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Hevea brasiliensis rubber particles' fluid interfaces reveal size impact on early coagulation steps. | LitMetric

Hevea brasiliensis rubber particles' fluid interfaces reveal size impact on early coagulation steps.

Colloids Surf B Biointerfaces

IPR - UMR UR1 CNRS 6251, Rennes University, Rennes F-35000, France; ScanMAT - UAR 2025, Rennes University, Rennes F-35042, France. Electronic address:

Published: January 2025

AI Article Synopsis

  • Natural rubber comes from the coagulation of rubber particles found in the latex of the Hevea brasiliensis tree, comprising small rubber particles (SRP) and large rubber particles (LRP) with a bimodal size distribution.
  • This study investigates how these particles coagulate differently based on their size, examining their stability and behavior when placed at the air-liquid interface.
  • Results show that SRP adsorb and form films faster than LRP, with distinct behaviors observed during this process, influenced by specific proteins present in the rubber particles.

Article Abstract

Natural rubber originates from the coagulation of rubber particles (RP) from Hevea brasiliensis latex. The size distribution of Hevea RP is bimodal with the presence of small rubber particles (SRP) and large rubber particles (LRP). This study aims at getting a better understanding of the early coagulation steps of Hevea RP taking into account the particle size. SRP and LRP were obtained by centrifugation of freshly tapped ammonia-free latex from RRIM600 clone. Size and zeta potential measurements showed that both RP fractions were efficiently separated and stable in basic buffer. SRP and LRP dispersions were placed in a Langmuir trough and RP were let to adsorb at the air-liquid interface to form interfacial films. Surface tension and ellipsometry indicate that the formation kinetics and the stabilization of the film at the air-liquid interface are faster for SRP than LRP. Moreover, the arrangement of RP at the interface differs between SRP and LRP, as shown by Brewster angle microscopy, atomic force microscopy and confocal laser scanning microscopy. First, the RP membrane and cis-1,4-polyisoprene core spread at the air-liquid interface before clustering. Then, while the SRP fuse, the LRP keep their structure in individual particles in floating aggregate. The role of the non-isoprene molecules on the different organization of SRP and LRP films is discussed, the one of the two major RP proteins, SRPP1 (Small Rubber Particle Protein) and Rubber Elongation Factor (REF1) in the early coagulation steps.

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Source
http://dx.doi.org/10.1016/j.colsurfb.2024.114281DOI Listing

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