No abstract

Non-rubber components, mainly indicating phospholipid and protein, were separately removed from natural rubber to individually study their effect on structure and properties of the rubber. Fourier Transform Infrared Spectroscopy (FTIR) and 1 H nuclear magnetic resonance ( 1 H NMR) were applied to characterize the chemical structure and the non-rubber component residual. Rheology study and stress relaxation measurement were adopted to study the role non-rubbers played in natural networks. Rheological study of natural rubber (NR) and deproteinized natural rubber (DPNR) exhibited similar dynamic modulus at 170 o C. The lack of superposition in van Gurp Palmen (vGP) curves at different temperature for NR and DPNR, together with the shape of vGP curves proved that long chain branching was mainly constructed by phospholipid. Stress relaxation measurement at room temperature was fitted with Maxwell model and showed that NR relaxation curve underwent a quick decrease and then come to 58% equilibrium stress retention, about 3 times higher than that of DPNR, indicating that protein in NR contributed to the network structure at room temperature. Combined the chemical with molecule dynamic study, the interaction between protein and phospholipid in non-rubber component network was proposed.

A new approach to the development of functional biomaterials is to obtain a controllable nanostructure through supramolecular self-assembly.