Highly-purified natural rubber by saponification of latex: Analysis of residual proteins in saponified natural rubber

Abstract

Highly purified natural rubber (NR) was prepared by saponification of fresh latex (FL-latex) and preserved high-ammonia latex (HA-latex) in the presence of surfactant to reduce the residual proteins in resulting solid NR. Saponification of latex diluted to 30% DRC was carried out with 1-7% (w/v) sodium hydroxide at room temperature for 1-7 hr at 70 °C and coagulated with formic acid. The nitrogen content of NR obtained by coagulation of the saponified latex markedly decreased to less than 0.014% by centrifugation of the saponified latex or soaking the coagulum in aqueous sodium hydroxide solution. The nitrogenous compounds from saponified NR (SAP-NR) were extracted with sodium dodecyl sulphate (SDS) aqueous solution and subjected to SDS-Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis to check the molecular weight of extracts. The extract from SAP-NR and deproteinized NR by protease (DPNR) for comparison was subjected to the analysis of allergic protein by FIT Kit method, based on Enzyme-Linked Immunosorbent Assay (ELISA) method. No extractable protein was observed in SAP-NR, whereas DPNR contained 1.5 Hg/ml proteins. The results from SDS-PAGE analysis and FIT Kit test demonstrated that NR free from allergic proteins is obtainable by saponification of FL-latex with 1.5% NaOH at 70 0C for 1 hr or at room temperature for 24 hr.