Thermostable Laccases from Bacteria
This is a modal window.
The media could not be loaded, either because the server or network failed or because the format is not supported.
Formal Metadata
| Title |
| |
| Title of Series | ||
| Number of Parts | 22 | |
| Author | ||
| License | CC Attribution 3.0 Unported: You are free to use, adapt and copy, distribute and transmit the work or content in adapted or unchanged form for any legal purpose as long as the work is attributed to the author in the manner specified by the author or licensor. | |
| Identifiers | 10.5446/14088 (DOI) | |
| Publisher | ||
| Release Date | ||
| Language |
Content Metadata
| Subject Area | |
| Genre |
9
11
18
00:00
ChemistryTemperaturbeständigkeitAzo couplingRadical (chemistry)BiophysicsLevomethadonDeterrence (legal)BrothSubstrat <Chemie>ProteinLactoseAngiotensin-converting enzymeSoilPhenol formaldehyde resinAmino acidEnzymePolymerLigninMultiprotein complexBiomolecular structureTiermodellChemistryFood additiveSet (abstract data type)Chemical structureSimulationTemperaturbeständigkeitLecture/Conference
Transcript: English(auto-generated)
00:03
My project is about protein chemistry, more specifically on the class of enzyme called lacases, which catalyze degradation of phenolic compounds in nature. One notable thing about the lacases is the broad substrate specificity, which includes complex polymers such as lignin. Another
00:24
important point about the lacases is that they are quite stable. They are an extracellular enzyme that are secreted to the environment in order to scavenge the soil for these hardly soluble substrates. This makes the lacases more
00:40
stable than your average protein, which is exemplified by their thermostability. Many lacases can function at up to 60 degrees or even higher. These two traits, the broad substrate specificity and thermostability makes the lacases a natural candidate as a catalytic enzyme in industrial
01:04
applications. However, despite three decades of intense research, only a few such applications have been commercialized. My project is to tie together some of these many datasets that are available with some
01:22
new simulations of the three-dimensional structure, tie them into a statistical model that will help to predict the stability of the lacase directly from the sequence of amino acids. With this model, I will hopefully be able to identify new mutants of lacases with enhanced
01:43
thermostability. And as a proof of concept, I will turn to the