| 醇脱氢酶在聚乙烯膜表面的固定化研究 |
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| 引用本文： | 郭梦雅,季书馨,谷凤娟,孟子晖,刘文芳,王燕子. 醇脱氢酶在聚乙烯膜表面的固定化研究[J]. 化工学报, 2020, 71(9): 4246-4254. DOI: 10.11949/0438-1157.20200509 |
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| 作者姓名： | 郭梦雅 季书馨 谷凤娟 孟子晖 刘文芳 王燕子 |
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| 作者单位： | 1.北京理工大学化学与化工学院，北京 102488;2.深圳大学化学与环境工程学院，广东 深圳 518060 |
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| 基金项目： | 北京市自然科学基金;中国博士后科学基金 |
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| 摘 要： | 以聚丙烯酸(PAA)改性的聚乙烯(PE)膜为载体,研究了醇脱氢酶(ADH)的两种固定化路线,并以甲醛为底物考察了固定化酶的催化性能。路线1用聚乙烯亚胺(PEI)进一步改性,使用戊二醛(GA)固定化ADH。最优固定化pH为6.0,温度为5～15℃,酶浓度为1.0 mg/ml,GA浓度为0.01%(质量);固定化酶的最适反应pH为6.5,温度为15～30℃,反应速率最高为9.6μmol/(L·min);重复利用10次后可保持47.3%的活性。路线2以PAA-PE为载体,用1-(3-二甲氨基丙基)-2-乙基碳二亚胺盐酸盐(EDC)和N-羟基琥珀酰亚胺(NHS)为活化剂,固定化ADH。EDC和NHS最优摩尔比为1∶0.5,固定化时间为24 h;固定化酶的最适反应pH为6.5,温度为20～37℃,反应速率为15.58μmol/(L·min);重复利用10次后可保持53.8%的活性。
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| 关 键 词： | 醇脱氢酶 聚乙烯膜 聚乙烯亚胺 酶固定化 共价结合 |
| 收稿时间： | 2020-05-08 |
Immobilization of alcohol dehydrogenase on the surface of polyethylene membrane |
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| GUO Mengya,JI Shuxin,GU Fengjuan,MENG Zihui,LIU Wenfang,WANG Yanzi. Immobilization of alcohol dehydrogenase on the surface of polyethylene membrane[J]. Journal of Chemical Industry and Engineering(China), 2020, 71(9): 4246-4254. DOI: 10.11949/0438-1157.20200509 |
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| Authors: | GUO Mengya JI Shuxin GU Fengjuan MENG Zihui LIU Wenfang WANG Yanzi |
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| Affiliation: | 1.School of Chemistry and Chemical Engineering, Beijing Institute of Technology, Beijing 102488, China;2.College of Chemistry and Environmental Engineering, Shenzhen University, Shenzhen 518060, Guangdong, China |
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| Abstract: | Using polyacrylic acid (PAA) modified polyethylene (PE) membrane as a carrier, two immobilization routes of alcohol dehydrogenase (ADH) were studied, and the catalytic performance of immobilized enzyme was investigated using formaldehyde as a substrate. In the first route, PAA-PE membrane was further modified by polyethyleneimine (PEI) and then ADH was covalently linked by glutaraldehyde (GA) to the surface of PEI/PAA-PE. The results show that the optimal immobilization pH was 6.0, immobilization temperature was 5—15℃, ADH and GA concentrations were 1.0mg/ml and 0.01%(mass). For immobilized enzyme, the optimal reaction pH was 6.5, temperature was 15—30℃, and the highest reaction rate was 9.6 μmol/(L·min), the remaining activity was 47.3% after 10 use cycles. In the second route, ADH was immobilized on PAA-PE membrane with 1-(3-dimethylaminopropyl)-2-ethylcarbodiimide hydrochloride (EDC) and N-hydroxysuccinimide (NHS) as activators. The results show that the optimal molar ratio of EDC and NHS was 1∶0.5, and the immobilization time was 24 h. For immobilized enzyme, the optimal reaction pH was 6.5, temperature was 20—37℃, and the highest reaction rate was 15.58 μmol/(L·min), 53.8% activity was remained after 10 cycles. |
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| Keywords: | alcohol dehydrogenase polyethylene film polyethylenimine enzyme immobilization covalently bonding |
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