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Publications citing the applications of openQCM (by Novaetech S.r.l.) instruments and accessories in scientific research.
The list of scientific papers published on the most important journals showing the usage of openQCM in several scientific fields, such as thin film deposition, chemical sensors, biological research and biosensors.
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Millan, Fabien; Hanik, Nils
Degradation kinetics of medium chain length Polyhydroxyalkanoate degrading enzyme: a quartz crystal microbalance study Journal Article
In: Frontiers in Bioengineering and Biotechnology, vol. 11, pp. 1303267, 2023.
Abstract | Links | BibTeX | Tags: biodegradable polymers, degradation kinetics, depolymerase enzymes, enzymatic degradation, openQCM, openQCM Q-1, polyhydroxyalkanoates, Python, Quartz Crystal Microbalance
@article{millan2023degradation,
title = {Degradation kinetics of medium chain length Polyhydroxyalkanoate degrading enzyme: a quartz crystal microbalance study},
author = {Fabien Millan and Nils Hanik},
url = {https://www.frontiersin.org/journals/bioengineering-and-biotechnology/articles/10.3389/fbioe.2023.1303267/full},
doi = {https://doi.org/10.3389/fbioe.2023.1303267},
year = {2023},
date = {2023-12-14},
urldate = {2023-12-14},
journal = {Frontiers in Bioengineering and Biotechnology},
volume = {11},
pages = {1303267},
publisher = {Frontiers Media SA},
abstract = {This study investigates the enzymatic degradation processes of different classes of polyhydroxyalkanoates (PHAs), a group of biopolymers naturally synthesized by various microorganisms. Medium chain length PHAs (mcl-PHAs) are distinguished biopolymers due to their biodegradability and diverse material properties. Using quartz crystal microbalance measurements as a valuable tool for accurate real-time monitoring of the enzymatic degradation process, the research provides detailed kinetic data, describing the interaction between enzymes and substrates during the enzymatic degradation process. Thin films of poly-3-hydroxybutyrate (PHB) and polyhydroxyoctanoate copolymer (PHO), containing molar fractions of about 84% 3-hydroxyoctanoate and 16% 3-hydroxyhexanoate, were exposed to scl-depolymerases from Pseudomonas lemoignei LMG 2207 and recombinant mcl-depolymerase produced in Escherichia coli DH5α harboring the plasmid pMAD8, respectively. Analyses based on a heterogeneous kinetic model for the polymer degradation indicated a six-fold stronger adsorption equilibrium constant of mcl-depolymerase to PHO. Conversely, the degradation rate constant was approximately twice as high for scl-depolymerases acting on PHB. Finally, the study highlights the differences in enzyme-substrate interactions and degradation mechanisms between the investigated scl- and mcl-PHAs.},
keywords = {biodegradable polymers, degradation kinetics, depolymerase enzymes, enzymatic degradation, openQCM, openQCM Q-1, polyhydroxyalkanoates, Python, Quartz Crystal Microbalance},
pubstate = {published},
tppubtype = {article}
}
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