响应面法优化藜麦种皮过氧化物酶固定化条件  被引量:3

Optimization of peroxidase immobilization conditions from Chenopodium quinoa bran using response surface methodology

在线阅读下载全文

作  者:范三红[1] 田贺贺 柴利萍 刘欢欢[1] 李晨[1] 

机构地区:[1]山西大学生命科学学院,山西太原030006

出  处:《食品工业科技》2017年第13期197-201,共5页Science and Technology of Food Industry

基  金:山西大学科研训练项目(2015013225);山西省青年科学基金(2015021047);山西省高校科技创新项目(2016116)

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。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, CaCl2 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 rain, the ratio of carrier to peroxidase of 1.25:1 (mL/mL).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.

关 键 词:藜麦种皮 过氧化物酶 响应面法 固定化 

分 类 号:TS201.1[轻工技术与工程—食品科学]

 

参考文献:

正在载入数据...

 

二级参考文献:

正在载入数据...

 

耦合文献:

正在载入数据...

 

引证文献:

正在载入数据...

 

二级引证文献:

正在载入数据...

 

同被引文献:

正在载入数据...

 

相关期刊文献:

正在载入数据...

相关的主题
相关的作者对象
相关的机构对象