贾凌云

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教授

博士生导师

硕士生导师

主要任职:生物工程学院院长、党委副书记

性别:女

毕业院校:大连理工大学

学位:博士

所在单位:生物工程学院

学科:生物工程与技术. 生物化工

办公地点:知微楼519房间

电子邮箱:lyjia@dlut.edu.cn

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Facile Oriented Immobilization of Histidine-Tagged Proteins on Nonfouling Cobalt Polyphenolic Self-Assembly Surfaces

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论文类型:期刊论文

发表时间:2017-12-01

发表刊物:ACS BIOMATERIALS SCIENCE & ENGINEERING

收录刊物:SCIE、EI

卷号:3

期号:12

页面范围:3328-3337

ISSN号:2373-9878

关键字:tannic acid; cobalt; His-tagged proteins; oriented immobilization; nonfouling

摘要:In this study, a completely green and facile protocol to oriented immobilization of histidine-tagged (His-tagged) proteins based on plant polyphenolic tannic acid (TA) is described. This is the first time that TA has been applied as ionic chelators to immobilize His-tagged proteins. To reduce the nonspecific interactions between the TA and immobilized proteins, we assembled nonfouling zwitterionic poly(sulfobetaine methacrylate) (PSBMA) on the TA surface. The use of PSBMA could maintain the high activity of the His-tagged proteins and inhibit the adsorption of untagged protein to the TA surface. Subsequently, the obtained TA/PSBMA film was further chelated with Con for specific binding to a His-tagged protein. As Co-III is more stable and inert than Co-II, the chelated Co-II was oxidized to Co-III. Using this approach, His-tagged Chitinase was anchored to TA/PSBMA/Co-III film as a catalyst for the hydrolysis of chitin. The loading capacity of the film for the His-tagged Chitinase can reach similar to 4.0 mu g/cm(2). Moreover, the oriented immobilized Chitinase had high catalytic activity and excellent thermal and storage stability as well as being more resistant to proteolytic digestion by papain. This low-cost and green protein-oriented immobilization strategy may serve as a versatile platform for a range of applications, such as biomaterials, biocatalysis, sensors, drug delivery, and so on.