Kennedy J F, Kay I M
Carbohydr Res. 1977 Jul;56(2):211-8. doi: 10.1016/s0008-6215(00)83343-1.
The use of particles of porous titanium (IV) oxide as a suitable matrix for enzyme immobilisation has been investigated with dextranase. Treatment of the particles with enzyme in the presence and absence of ammonium ions showed that the presence of ammonia induced a greater coupling of protein, whereas a greater retention of enzyme specific activity was achieved in the absence of ammonia. Properties of the immobilised enzyme include a pH-dependence and reversibility of the coupling between enzyme and matrix. The immobilised dextranase was most stable at pH 5.0. Automated analytical techniques for measuring the activity of dextranase and other polysaccharidases in soluble and insoluble forms are also reported.
已经研究了使用多孔二氧化钛颗粒作为固定化酶的合适基质来固定右旋糖酐酶。在有和没有铵离子存在的情况下用酶处理颗粒，结果表明氨的存在会诱导更多的蛋白质偶联，而在没有氨的情况下能实现更高的酶比活性保留。固定化酶的特性包括酶与基质之间偶联的pH依赖性和可逆性。固定化的右旋糖酐酶在pH 5.0时最稳定。还报道了用于测量可溶性和不溶性形式的右旋糖酐酶及其他多糖酶活性的自动化分析技术。
