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dc.contributor.authorJitlada Sansatsadeekulen_US
dc.contributor.authorJitladda Sakdapipanichen_US
dc.contributor.authorPorntip Rojruthaien_US
dc.contributor.otherMahidol Universityen_US
dc.date.accessioned2018-05-03T08:02:15Z-
dc.date.available2018-05-03T08:02:15Z-
dc.date.issued2011-06-01en_US
dc.identifier.citationJournal of Bioscience and Bioengineering. Vol.111, No.6 (2011), 628-634en_US
dc.identifier.issn13474421en_US
dc.identifier.issn13891723en_US
dc.identifier.other2-s2.0-79957614611en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=79957614611&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/11536-
dc.description.abstractNon-rubber components present in natural rubber (NR) latex, such as proteins and phospholipids, are presumed to be distributed in the serum fraction as well as surrounding the rubber particle surface. The phospholipid-protein layers covering the rubber particle surface are especially interesting due to their ability to enhance the colloidal stability of NR latex. In this study, we have characterized the components surrounding the NR particle surface and investigated their role in the colloidal stability of NR particles. Proteins from the cream fraction were proteolytically removed from the NR latex and compare to those from the serum fractions using SDS-polyacrylamide gel electrophoresis revealing that both fractions contained similar proteins in certain molecular weights such as 14.5, 25 and 27kDa. Phospholipids removed from latex by treatment with NaOH were analyzed using 1 H-NMR spectroscopy and several major signals were assignable to -(CH 2 ) n -, -CH 2 OP, -CH 2 OC=O and -OCH 2 CH 2 NH-. These signals are important evidence that indicates phospholipids associate with the rubber chain. The colloidal behavior of rubber lattices before and after removal of protein-lipid membrane was evaluated by zeta potential analysis and scanning electron microscope (SEM). The lowest zeta potential value of NR particles was observed at pH 10, consequently leading to the highest stability of rubber particles. Additionally, SEM micrographs clearly displayed a gray ring near the particle surface corresponding to the protein-lipid membrane layer. © 2011 The Society for Biotechnology, Japan.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=79957614611&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectChemical Engineeringen_US
dc.subjectImmunology and Microbiologyen_US
dc.titleCharacterization of associated proteins and phospholipids in natural rubber latexen_US
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.1016/j.jbiosc.2011.01.013en_US
Appears in Collections:Scopus 2011-2015

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