New evidence disclosed for networking in natural rubber by dielectric relaxation spectroscopy.

Resolving the structure of natural rubber (NR) has been an important issue for a long time and essential progress has been made. It is well established that non-rubber components have significant effects on the performance of NR. A detailed discussion on the effects of proteins and phospholipids on the chain dynamics of NR will be crucial for the in-depth understanding of the role of proteins and phospholipids in NR. However, to date, there is still a lack of elaborate studies on the dielectric spectroscopy of NR. In the present study, we performed detailed dielectric relaxation analysis, together with rheological measurements, to reveal the effects of proteins and phospholipids on the chain dynamics of NR. Distinctly different from the widely accepted segmental mode (SM) and normal mode (NM), a new relaxation mode in deproteinized NR (DPNR) was identified for the first time, which cannot be found either in NR or in transesterified DPNR (TE-DPNR). Because this new mode relaxation process behaves as a thermally activated process and it is about four orders of magnitude slower than NM, it could be rationally attributed to the relaxation of the phospholipids core of DPNR, named branch mode (BM) relaxation. When further conversion of DPNR to TE-DPNR was conducted, the phospholipids were removed and BM disappeared. In addition, a new relaxation mode, which occurs at considerably lower temperature than that for SM, was revealed in TE-DPNR, and may be related to the relaxation of free mono- or di-phosphate groups at the α ends in TE-DPNR. Hence, the identification of the new relaxation modes in DPNR and TE-DPNR provide new evidence for the natural networking structure linked by protein-based ω ends and phospholipids-based α ends.