Publication Details |
| Category | Text Publication |
| Reference Category | Book chapters |
| DOI | 10.1007/978-3-030-47906-0_4 |
| Title (Primary) | Laccases in the context of potentially cooperating enzymes |
| Title (Secondary) | Laccases in bioremediation and waste valorisation |
| Author | Haghbeen, K.; Schlosser, D.
|
| Publisher | Schlosser, D. |
| Source Titel | Microbiology Monographs |
| Year | 2020 |
| Department | UMB |
| Volume | 33 |
| Page From | 79 |
| Page To | 114 |
| Language | englisch |
| Keywords | Biorefinery; Bioremediation; Biotransformation; Enzyme cascade; Enzyme product; Enzyme substrate; Multi-enzyme cocktail; Wastewater treatment |
| UFZ inventory | Leipzig, Bibliothek, Hauptlesesaal, 00534321, 20-0230 DK: 504.064.4 Lac |
| Abstract | Laccases have attracted scientists and practitioners already since a long time, due to their catalytic versatility, robustness, and potential usability for a wide spectrum of diverse applications. In lignocellulose decaying microorganisms, laccases and further enzymes frequently form suites of biocatalysts cooperating in decay type-specific concerted actions. Such possible natural enzymatic interactions have largely inspired biotechnological concepts aiming at the use of multi-enzyme cocktails or enzyme cascades for diverse applications such as wastewater treatment, biorefinery approaches targeting the production of biofuels and platform chemicals, as well as pharmaceutical and industrial biotransformations. This chapter illustrates both proven and potential (albeit still rather hypothetical) cooperations between laccases and other microbial enzymes. The thereby addressed types of cooperation involve (1) enzymes being structurally and catalytically similar to laccases such as tyrosinases, which may complement laccase reactivity; (2) enzymes (or subsequent reactions) fueled with substrates (or reactants) generated during laccase reactions, as exemplified for lignin-modifying manganese peroxidases and β-etherases; and (3) enzymes potentially producing substrates for laccases, e.g., unspecific peroxygenases. |
| Persistent UFZ Identifier | https://www.ufz.de/index.php?en=20939&ufzPublicationIdentifier=23592 |
| Haghbeen, K., Schlosser, D. (2020): Laccases in the context of potentially cooperating enzymes In: Schlosser, D. (ed.) Laccases in bioremediation and waste valorisation Microbiology Monographs 33 Springer, Berlin, Heidelberg, New York, p. 79 - 114 10.1007/978-3-030-47906-0_4 |
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