Immobilization of prostaglandin synthetase by hydrophobic adsorption |
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Authors: | Lin Ma Xu-Ting Wang De-Lin You Shuang Tang Zhong-Li Huang Yu-Hua Cheng |
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Institution: | (1) The National Laboratory of Enzyme Engineering, Jilin University, 130023 Changchun, China |
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Abstract: | In this article, the immobilization of prostaglandin synthetase onn-alkyl or aryl amino-agar beads by hydrophobic adsorption is reported. The effects of different hydrophobic groups in the
agar beads, pH of buffer, concentration of salts on the adsorption of prostaglandin synthetase, and the properties of immobilized
prostaglandin synthetase were also studied. The results showed that 20–35 mg of microsome containing PG synthetase (protein
content 8–15 mg) could be adsorbed on each gram ofn-dodecylamino-agar beads after suction drying the gel in the buffer of pH 5.5 (containing 0.5 mol/L KC1), 0.1 mol/L citric-phosphate
at 4‡C. The remaining immobilized enzyme activity was over 80%. The optimum pH of immobilized PG synthetase is 8.0, similar
to that of the native enzymes. The thermostability of immobilized PG synthetase in the buffer containing 0.5 mol/L KC1 was
increased. Immobilized PG synthetase was used as a catalyst of synthesis of prostaglandin E1. The preservation of activity after 10 working cycles was 86.2%. |
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Keywords: | Prostaglandin synthetase immobilization hydrophobic adsorption prostaglandin E1 |
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