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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/24322
Title: Nonuniformity in natural rubber as revealed by small-angle neutron scattering, small-angle x-ray scattering, and atomic force mircoscopy
Authors: Takeshi Karino
Yuko Ikeda
Yoritaka Yasuda
Shinzo Kohjiya
Mitsuhiro Shibayama
University of Tokyo
Kyoto Institute of Technology
Kyoto University
Japan Science and Technology Agency
Mahidol University
Keywords: Chemical Engineering;Materials Science
Issue Date: 1-Feb-2007
Citation: Biomacromolecules. Vol.8, No.2 (2007), 693-699
Abstract: The microscopic structures of natural rubber (NR) and deproteinized NR (DPNR) were investigated by means of small-angle neutron scattering (SANS), small-angle X-ray scattering (SAXS), and atomic force microscopy (AFM). They were compared to those of isoprene rubber (IR), which is a synthetic analogue of NR in terms of chemical structure without any non-rubber components like proteins. Comparisons of the structure and mechanical properties of NR, DPNR, and IR lead to the following conclusions. (i) The well-known facts, for example, the outstanding green strength of NR and strain-induced crystallization, are due not much to the presence of proteins but to other components such as the presence of phospholipids and/or the higher stereoregularity of NR. It also became clear the naturally residing proteins accelerate the upturn of stress at low strain. The protein phases work as cross-linking sites and reinforcing fillers in the rubbery matrix. (ii) The microscopic structures of NR were successfully reproduced by SANS intensity functions consisting of squared-Lorentz and Lorentz functions, indicating the presence of inhomogeneities in bulk and thermal concentration fluctuations in swollen state, respectively. On the other hand, IR rubbers were homogeneous in bulk. (iii) The inhomogeneities in NR are assigned to protein aggregates of the order of 200 Å or larger. Although these aggregates are larger in size as well as in volume fraction than those of cross-link inhomogeneities introduced by cross-linking, they are removed by deproteinization. (iv) Swelling of both NR and IR networks introduces gel-like concentration fluctuations whose mesh size is of the order of 20 Å. © 2007 American Chemical Society.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=33847278952&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/24322
ISSN: 15257797
Appears in Collections:Scopus 2006-2010

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