Wu S, Lin J, Chan S I
Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena 91125.
Appl Biochem Biotechnol. 1994 Apr;47(1):11-20. doi: 10.1007/BF02788671.
We have encapsulated several hemoproteins in the sol-gel glass to catalyze the oxidation reaction of dibenzothiophene (model for organic sulfur compounds in coal) with hydrogen peroxide. In addition to cytochrome c and myoglobin, which have previously been encapsulated in sol-gel glasses, two other hemoproteins, horseradish peroxidase and bovine blood hemoglobin, have now been successfully immobilized in sol-gel media with the retention of their spectroscopic properties. All four hemoproteins studied also demonstrate similar catalytic activities toward the oxidation of dibenzothiophene as compared with the results obtained with the proteins in solution. In the case of encapsulated cytochrome c, the more water-soluble S-oxide was obtained with much higher selectivity over the less water-soluble sulfone (S-oxide/sulfone = 7.1) as compared to what was obtained in the aqueous/organic medium (S-oxide/sulfone = 2.3). Because of the advantage of easy separation of the encapsulated proteins from the liquid reaction mixture, it is clear from these studies that the immobilization of active hemoproteins in the solid glass media could serve as more practical biocatalysts.
我们已将几种血红素蛋白封装在溶胶 - 凝胶玻璃中，以催化二苯并噻吩（煤中有机硫化合物的模型）与过氧化氢的氧化反应。除了先前已封装在溶胶 - 凝胶玻璃中的细胞色素c和肌红蛋白外，另外两种血红素蛋白，辣根过氧化物酶和牛血血红蛋白，现已成功固定在溶胶 - 凝胶介质中，并保留了它们的光谱特性。与溶液中蛋白质的结果相比，所研究的所有四种血红素蛋白对二苯并噻吩的氧化也表现出相似的催化活性。对于封装的细胞色素c，与在水/有机介质中获得的结果相比（S - 氧化物/砜 = 2.3），以更高的选择性获得了水溶性更高的S - 氧化物，而不是水溶性较低的砜（S - 氧化物/砜 = 7.1）。由于从液体反应混合物中易于分离封装蛋白的优点，从这些研究中可以清楚地看出，将活性血红素蛋白固定在固体玻璃介质中可以用作更实用的生物催化剂。
