shows increased thermostability and activity compared to the wild-type enzyme
T50V
site-directed mutagenesis, the mutant shows increased thermostability and activity compared to the wild-type enzyme
T50V/T147L
site-directed mutagenesis, the half-life of the mutant is increased compared to the wild-type enzyme
Y69F
the barrier for conversion of the 4C1 chair to the more-stable 2,5B boat in the wild-type enzyme-substrate complex is significantly lower than it is for the mutant. The mutation reduces the degree of oxacarbenium-ion character in the proximal xylose ring of the enzyme-substrate complex
E129A/E236A
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the naturally occuring enzyme mutant XynBE18 shows also beta-1,3-1,4-glucan hydrolase activity, EC 3.2.1.6. Recombinant XynBE18 shows specificity toward oat spelt xylan and birchwood xylan and barley beta-1,3-1,4-glucan and lichenin, no activity with carboxymethylcellulose or Avicel, overview
K131S/K132S
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site-directed mutagenesis, with or without deletion mutation DELTAP130, the mutant without deletion shows no sensitivity to inhibitor XIP-1, like the wild-type enzyme, but shows increased activity compared to the wild-type, the mutant with deletion mutation is sensitive to inhibitor XIP-1
Q121R
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shows a marked 33% increase in specific activity, mainly due to a 2fold increase in kcat. It does not alter the hydrolysis product profile of wheat arabinoxylan, shows highest increase in activity on low substituted xylan
S44A
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loses both pH-dependence profile and activity, reduces activity mainly due to a reduction in kcat whereas the apparent affinity remains unchanged
S44D
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shows only slight alteration in Km and Vmax, reduces activity mainly due to a reduction in kcat whereas the apparent affinity remains unchanged. It shifts the activity to acidic pHs by ca. 1 unit, decreasing the optimum pH to 4.5. It has a broader pH profile retaining ca. 60% of its maximum activity at pH 3.0 as compared to the wild-type
S44N
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shows only slight alteration in Km and Vmax, reduces activity mainly due to a reduction in kcat whereas the apparent affinity remains unchanged. It shifts the activity to alkaline pHs by ca. 0.5 unit with a pH optimum of 5.5
biofuel production
E128H
-
inhibits the breakdown of the glycosyl-enzyme intermediate. Restoration of the breakdown activity of the mutant by adding exogenous nucleophiles, such as sodium azide, results in a mutant that acts as a switching enzyme with azide
G23A/G24P/S26T
-
the mutation increases the enzyme's thermostability
T11Y/N12H/N13D/F15Y/F16F
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the mutation increases the enzyme's thermostability
T30E/N32G/S33P
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the mutation increases the enzyme's thermostability
V3A/I4V/T6S/Q8E
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the mutation increases the enzyme's thermostability
E128H
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inhibits the breakdown of the glycosyl-enzyme intermediate. Restoration of the breakdown activity of the mutant by adding exogenous nucleophiles, such as sodium azide, results in a mutant that acts as a switching enzyme with azide
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D65P
98% of wild-type activity, decrease in melting temperature
D65P/N66G
102% of wild-type activity, increase in melting temperature
N44H
101%% of wild-type activity, decrease in melting temperature
N63L
85% of wild-type activity, decrease in melting temperature
N66G
100% of wild-type activity, decrease in melting temperature
S102N
100%% of wild-type activity, increase in melting temperature
S35C
101% % of wild-type activity, decrease in melting temperature
S35C/N44H/Y61M/T62C/N63L/D65P/N66G/T101P/S102N
114% of wild-type activity, 20 degrees increase in melting temperature
S35C/T62C
97%% of wild-type activity, increase in melting temperature
T62C
86%% of wild-type activity, decrease in melting temperature
Y61M
94% of wild-type activity, decrease in melting temperature
Y61M/N63L
109% of wild-type activity, decrease in melting temperature
N44H
Talaromyces pinophilus CF-2612
-
101%% of wild-type activity, decrease in melting temperature
-
S35C
Talaromyces pinophilus CF-2612
-
101% % of wild-type activity, decrease in melting temperature
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D281N
H209N
-
mutant shows increased thermostability relative to the wild type at 70°C and 75°C and is stable in the pH range 8.0-10.0, similar to wild-type
N257D
-
mutant shows increased thermostability relative to the wild type at 70°C and 75°C and is stable in the pH range 5.0-10.0
Q158R
-
mutant shows increased thermostability relative to the wild type at 70°C and 75°C and is stable in the pH range 5.0-10.0,
H209N
-
mutant shows increased thermostability relative to the wild type at 70°C and 75°C and is stable in the pH range 8.0-10.0, similar to wild-type
-
N257D
-
mutant shows increased thermostability relative to the wild type at 70°C and 75°C and is stable in the pH range 5.0-10.0
-
Q158R
-
mutant shows increased thermostability relative to the wild type at 70°C and 75°C and is stable in the pH range 5.0-10.0,
-
G25P
-
mainly leads to increase in alkaline pH stability without improving the specific activity
I91T
-
results in the main contribution to catalytic activity rather than alkaline pH stability
T11Y/N12H/N13D/F15Y/F16F
-
the mutation increases the enzyme's thermostability
T21A
-
mainly leads to increase in alkaline pH stability without improving the specific activity
T21A/G25P/V87P/J91T/G217L
-
mutant 2TfxA98, with approximately 12fold increased kcat/Km and 4.5fold decreased Km compared with its parent. Mutant 2TfxA98 inherits its thermostability from parent TfxA and enhances its alkaline pH stability through DNA shuffling. 2Tfx98 has significantly improved catalytic activities in performing the xylan hydrolysis. It is most active at 75°C, almost the same as the parental TfxA, but 2TfxA98 produces 1.9 times more reducing sugar than TfxA at 75°C of pH 9.0
A54T
-
when exposed to 80°C for 90 min the mutant displays a low stability and retains only 10% of its activity. It is extremely alkali tolerant. After 90 min at pH 10 it retains 93% of its activity. It has catalytic activity almost comparable to the wild-type
K30E/W40R/T57A/K80R
-
thermostable mutant, when exposed to 80°C for 90 min it displays 75% retention of its total activity. The mutant loses nearly 60% of its activity under extremely alkaline conditions (after 90 min at pH 10). It has a much lower activity as compared to the wild-type
Q1C/Q24C
F180Q/H144C/N92C
increased resistance towards thermal inactivation at alkaline pH
H144C/N92C
increased resistance towards thermal inactivation at alkaline pH
H22K/F180Q/H144C/N92C
increased resistance towards thermal inactivation at alkaline pH
K58R
site-directed mutagenesis, slight increase of thermostability at 55°C from half-life 5 min, wild-type, to 10-20 min, increased pH-stability compared to the wild-type enzyme
K58R/A160R
site-directed mutagenesis, no alteration of thermal or pH-stability
K58R/A160R/N97R
site-directed mutagenesis, no alteration of thermal or pH-stability
K58R/A160R/N97R/N67R
site-directed mutagenesis, no alteration of thermal or pH-stability
K58R/A160R/N97R/N67R/T26R
site-directed mutagenesis, no alteration of thermal or pH-stability
K58R/A160R/N97R/N67R/T26R/A132R
site-directed mutagenesis, no alteration of thermal or pH-stability
N11D
-
site-directed mutagenesis, increase of half-life to about 100 min at 65°C
N38E
-
site-directed mutagenesis, increase of half-life to about 100 min at 65°C
N97R/F93W/H144K
increased resistance towards thermal inactivation at alkaline pH
Q162H
-
site-directed mutagenesis, mutation at the C-terminus of the alpha-helix has a stabilizing effect at 55°C, not at 65°C
Q162Y
-
site-directed mutagenesis, mutation at the C-terminus of the alpha-helix has a stabilizing effect at 55°C, not at 65°C
S110C/N154C
-
site-directed mutagenesis, introduction of a disulfide bridge in the alpha-helix of the enzyme leads to increase of the half-life at 65°C from less than 1 min to 14 min
S110C/N154C/Q162H
-
site-directed mutagenesis, mutations lead to increased thermal and pH stability, overview
S110C/N154C/Q162H/N11D
-
site-directed mutagenesis, mutations lead to increased thermal and pH stability, overview
S110C/N154C/Q162H/N11D/N38D
-
site-directed mutagenesis, mutations lead to increased thermal and pH stability, overview
S110C/N154C/Q162Y
-
site-directed mutagenesis, mutations lead to increased thermal and pH stability, overview
S110C/N154C/Q162Y/N11D
-
site-directed mutagenesis, mutations lead to increased thermal and pH stability, overview
S186R
site-directed mutagenesis, reduced thermal stability at 50°C in absence of substrate compared to the wild-type enzyme
S186R/N67R
site-directed mutagenesis, reduced thermal stability at 50°C in absence of substrate compared to the wild-type enzyme
S186R/N67R/T26R
site-directed mutagenesis, reduced thermal stability at 50°C in absence of substrate, reduced stability at 60°C and unaltered at 65°C in presence of substrate, compared to the wild-type enzyme
S186R/N67R/T26R/Q34R
site-directed mutagenesis, highly reduced thermal stability at 50°C in absence of substrate, unaltered stability at 60°C and slightly increased at 65°C in presence of substrate, compared to the wild-type enzyme
S186R/N67R/T26R/Q34R/N69R
site-directed mutagenesis, reduced thermal stability at 50°C in absence of substrate, increased stability at 60°C and 65°C in presence of substrate, compared to the wild-type enzyme
S186R/N67R/T26R/Q34R/S40R
site-directed mutagenesis, highly reduced thermal stability at 50°C in absence of substrate, highly increased stability at 60°C and increased 65°C in presence of substrate, compared to the wild-type enzyme
N14H
thermostabilizing mutation, catalytic activity is broadly similar to the wild-type
Q34L
thermostabilizing mutation, catalytic activity is broadly similar to the wild-type
S35E
thermostabilizing mutation, catalytic activity is broadly similar to the wild-type
S71T
thermostabilizing mutation, catalytic activity is broadly similar to the wild-type
S9P
S9P/T13F/N14H/Y18F/Q34L/S35E/S71T
hyperthermostable mutant Xyn11TS, retains full activity after incubation at 90°C for 60 min, catalytic activity is broadly similar to the wild-type
T13F
Y18F
thermostabilizing mutation, catalytic activity is broadly similar to the wild-type
T28C/T60C
-
171% of wild-type activity, 2-3fold increases in bagasse hydrolysis at pH 9.0 and 60°C compared to the wild-type
T28C/T60C/T77C/E249C
-
158% of wild-type activity, 2-3fold increases in bagasse hydrolysis at pH 9.0 and 60°C compared to the wild-type
additional information
S100C/N150C
-
increased thermostability of about 5°C compared to the wild type enzyme
S100C/N150C
-
increased thermostability of about 5°C compared to the wild type enzyme
-
V169A/I170F/D171N
Halalkalibacterium halodurans
site-directed mutagenesis, the mutant shows a pH optimum of pH 7.0, incontrast to the wild-type enzyme which has an optimum at pH 9.0-9.5
V169A/I170F/D171N
Halalkalibacterium halodurans S7
-
site-directed mutagenesis, the mutant shows a pH optimum of pH 7.0, incontrast to the wild-type enzyme which has an optimum at pH 9.0-9.5
-
biofuel production
potential application in the field of biomass pretreatment and biofuel production
biofuel production
Pleurotus ostreatus HAUCC 162
-
potential application in the field of biomass pretreatment and biofuel production
-
D281N
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme. The TtGH8 D281N-beta-1,4-xylohexaose complex structure reveals that, the -1 subsite sugar is in a completely ring-flipped, southern hemisphere 1C4 chair conformation. Although this allows access to a hexasaccharide complex structure, the ring-flipped -1 sugar is unlikely to be representative of a catalytically relevant conformation since its position neither allows protonation of the leaving group by Glu73 nor is there a potential reactive water. In the 1C4 chair conformation the now axial (and down) O2 occupies the position that should instead be occupied by the nucleophilic water
D281N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme. The TtGH8 D281N-beta-1,4-xylohexaose complex structure reveals that, the -1 subsite sugar is in a completely ring-flipped, southern hemisphere 1C4 chair conformation. Although this allows access to a hexasaccharide complex structure, the ring-flipped -1 sugar is unlikely to be representative of a catalytically relevant conformation since its position neither allows protonation of the leaving group by Glu73 nor is there a potential reactive water. In the 1C4 chair conformation the now axial (and down) O2 occupies the position that should instead be occupied by the nucleophilic water
-
D281N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme. The TtGH8 D281N-beta-1,4-xylohexaose complex structure reveals that, the -1 subsite sugar is in a completely ring-flipped, southern hemisphere 1C4 chair conformation. Although this allows access to a hexasaccharide complex structure, the ring-flipped -1 sugar is unlikely to be representative of a catalytically relevant conformation since its position neither allows protonation of the leaving group by Glu73 nor is there a potential reactive water. In the 1C4 chair conformation the now axial (and down) O2 occupies the position that should instead be occupied by the nucleophilic water
-
Q1C/Q24C
introduction of disulfide bridge, leading to increase in temperature optimum at pH 6.5 by about 10 degrees to 75°C, increased resistance to thermal inactivation and increased melting temperature. At pH 8 and 70°C, the disulfide bridge increases the enzyme half-life 20fold in the presence of substrate
Q1C/Q24C
-
introduction of disulfide bridge, leading to increase in temperature optimum at pH 6.5 by about 10 degrees to 75°C, increased resistance to thermal inactivation and increased melting temperature. At pH 8 and 70°C, the disulfide bridge increases the enzyme half-life 20fold in the presence of substrate
-
S9P
locks the conformation of a surface loop, catalytic activity is broadly similar to the wild-type
T13F
thermostabilizing mutation, catalytic activity is broadly similar to the wild-type
additional information
generation of two constructs of XynC, one with its cellulose binding domain and the catalytic domain, pXynC-BC, and the other with only the catalytic domain, pXynC-C. The specific activities of XynC with and without the non-catalytic domains are similar
additional information
generation of two constructs of XynC, one with its cellulose binding domain and the catalytic domain, pXynC-BC, and the other with only the catalytic domain, pXynC-C. The specific activities of XynC with and without the non-catalytic domains are similar
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generation of two constructs of XynZ: pXynZ-BDC, which includes the dockerin domain, and pXynZ-C, which does not. For XynZ, the specific activity of the enzyme without the non-catalytic domains is about 5fold greater than that of the intact enzyme. The overall increase in activity is 9fold higher for XynZ-C versus XynZ-BDC
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generation of two constructs of XynZ: pXynZ-BDC, which includes the dockerin domain, and pXynZ-C, which does not. For XynZ, the specific activity of the enzyme without the non-catalytic domains is about 5fold greater than that of the intact enzyme. The overall increase in activity is 9fold higher for XynZ-C versus XynZ-BDC
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truncated derivatives XynAGN16L (truncation of GH 10 domain at N-terminus) and XynAGN16Lpd (truncation of GH 10 domain at N-terminus and polysaccharide deacetylases domain) show similar features, including catalytic activities at 0°C, thermolabilities at temperatures of more than 50°C, and similar substrate specificity. However, the polysaccharide deacetylases domain improves the affinity and catalytic efficiency towards xylans
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truncated derivatives XynAGN16L (truncation of GH 10 domain at N-terminus) and XynAGN16Lpd (truncation of GH 10 domain at N-terminus and polysaccharide deacetylases domain) show similar features, including catalytic activities at 0°C, thermolabilities at temperatures of more than 50°C, and similar substrate specificity. However, the polysaccharide deacetylases domain improves the affinity and catalytic efficiency towards xylans
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DELTAXBD, consists of the catalytic domain only and corresponds to ALa1-Pro222 of XynJ. Mutants DELTAXBDR5 and DELTAXBDK51R/R5 show about 50% activity of that of DELTAXBD and have optima of pH 9.0 and 9.5, respectively. Reinforcing the characteristic salt bridge in the catalytic cleft and introducing excess Arg residues on the protein surface shift the optimum pH of the wild-type enzyme from 8.5 to 9.5. Mutant DELTAXBDK51R exhibit almost the same temperature profile and temperature optimum as DELTAXBD. The temperature optima of mutants DELTAXBDR5 and DELTAXBDK51R/R5 are both 60°C. Mutants show lower specific activity than DELTAXBD at 37-60°C, but they show apparently higher activity at 65°C. Introduction of excess Arg residues on the protein surface increase the thermostability of DELTAXBD
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the fusion of the 1642-bp laccase (CorA) with either the 555-bp xylanase (XynA) or the thermostable variant (XynAG3) are performed by insertion of the xylanase into a surface loop of the laccase. The resulting chimeric constructs of 2197 bp contain a central region composed of the XynA or XynAG3 sequence flanked by the regions of the CorA encoding the N-terminal residues 1216 (forming the 5' region of the chimera) and the C-terminal region comprising residues 217513 of CorA. As a consequence, the final construct results in two linkage points between the laccase and xylanase domains
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generation of a bifunctional enzyme consisting of a GH11 endo-1,4-beta-xylanase fused to a GH43 beta-xylosidase, both from Bacillus subtilis. The substrate cleavage rate is altered by the molecular fusion improving at least 3fold the xylose production using specific substrates as beechwood xylan and hemicelluloses from pretreated biomass. The chimeric enzyme shows higher thermotolerance with a positive shift of the optimum temperature from 35°C to 50°C for xylosidase activity
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fusion of enzyme with a carbohydrate-binding module from Clostridium thermocellum which exhibits high affinity to xylan. The molecular fusion does not alter the pH and temperature dependence, but leads to an increase of 65% in the catalytic efficiency. As supplement in the commercial cocktail Accellerase1 1500, the chimeric enzyme improves the reducing sugar release by 17% from pretreated sugarcane bagasse
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fusion of enzyme with a carbohydrate-binding module from Clostridium thermocellum which exhibits high affinity to xylan. The molecular fusion does not alter the pH and temperature dependence, but leads to an increase of 65% in the catalytic efficiency. As supplement in the commercial cocktail Accellerase1 1500, the chimeric enzyme improves the reducing sugar release by 17% from pretreated sugarcane bagasse
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construction of a fusion protein with the carbohydrate-binding doamin of xylanase XynZ from Clostridium thermocellum. The fusion does not alter the pH and temperature dependence, but increases the catalytic activity by 65%
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construction of a fusion protein with the carbohydrate-binding doamin of xylanase XynZ from Clostridium thermocellum. The fusion does not alter the pH and temperature dependence, but increases the catalytic activity by 65%
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generation of a bifunctional enzyme consisting of a GH11 endo-1,4-beta-xylanase fused to a GH43 beta-xylosidase, both from Bacillus subtilis. The substrate cleavage rate is altered by the molecular fusion improving at least 3fold the xylose production using specific substrates as beechwood xylan and hemicelluloses from pretreated biomass. The chimeric enzyme shows higher thermotolerance with a positive shift of the optimum temperature from 35°C to 50°C for xylosidase activity
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fusion of enzyme with a carbohydrate-binding module from Clostridium thermocellum which exhibits high affinity to xylan. The molecular fusion does not alter the pH and temperature dependence, but leads to an increase of 65% in the catalytic efficiency. As supplement in the commercial cocktail Accellerase1 1500, the chimeric enzyme improves the reducing sugar release by 17% from pretreated sugarcane bagasse
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construction of a fusion protein with the carbohydrate-binding doamin of xylanase XynZ from Clostridium thermocellum. The fusion does not alter the pH and temperature dependence, but increases the catalytic activity by 65%
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the disruption of xyn11A causes only a moderate decrease, about 30%, in the level of extracellular endo-beta-1-4-xylanase activity
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the disruption of xyn11A causes only a moderate decrease, about 30%, in the level of extracellular endo-beta-1-4-xylanase activity
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the disruption of xyn11A causes only a moderate decrease, about 30%, in the level of extracellular endo-beta-1-4-xylanase activity
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construction of a deletion mutant lacking the C-terminal ricin-type beta-trefoil lectin domain-like part. Mutant shows a decrease in binding capacities to lignin and insoluble polysaccharides
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construction of a library of circular permutants, generated by random circular permutation of Bcx, random DNase cleavage of the circularized Bcx gene, to introduce new termini in loop regions while linking its native termini directly or via one or two glycines, qualitative analysis, overview. Several permutations place key catalytic residues at or near the new termini with minimal deleterious effects on activity, up to 4fold increased activity. Mutant structure determination and analysis by X-ray diffraction and by NMR spectroscopy. Detailed stability and activity studies on three selected permutants, cpN35G2', cpY94G2', and cpY174G2', overview
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construction of a library of circular permutants, generated by random circular permutation of Bcx, random DNase cleavage of the circularized Bcx gene, to introduce new termini in loop regions while linking its native termini directly or via one or two glycines, qualitative analysis, overview. Several permutations place key catalytic residues at or near the new termini with minimal deleterious effects on activity, up to 4fold increased activity. Mutant structure determination and analysis by X-ray diffraction and by NMR spectroscopy. Detailed stability and activity studies on three selected permutants, cpN35G2', cpY94G2', and cpY174G2', overview
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removal of the CBMs from Xyn10A strongly reduces the ability of plant cell wall hydrolysis
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removal of the CBMs from Xyn10A strongly reduces the ability of plant cell wall hydrolysis
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generation of a truncationmutant lacking the N-terminal domain, the mutant is catalytically inactive
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generation of a truncationmutant lacking the N-terminal domain, the mutant is catalytically inactive
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removal of the CBMs from Xyn10A strongly reduces the ability of plant cell wall hydrolysis
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a DELTAxyn5 mutant, as well as a xyn5DELTASLH mutant, lacking the SLH domain, grow poorly and produce minimal amounts of Xyn1 and Xyn3 on water-insoluble xylan. The xyn5DELTASLH mutant is secreted to the culture medium
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generation of XynB mutans variants, e.g. deletion mutant DELTAP130, displaying increased catalytic efficiency towards wheat arabinoxylan and xylo-oligosaccharides and identified specific determinants in PgXynB thumb region responsible for resistance to the wheat xylanase inhibitor XIP-I
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enzyme knockout mutant, strain is as virulent as wild-type in infecting the rice host
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silencing of the endoxylanase by double-stranded RNA targeting, by RNA interference, RNAi, of the carbohydratebinding module, CBM, region results in an average decrease in infection of 60%
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silencing of the endoxylanase by double-stranded RNA targeting, by RNA interference, RNAi, of the carbohydratebinding module, CBM, region results in an average decrease in infection of 60%
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preparation of a robust immobilized biocatalyst of beta-1,4-endoxylanase C-terminally His-tagged Xys1 by surface coating with polymers for production of xylooligosaccharides from different xylan sources. Surface coating of dextran-modified Ag-G-Xys1-L and Ag-G-Xys1-H biocatalysts with cationic polymer (PEI) by chemical modifications via ionic exchange. The optimized biocatalyst is 550fold more stable than one-point covalent immobilized C-terminally His-tagged Xys1 at 70°C, pH 7.0. Hydrolysis of beechwood, wheat straw and corncob xylans is 93% in 4 h, 44% in 5 h and 100% in 1 h, respectively. Maximum values of xylooligosaccharides are found for beechwood at 20.6 mg/ml, wheat at 12.5 mg/ml, and corncob at 30.4 mg/ml. The optimized biocatalyst is reused for 15 reaction cycles without affecting its catalytic activity. Method optmization and evaluation, overview
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preparation of a robust immobilized biocatalyst of beta-1,4-endoxylanase C-terminally His-tagged Xys1 by surface coating with polymers for production of xylooligosaccharides from different xylan sources. Surface coating of dextran-modified Ag-G-Xys1-L and Ag-G-Xys1-H biocatalysts with cationic polymer (PEI) by chemical modifications via ionic exchange. The optimized biocatalyst is 550fold more stable than one-point covalent immobilized C-terminally His-tagged Xys1 at 70°C, pH 7.0. Hydrolysis of beechwood, wheat straw and corncob xylans is 93% in 4 h, 44% in 5 h and 100% in 1 h, respectively. Maximum values of xylooligosaccharides are found for beechwood at 20.6 mg/ml, wheat at 12.5 mg/ml, and corncob at 30.4 mg/ml. The optimized biocatalyst is reused for 15 reaction cycles without affecting its catalytic activity. Method optmization and evaluation, overview
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preparation of a robust immobilized biocatalyst of beta-1,4-endoxylanase C-terminally His-tagged Xys1 by surface coating with polymers for production of xylooligosaccharides from different xylan sources. Surface coating of dextran-modified Ag-G-Xys1-L and Ag-G-Xys1-H biocatalysts with cationic polymer (PEI) by chemical modifications via ionic exchange. The optimized biocatalyst is 550fold more stable than one-point covalent immobilized C-terminally His-tagged Xys1 at 70°C, pH 7.0. Hydrolysis of beechwood, wheat straw and corncob xylans is 93% in 4 h, 44% in 5 h and 100% in 1 h, respectively. Maximum values of xylooligosaccharides are found for beechwood at 20.6 mg/ml, wheat at 12.5 mg/ml, and corncob at 30.4 mg/ml. The optimized biocatalyst is reused for 15 reaction cycles without affecting its catalytic activity. Method optmization and evaluation, overview
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obtained switching mutant N127S-E128H, rate of hydrolysis is apparently zero in the absence of sodium azide, accumulates the glycosyl-enzyme intermediate, breakdown rate of glycosyl-enzyme intermediate is dramatically accelerated by two orders of magnitude in the presence of 300 mM sodium azide
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substituting of Streptomyces olivaceovirdis SoxB 33 N-terminal amino acid residues with the corresponding residues of the thermophilic xylanase TfxA from Thermomonospora fusca strain ATCC 27730 significantly enhances the enzyme thermostability, overview
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obtained switching mutant N127S-E128H, rate of hydrolysis is apparently zero in the absence of sodium azide, accumulates the glycosyl-enzyme intermediate, breakdown rate of glycosyl-enzyme intermediate is dramatically accelerated by two orders of magnitude in the presence of 300 mM sodium azide
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recombinant protein expressed in Pichia pastoris without signal peptide exhibits better physicochemical properties than those of the native enzyme including higher optimal temperature of 60°C, and specific activity, but lower optimal pH 4.0
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truncated versions xynAS27cd (CBM-linker-truncated version) and xynAS27cdl (CBM-truncated version) show less pH and thermal stability, and less affinity and hydrolytic activity to insoluble substrate than the intact one
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the catalytic domain is identified and truncated to remove the original signal peptide and linker region and to include an N-terminal hexahistidine tag and 3C protease cleavage site
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the catalytic domain is identified and truncated to remove the original signal peptide and linker region and to include an N-terminal hexahistidine tag and 3C protease cleavage site
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the catalytic domain is identified and truncated to remove the original signal peptide and linker region and to include an N-terminal hexahistidine tag and 3C protease cleavage site
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the catalytic domain is identified and truncated to remove the original signal peptide and linker region and to include an N-terminal hexahistidine tag and 3C protease cleavage site
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substitution of 31 N-terminal amino acids by thecorresponding region of 22 amino acid residues of the Bacillus subtilis xylanase A
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substitution of 31 N-terminal amino acids by thecorresponding region of 22 amino acid residues of the Bacillus subtilis xylanase A
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random mutagenesis leads to mutant M7 with improved kinetic and thermodynamic properties
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fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
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the C-terminal carbohydrate binding module has only a slight effect, whereas a polyhistidine tag increases the thermostability of XYN10A
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improving the thermostability of Trichoderma reesei xylanase 2 by introducing the thermostabilizing domain A2 from Thermotoga maritima XynA into the N-terminal region of the Xyn2 protein
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construction of several mutant with increased number of arginines on the protein surface showing unaltered thermal stability but narrowed pH optimum, mutation of arginines to Ser/Thr causes a pH profile shift
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construction of several mutant with increased number of arginines on the protein surface showing unaltered thermal stability but narrowed pH optimum, mutation of arginines to Ser/Thr causes a pH profile shift
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increase in thermal stability in the mutants leads to increased pH stability as well, but also to reduced activity at both acidic and alkaline pH levels
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improving the thermostability of Trichoderma reesei xylanase 2 by introducing the thermostabilizing domain A2 from Thermotoga maritima XynA into the N-terminal region of the Xyn2 protein
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LC132960
the addition of a xylan-binding domain to the C-terminus of Xyn III improves its hydrolytic activity on insoluble xylan
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the addition of a xylan-binding domain to the C-terminus of Xyn III improves its hydrolytic activity on insoluble xylan
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improving the thermostability of Trichoderma reesei xylanase 2 by introducing the thermostabilizing domain A2 from Thermotoga maritima XynA into the N-terminal region of the Xyn2 protein
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construction of truncated mutants, lacking the carbohydrate binding module CBM, which functions to selectively bind insoluble xylan and increase the rate of hydrolysis. Xyl1A corresponds to the GH11 domain coding sequence, Xyl1B corresponds to the GH11 and the CBM1 domain coding sequences, and Xyl1C corresponds to the two CBM coding sequences
