Structural characterization of α-terminal group of natural rubber. 1. Decomposition of branch-points by lipase and phosphatase treatments

Abstract

Deproteinized natural rubber latex (DPNR-latex) was treated with lipase and phosphatase in order to analyze the structure of the chain-end group (α-terminal). The enzymatic treatment decreased the content of long-chain fatty acid ester groups in DPNR from about 6 to 2 mol per rubber molecule. The molecular weight and intrinsic viscosity were reduced to about one-third after treatment with lipase and phosphatase. The Huggins' k′ constant of the enzyme-treated DPNR showed the formation of linear rubber molecules. The molecular weight distribution of DPNR changed apparently after treatment with lipase and phosphatase. 1H NMR spectrum of rubber obtained from DPNR-latex showed small signals due to monophosphate, diphosphate and phospholipids at the α-terminus. Treatment of DPNR-latex with lipase and phosphatase decreased the relative intensity of the 1H NMR signals corresponding to phospholipids, whereas no change was observed for the signals due to mono- and diphosphates. The residual mono- and diphosphate signals as well as some phospholipid signals after lipase and phosphatase treatments indicate that mono- and diphosphate groups are directly linked at the α-terminus with the modified structure, expected by aggregation or linking with phospholipid molecules. © 2005 American Chemical Society.