Abstract:Using Pseudomonas stutzeri cells with synthetic activity, the crude lipases in different cell components were separated and obtained by ultrasonic destruction-solvent extraction, and the changes in the activities of lipases in different cell components under different conditions were determined. The results showed that the lipases with synthetic activity were localized in the cytoplasm, cell membrane, and cell wall of P. stutzeri cells, and the proportions of the corresponding synthetic activities in the whole cell were 47.25%, 22.70%, and 30.05%, respectively. The equilibrium time of the transesterification reaction catalyzed by lipases in the different components was higher than that for whole-cell catalysis. The lipases from different components showed the highest synthetic activity when the culture time was 48 h and soybean oil was used as the inducer. Based on the above study results, a production model of lipases in P. stutzeri cells was established. These results provide an important reference revealing the catalytic mechanism of whole-cell catalysis using P. stutzeri as a representative organism, and could promote the development and application of high-efficiency whole-cell biocatalysts.
