Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Wang, Q.; Xia, T.
    Enhancement of the activity and alkaline pH stability of Thermobifida fusca xylanase A by directed evolution (2008), Biotechnol. Lett., 30, 937-944.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.2.1.8 industry DNA shuffling improves the catalytic activity and alkaline pH stability of Thermobifida fusca xylanase A toward the hydrolysis of xylan evolved enzyme 2TfxA98 can meet the requirements of biobleaching by its stability and activation under conditions of alkaline and high temperatures Thermobifida fusca

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.8 TfxA-cat gene cleaved by BamHI and PstI and ligated with vector pQE30 Thermobifida fusca

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.8 G217L increases activity and alkaline pH stability to some extent Thermobifida fusca
3.2.1.8 G25P mainly leads to increase in alkaline pH stability without improving the specific activity Thermobifida fusca
3.2.1.8 I91T results in the main contribution to catalytic activity rather than alkaline pH stability Thermobifida fusca
3.2.1.8 T21A mainly leads to increase in alkaline pH stability without improving the specific activity Thermobifida fusca
3.2.1.8 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 Thermobifida fusca
3.2.1.8 V87P significantly improves both the activity and alkaline pH stability Thermobifida fusca

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.8 Thermobifida fusca
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.8 recombinant TfxA and the mutants purified to homogeneity on nickel-chelating column Thermobifida fusca

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.8 506
-
 mutant G25P Thermobifida fusca
3.2.1.8 565
-
 mutant T21A Thermobifida fusca
3.2.1.8 686
-
 wild-type Thermobifida fusca
3.2.1.8 851
-
 mutant G217L Thermobifida fusca
3.2.1.8 896
-
 mutant I91T Thermobifida fusca
3.2.1.8 940
-
 mutant V87P Thermobifida fusca
3.2.1.8 1108
-
 mutant 2TfxA98 Thermobifida fusca

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.8 xylan + H2O
-
 Thermobifida fusca ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.8 xylanase A
-
 Thermobifida fusca

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.8 70
-
 both recombinant TfxA and mutant 2TfxA98 are stable at 70°C during 30 min incubation, although the mutant is slightly less stable than the parent at 70°C after 30 min of incubation Thermobifida fusca

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.8 86
-
 xylan wild-type Thermobifida fusca
3.2.1.8 225
-
 xylan mutant 2TfxA98 Thermobifida fusca