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《Chinese Journal of Biotechnology》 1993-01
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Immobilization of Trypsin on Sepharose Derivatives Using Various Covalent Bonding Methods

Xu Jun, Qi Jun Yuan Zhongyi (Shanghai Institute of Biochemistry, Shanghai 200032)  
Sepharose and its derivatives containing ABSE-,-NH_2,-COOH,-NCS and oxiran e groups were activated via chlorotriazine, dizaotization, glutaraldehyde or water-soluble carbodiimide and then used for immobilization of trypsin. The protein recoveries of the immobilized enzyme preparations via diazotization, chlorotriazine and glutaraldehyde were 59%, 93% and 28%, respectively, and the activity recoveries of these methods were 53%, 38% and 20%, respectively, better than those of the other four methods. These immobilized trypsin also showed high stabilities during repeated operations. Besides, the enzymatic properities, such as the optimum pH, temperature, Km and different activities of these imobilized trypsin preparations towards azocasein and BAPNA were studied in comparison to the native trypsin.
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