Development of Reaction Element for Nonaquous Bioprocess

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An organic solvent-tolerant protease (PST-01 protease) from Pseudomonas aeruginosa PST-01 was purified and characterized. The PST-01 protease was stable in the presence of various organic solvents. Peptide syntheses were performed in monophasic aqueous solution containing an organic solvent using PST-01 protease. The initial reaction rate and the equilibrium yield of the peptide in the presence of 60%(v/v) DMSO were 5.1 times and 7.0 times higher than that in the absence of an organic solvent, respectively.Amphiphilic polymer particles which have hydrophilic guanidino groups and hydrophobic stearoyl groups were the best particles for the immobilization of Rhizopus delemar lipase. The hydrolytic activity of the immobilized lipase prepared with the amphiphilic polymer particles was 150-8700 times higher than those of the immobilized lipases prepared by previous investigators using Dowex MWA-1, porous glass beads, and Sepharose 4B. The stability and the transesterification activity of lipase were both enhanced by immobilizing lipase on the amphiphilic polymer particles. The specific transesterification activity of the immobilized lipase prepared with the amphiphilic polymer particles was 93.4 times higher than that of the lyophilized lipase.Surfactant-coated protease was prepared with a synthesized surfactant. The peptide synthetic activity and transeste rification activity of the surfactant-coated protease in organic solvents were higher than that of the powder protease. The activity of the surfactant-coated protease was 260 times higher that of the powder protease.