BACKGROUND: Natural rubber latex contains allergenic proteins. Therefore, processes for deproteinizing the latex are needed. An immobilized enzyme process for deproteinization is reported. An optimal protocol was first developed for immobilizing a protease on cellulose−chitosan composite beads. The beads were then used in developing an optimal deproteinization treatment. The main effects and the interactions of the factors for the two processes were identified using a two-level full factorial experimental design.RESULTS: Under optimal conditions (15% cellulose in beads, immobilizing reaction pH of 9, immobilization period of 24 h), the beads attained the highest specific activity of 1685.3 U g −1 beads. Using these beads, the optimal conditions for deproteinization of the latex were: an enzyme loading of 0.1 parts per hundred of rubber (phr), a sodium dodecyl sulfate concentration of 20 phr, 30 • C, and a treatment period of 12 h. The nitrogen content of the rubber was reduced to 0.012% from an initial value of 0.3%. The enzyme beads were operationally stable and could be reused for at least five cycles. CONCLUSIONS:The optimized treatment effectively deproteinized the natural rubber. The final product was free of peptides. This deproteinization treatment was more effective than the conventional urea-based treatment performed for comparison.