| 000 | 05849naaaa2201633uu 4500 | ||
|---|---|---|---|
| 001 | https://directory.doabooks.org/handle/20.500.12854/69259 | ||
| 005 | 20220714181207.0 | ||
| 020 | _abooks978-3-03943-465-7 | ||
| 020 | _a9783039434640 | ||
| 020 | _a9783039434657 | ||
| 024 | 7 |
_a10.3390/books978-3-03943-465-7 _cdoi |
|
| 041 | 0 | _aEnglish | |
| 042 | _adc | ||
| 072 | 7 |
_aTB _2bicssc |
|
| 100 | 1 |
_aSunna, Anwar _4edt _91598380 |
|
| 700 | 1 |
_aDaniellou, Richard _4edt _91598381 |
|
| 700 | 1 |
_aSunna, Anwar _4oth _91598380 |
|
| 700 | 1 |
_aDaniellou, Richard _4oth _91598381 |
|
| 245 | 1 | 0 | _aNovel Enzyme and Whole-Cell Biocatalysts |
| 260 |
_aBasel, Switzerland _bMDPI - Multidisciplinary Digital Publishing Institute _c2020 |
||
| 300 | _a1 electronic resource (332 p.) | ||
| 506 | 0 |
_aOpen Access _2star _fUnrestricted online access |
|
| 520 | _aThe concept of a circular economy relies on waste reduction, valorization, and recycling. Global trends for "green" synthesis of chemicals have positioned the field of enzyme technology and biocatalysis (multi-enzymes and whole-cells) as an alternative for the synthesis of more social- and environmentally-responsible bio-based chemicals. Recent advances in synthetic biology, computational tools, and metabolic engineering have supported the discovery of new enzymes and the rational design of whole-cell biocatalysts. In this book, we highlight these current advances in the field of biocatalysis, with special emphasis on novel enzymes and whole-cell biocatalysts for applications in several industrial biotechnological applications. | ||
| 540 |
_aCreative Commons _fhttps://creativecommons.org/licenses/by/4.0/ _2cc _4https://creativecommons.org/licenses/by/4.0/ |
||
| 546 | _aEnglish | ||
| 650 | 7 |
_aTechnology: general issues _2bicssc _9928609 |
|
| 653 | _a2G ethanol | ||
| 653 | _ahemicellulose usage | ||
| 653 | _aS. cerevisiae | ||
| 653 | _aenzyme immobilization | ||
| 653 | _acell immobilization | ||
| 653 | _aSHIF | ||
| 653 | _amannonate dehydratase | ||
| 653 | _amannose metabolism | ||
| 653 | _aThermoplasma acidophilum | ||
| 653 | _amannono-1,4-lactone | ||
| 653 | _a2-keto-3-deoxygluconate | ||
| 653 | _aaldohexose dehydrogenase | ||
| 653 | _acyclodextrin glucanotransferases | ||
| 653 | _alarge-ring cyclodextrins | ||
| 653 | _asemi rational mutagenesis | ||
| 653 | _acarbohydrate active enzymes | ||
| 653 | _aarchaea | ||
| 653 | _aglycosidase | ||
| 653 | _aSulfolobus solfataricus | ||
| 653 | _aSaccharolobus solfataricus | ||
| 653 | _aLactobacillus | ||
| 653 | _aβ-galactosidase | ||
| 653 | _aimmobilization | ||
| 653 | _acell surface display | ||
| 653 | _aLysM domains | ||
| 653 | _abiocatalysis | ||
| 653 | _aextremophile | ||
| 653 | _a5-hydroxymethylfurfural | ||
| 653 | _a5-hydroxymethylfuroic acid | ||
| 653 | _aplatform chemicals | ||
| 653 | _awhole cells | ||
| 653 | _aNew Delhi metallo-β-lactamase | ||
| 653 | _aNDM-24 | ||
| 653 | _akinetic profile | ||
| 653 | _asecondary structure | ||
| 653 | _aglycoside hydrolase | ||
| 653 | _athioglycosides | ||
| 653 | _aFervidobacterium | ||
| 653 | _aendo-β-1,3-glucanase | ||
| 653 | _alaminarinase | ||
| 653 | _athermostable | ||
| 653 | _agene duplication | ||
| 653 | _acofactor F420 | ||
| 653 | _adeazaflavin | ||
| 653 | _aoxidoreductase | ||
| 653 | _ahydride transfer | ||
| 653 | _ahydrogenation | ||
| 653 | _aasymmetric synthesis | ||
| 653 | _acofactor biosynthesis | ||
| 653 | _aω-transaminase | ||
| 653 | _aα-methylbenzylamine | ||
| 653 | _achiral amine | ||
| 653 | _abiotransformation | ||
| 653 | _abiodiesel | ||
| 653 | _awaste cooking oil | ||
| 653 | _alipase immobilization | ||
| 653 | _ainterfacial activation | ||
| 653 | _afunctionalized magnetic nanoparticles | ||
| 653 | _aDNase | ||
| 653 | _akinetic profiles | ||
| 653 | _aRNase | ||
| 653 | _asemi-rational mutagenesis | ||
| 653 | _asubstrate specificity | ||
| 653 | _aengineered Escherichia coli | ||
| 653 | _aflavonoid glucuronides | ||
| 653 | _amultienzyme whole-cell biocatalyst | ||
| 653 | _aorganic solvents | ||
| 653 | _apsychrophilic yeast | ||
| 653 | _ahormone-sensitive lipase | ||
| 653 | _aGlaciozyma antarctica | ||
| 653 | _aAntarctica and homology modelling | ||
| 653 | _akeratinase | ||
| 653 | _aserine protease | ||
| 653 | _ametalloprotease | ||
| 653 | _apeptidase | ||
| 653 | _akeratin hydrolysis | ||
| 653 | _akeratin waste | ||
| 653 | _avalorisation | ||
| 653 | _abioactive peptides | ||
| 653 | _aene reductase | ||
| 653 | _aenzyme sourcing | ||
| 653 | _aold yellow enzyme | ||
| 653 | _asolvent stability | ||
| 653 | _amachine learning | ||
| 653 | _aflux optimization | ||
| 653 | _aartificial neural network | ||
| 653 | _asynthetic biology | ||
| 653 | _aglycolysis | ||
| 653 | _ametabolic pathways optimization | ||
| 653 | _acell-free systems | ||
| 653 | _ahydrolase | ||
| 653 | _alipase | ||
| 653 | _aesterase | ||
| 653 | _aBacillus subtilis lipase A | ||
| 653 | _atransesterification | ||
| 653 | _aorganic solvent | ||
| 653 | _awater activity | ||
| 653 | _aimmobilized lipase | ||
| 653 | _aRSM | ||
| 653 | _afuel properties | ||
| 653 | _achemo-enzymatic synthesis | ||
| 653 | _aglycosyl transferases | ||
| 653 | _aprotein engineering | ||
| 653 | _acarbohydrates | ||
| 653 | _aindustrial enzymes | ||
| 653 | _athermostable enzymes | ||
| 653 | _aglycoside hydrolases | ||
| 653 | _acell-free biocatalysis | ||
| 653 | _anatural and non-natural multi-enzyme pathways | ||
| 653 | _abio-based chemicals | ||
| 856 | 4 | 0 |
_awww.oapen.org _uhttps://mdpi.com/books/pdfview/book/3047 _70 _zDOAB: download the publication |
| 856 | 4 | 0 |
_awww.oapen.org _uhttps://directory.doabooks.org/handle/20.500.12854/69259 _70 _zDOAB: description of the publication |
| 999 |
_c3001280 _d3001280 |
||