Enzymatic tempering of a mussel adhesive protein film
Enzymatic tempering of a mussel adhesive protein film
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DOI：
10.1021/la970881w
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发表时间：
1998-03-03
期刊：
影响因子：
3.9
通讯作者：
Waite, JH
中科院分区：
文献类型：
--
作者：
Hansen, DC;Corcoran, SG;Waite, JH
从贻贝中分离的粘附蛋白被吸附到高度定向的热解石墨上，并被酶氧化以产生紧密结合到基质上的硬化膜。使用原子力显微镜对表面和吸附的生物聚合物进行成像，表明在1 s的吸附时间内从溶液均匀覆盖基底。对于硬化膜，吸附蛋白质膜的膜厚度估计为25和73埃。使用范围从小于或等于20到大于或等于600 nN的成像力来分别确定不添加和添加儿茶酚氧化酶的粘附性蛋白质膜的稳定性。结果表明，通过酶促氧化，粘附蛋白膜对位移的抵抗力可以增强10倍。氧化可能导致吸附的蛋白质链之间形成共价交联。
An adhesive protein isolated from the marine mussel Mytilus edulis has been adsorbed to highly oriented pyrolytic graphite and enzymatically oxidized to yield a sclerotized film that is tightly bound to the substrate. Atomic force microscopy was used to image the surface and the adsorbed biopolymer, indicating uniform coverage of the substrate within 1 s of adsorption time from solution. Film thicknesses of the adsorbed protein films were estimated to be 25 and 73 Angstrom for the sclerotized films. Imaging forces ranging from less than or equal to 20 to greater than or equal to 600 nN were used to determine the stability of adhesive protein films without and with added catechol oxidase, respectively. Results indicate that the resistance of adhesive protein films to displacement can be enhanced 10-fold by enzymatic oxidation. Oxidation presumably leads to formation of covalent crosslinks between adsorbed protein chains.