Adsorption study of heme proteins on SBA-15 mesoporous silica with pore-filling models
Adsorption study of heme proteins on SBA-15 mesoporous silica with pore-filling models
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DOI：
10.1016/j.tsf.2005.07.046
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发表时间：
2006-03-21
期刊：
影响因子：
2.1
通讯作者：
Ariga, K
中科院分区：
文献类型：
--
作者：
Miyahara, M;Vinu, A;Ariga, K
肌红蛋白的朗缪尔型吸附发生在SBA-15内表面介孔通道的单层覆盖上。根据N-2吸附/脱附等温线计算出肌红蛋白在孔中的占有率约为50%。毛孔填充模型显示，肌红蛋白分子在毛孔中被很好地填充。在肌红蛋白的等电点附近观察到最大的吸附，这表明抑制蛋白质之间和/或蛋白质与吸附剂之间的电斥力起着重要作用。FT-IR光谱研究证实，肌红蛋白即使在吸附后也是稳定的。获得的结果与观察到的另一种氧化还原蛋白细胞色素c.(C)2005 Elsevier B.V.的结果相当。保留所有权利。
The Langmuir-type adsorption of myoglobin occurred with monolayer coverage of the inner surface mesopore channels of SBA-15. Myoglobin occupation of the pores was calculated as ca. 50% based on N-2 adsorption/desorption isotherms. Pore-filling models revealed that myoglobin molecules are well packed in the pores. The maximum adsorption was observed near the isoelectric point of myoglobin, suggesting the important role of suppression of electric repulsion between the proteins and/or between the protein and the adsorbent. FT-IR spectroscopic studies confirmed that the myoglobin is stable even after the adsorption. The results obtained are comparable with those observed for another redox protein, cytochrome c. (c) 2005 Elsevier B.V. All rights reserved.