| 000 | 01751 a2200541 4500 | ||
|---|---|---|---|
| 005 | 20250517171858.0 | ||
| 264 | 0 | _c20180601 | |
| 008 | 201806s 0 0 eng d | ||
| 022 | _a1738-8872 | ||
| 024 | 7 |
_a10.4014/jmb.1705.05026 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aTian, Yong-Sheng | |
| 245 | 0 | 0 |
_aImprovement of the Thermostability of Xylanase from _h[electronic resource] |
| 260 |
_bJournal of microbiology and biotechnology _cOct 2017 |
||
| 300 |
_a1783-1789 p. _bdigital |
||
| 500 | _aPublication Type: Journal Article | ||
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 |
_aBacillales _xenzymology |
| 650 | 0 | 4 |
_aDisulfides _xchemistry |
| 650 | 0 | 4 |
_aEndo-1,4-beta Xylanases _xgenetics |
| 650 | 0 | 4 | _aEnzyme Assays |
| 650 | 0 | 4 | _aEnzyme Stability |
| 650 | 0 | 4 | _aGene Expression Regulation, Fungal |
| 650 | 0 | 4 | _aHalf-Life |
| 650 | 0 | 4 | _aHot Temperature |
| 650 | 0 | 4 | _aHydrogen-Ion Concentration |
| 650 | 0 | 4 | _aKinetics |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 |
_aMutagenesis, Site-Directed _xmethods |
| 650 | 0 | 4 | _aMutation |
| 650 | 0 | 4 |
_aPichia _xgenetics |
| 650 | 0 | 4 | _aProtein Conformation |
| 650 | 0 | 4 | _aProtein Folding |
| 650 | 0 | 4 | _aProtein Stability |
| 650 | 0 | 4 | _aProtein Structure, Tertiary |
| 650 | 0 | 4 | _aRecombinant Proteins |
| 650 | 0 | 4 | _aSequence Alignment |
| 650 | 0 | 4 | _aSequence Analysis |
| 650 | 0 | 4 |
_aXylosidases _xmetabolism |
| 650 | 0 | 4 |
_abeta-Glucosidase _xgenetics |
| 700 | 1 | _aXu, Jing | |
| 700 | 1 | _aChen, Lei | |
| 700 | 1 | _aFu, Xiao-Yan | |
| 700 | 1 | _aPeng, Ri-He | |
| 700 | 1 | _aYao, Quan-Hong | |
| 773 | 0 |
_tJournal of microbiology and biotechnology _gvol. 27 _gno. 10 _gp. 1783-1789 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.4014/jmb.1705.05026 _zAvailable from publisher's website |
| 999 |
_c27507752 _d27507752 |
||