Effect of Proteins on the Network Formation and Degradation of Peroxide Cross-Linked Natural Rubber Elucidated by Time-Domain NMR
Issued Date
2025-04-01
Resource Type
eISSN
20734360
Scopus ID
2-s2.0-105003651206
Journal Title
Polymers
Volume
17
Issue
8
Rights Holder(s)
SCOPUS
Bibliographic Citation
Polymers Vol.17 No.8 (2025)
Suggested Citation
Nimpaiboon A., González-Jiménez A., Pérez-Aparicio R., Martín-Salamanca F., Zepeda-Rodríguez Z., López-Valentín J., Sakdapipanich J. Effect of Proteins on the Network Formation and Degradation of Peroxide Cross-Linked Natural Rubber Elucidated by Time-Domain NMR. Polymers Vol.17 No.8 (2025). doi:10.3390/polym17081063 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/109967
Title
Effect of Proteins on the Network Formation and Degradation of Peroxide Cross-Linked Natural Rubber Elucidated by Time-Domain NMR
Corresponding Author(s)
Other Contributor(s)
Abstract
The importance of sustainable polymers has increased greatly in the last years since most polymers are derived from non-renewable sources. Sustainable polymers (i.e., biopolymers) such as natural rubber (NR) are proposed as a solution for this concern. A comparative study between NR and deproteinized NR (DPNR) was carried out to elucidate the role of proteins on the network formation and degradation of peroxide cross-linked NR using time-domain NMR experiments. The 1H multiple-quantum (MQ) NMR experiments provided information on the cross-link density and its spatial distribution, while the actual fraction of non-coupled network defects was obtained by exploiting the Hahn echo approach measured on swollen samples. The results showed that proteins influenced the network formation during the vulcanization process of NR, leading to a higher number of non-elastic network defects and promoting the creation of additional cross-links with a broader spatial distribution. The formation of network heterogeneities in different length scales deeply influences the mechanical properties of NR samples. On the other hand, the proteins showed a pro-oxidant activity on the degradation behavior by accelerating the degradation process of peroxide cross-linked NR.