Optimization of peroxidase immobilization conditions from Chenopodium quinoa bran using response surface methodology
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摘要: 以从藜麦种皮中提取的过氧化物酶为原材料,利用0.2%聚乙烯醇-3%海藻酸钠（PVA-CA）为载体,Ca Cl2溶液作固定剂,采用包埋法对藜麦种皮过氧化物酶进行固定。在单因素实验的基础上,利用响应面分析法对藜麦种皮过氧化酶固定化的影响因素进行了优化。优化后得到的最佳固定化条件如下:氯化钙浓度为7%,固定化时间为26 min,载体与酶液的比例为1.25∶1（m L/m L）,在此条件下实际测得固定化酶的活性为416.5 U。实测值与理论值（417.4U）相差较小,充分验证了所建模型的可靠性。Abstract: The peroxidase extracted from Chenopodium quinoa bran were fixed by the method of embedment, using the peroxidase from Chenopodium quinoa as raw materials, 0.2% of polyvinyl alcohol and 3% of sodium alginate as the carrier, Ca Cl2 solution as fixative.On the basis of single factor experiments, the response surface methodology was employed to optimize the related influential immobilization conditions of peroxidase from Chenopodium quinoa bran. The results of optimum immobilization conditions were as follow: CaCl2 concentration of 7%, immobilization time of 26 min, the ratio of carrier to peroxidase of 1.25 ∶ 1 ( m L/m L) . With these conditions, the optimum activity of immobilization peroxidase from Chenopodium quinoa were obtained, and the activity of the peroxidase was 416.5 U. The experimental value was in high agreement with the predicted value ( 417.4 U) , which showed the validity of this response model.
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Keywords:
- Chenopodium quinoa bran /
- peroxidase /
- response surface /
- immobilization
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