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Investigation of the Thermal Stability of Proteinase K for the Melt Processing of Poly(l-lactide)

Title data

Xu, Chengzhang ; Battig, Alexander ; Schartel, Bernhard ; Siegel, Renée ; Senker, Jürgen ; von der Forst, Inge ; Unverzagt, Carlo ; Agarwal, Seema ; Möglich, Andreas ; Greiner, Andreas:
Investigation of the Thermal Stability of Proteinase K for the Melt Processing of Poly(l-lactide).
In: Biomacromolecules. (3 November 2022) .
ISSN 1526-4602
DOI: https://doi.org/10.1021/acs.biomac.2c01008

Official URL: Volltext

Project information

Project financing: Deutsche Forschungsgemeinschaft

Abstract in another language

The enzymatic degradation of aliphatic polyesters offers unique opportunities for various use cases in materials science. Although evidently desirable, the implementation of enzymes in technical applications of polyesters is generally challenging due to the thermal lability of enzymes. To prospectively overcome this intrinsic limitation, we here explored the thermal stability of proteinase K at conditions applicable for polymer melt processing, given that this hydrolytic enzyme is well established for its ability to degrade poly(l-lactide) (PLLA). Using assorted spectroscopic methods and enzymatic assays, we investigated the effects of high temperatures on the structure and specific activity of proteinase K. Whereas in solution, irreversible unfolding occurred at temperatures above 75–80 °C, in the dry, bulk state, proteinase K withstood prolonged incubation at elevated temperatures. Unexpectedly little activity loss occurred during incubation at up to 130 °C, and intermediate levels of catalytic activity were preserved at up to 150 °C. The resistance of bulk proteinase K to thermal treatment was slightly enhanced by absorption into polyacrylamide (PAM) particles. Under these conditions, after 5 min at a temperature of 200 °C, which is required for the melt processing of PLLA, proteinase K was not completely denatured but retained around 2% enzymatic activity. Our findings reveal that the thermal processing of proteinase K in the dry state is principally feasible, but equally, they also identify needs and prospects for improvement. The experimental pipeline we establish for proteinase K analysis stands to benefit efforts directed to this end. More broadly, our work sheds light on enzymatically degradable polymers and the thermal processing of enzymes, which are of increasing economical and societal relevance.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Bioorganic Chemistry > Chair Bioorganic Chemistry - Univ.-Prof. Dr. Carlo Unverzagt
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Inorganic Chemistry III > Chair Inorganic Chemistry III - Univ.-Prof. Dr. Jürgen Senker
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Macromolecular Chemistry II > Chair Macromolecular Chemistry II - Univ.-Prof. Dr. Andreas Greiner
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Andreas Möglich
Research Institutions > Research Centres > Nordbayerisches Zentrum für NMR-Spektroskopie - NMR-Zentrum
Research Institutions > Affiliated Institutes > Bavarian Polymer Institute (BPI)
Research Institutions > Collaborative Research Centers, Research Unit > SFB 1357 - MIKROPLASTIK
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
600 Technology, medicine, applied sciences > 660 Chemical engineering
Date Deposited: 08 Nov 2022 07:45
Last Modified: 08 Nov 2022 10:48
URI: https://eref.uni-bayreuth.de/id/eprint/72708