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机构地区:[1]辽宁工程技术大学理学院,辽宁阜新123000
出 处:《应用化工》2017年第12期2342-2345,共4页Applied Chemical Industry
基 金:国家自然基金青年基金项目(51304114);大学生创新创业训练计划项目(201610147000046)
摘 要:以马铃薯为原料,提取其中的多酚氧化酶,采用改性蛭石为载体,对其进行固定化,研究游离与固定化酶的最适催化温度、pH值,固定化酶的储存稳定性、重复使用稳定性及对苯酚的清除性能。结果表明,改性后蛭石出现了较多沟壑状孔隙,颗粒质感疏松,有利于固定化酶分子;最佳固定化条件为:改性蛭石含量0.4 g,戊二醛浓度2.0%,搅拌时间2 h,在此条件下,酶活力回收率可达到60.67%;游离与固定化酶的最适催化温度均为50℃,最适催化pH值均为7.0;固定化酶4℃下储存28 d后酶活力可保留52.1%,具有较好的储存稳定性;重复使用5次后,仍能保持61.0%的初始活性,说明固定化酶构象较稳定,固定化马铃薯多酚氧化酶对苯酚具有较好的清除性能。Polyphenol oxidase is extracted from potatoes and immobilized by modified vermiculite as carrier. The optimum catalytic temperature and pH of free enzyme and immobilized enzyme,the storage stability,reusing stability and the phenol removal performance of immobilized enzyme are studied. The results show that after modification,there are many gully pores and the granule texture is loose,which is beneficial to immobilized enzyme molecules. The best immobilized condition requires 0. 4 g of vermiculite,glutaldehyde with a concentration of 2%,two-hour-long stirring. The recovery rate of enzyme activity can reach 60. 67% under this condition. The optimum catalytic temperature of both free enzyme and immobilized enzyme is 50 ℃. The optimum catalytic pH is 7. After storing for 28 d at 4 ℃,enzyme activity remains 52. 1% and still has good stability. It can still keep 61% of initial activity after reusing for 5 times which suggests a stable conformation of immobilized enzyme. The immobilized polyphenol oxidase of potatoes has good properties of scavenging phenol.
分 类 号:TQ925.9[轻工技术与工程—发酵工程] TQ589
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