摘要
Polyphenol oxidase was purified from leaves of Nicotiana tobaccum and the needle shape crystals were formed. The enzyme was immobilized on nylon membrane with glutaraldehyde as the cross linking agent. The appropriate conditions for immobilization were as follows: (1) The concentration of enzyme, 13 5 U/ml (concentration of protein: 0 03 mg/ml); (2) The optimum time for cross linking by glutaraldehyde was 20 minutes; (3)The optimum time for immobilization was 7 hours; (4) The optimum concentration of glutaraldehyde was 0 25%; (5) The optimum temperature was 4℃. The activity of immobilized enzyme reached 35—40 U/g matrix, and the activity recovery was 76 2% and the coupling efficiency was 76 3%. The stability of immobilized enzyme under acid, basic and high temperature conditions were enhanced and shifted toward basic pH range. It will be beneficial for industrial utilization.
Polyphenol oxidase was purified from leaves of Nicotiana tobaccum and the needle shape crystals were formed. The enzyme was immobilized on nylon membrane with glutaraldehyde as the cross linking agent. The appropriate conditions for immobilization were as follows: (1) The concentration of enzyme, 13 5 U/ml (concentration of protein: 0 03 mg/ml); (2) The optimum time for cross linking by glutaraldehyde was 20 minutes; (3)The optimum time for immobilization was 7 hours; (4) The optimum concentration of glutaraldehyde was 0 25%; (5) The optimum temperature was 4℃. The activity of immobilized enzyme reached 35—40 U/g matrix, and the activity recovery was 76 2% and the coupling efficiency was 76 3%. The stability of immobilized enzyme under acid, basic and high temperature conditions were enhanced and shifted toward basic pH range. It will be beneficial for industrial utilization.
出处
《中国生物化学与分子生物学报》
CAS
CSCD
1999年第4期662-666,共5页
Chinese Journal of Biochemistry and Molecular Biology
关键词
烟草
多酚氧化酶
分离
固定化
Nicotiana tobaccum
Polyphenol oxidase
Purification
Immobilization
