Crumbliss A L, Perine S C, Stonehuerner J, Tubergen K R, Zhao J, Henkens R W, O'Daly J P
Department of Chemistry, Duke University, Durham, North Carolina 27706, USA.
Biotechnol Bioeng. 1992 Aug 5;40(4):483-90. doi: 10.1002/bit.260400406.
Glucose oxidase, horseradish peroxidase, xanthine oxidase, and carbonic anhydrase have been adsorbed to colloidal gold sols with good retention of enzymatic activity. Adsorption of xanthine oxidase on colloidal gold did not result in a change in enzymatic activity as determined by active site titration with the stoichiometric inhibitor pterin aldehyde and by measurement of the apparent Michaelis constant (K'(M)). Gold sols with adsorbed glucose oxidase, horseradish peroxidase, and xanthine oxidase have also been electrodeposited onto conducting matrices (platinum gauze and/or glassy carbon) to make enzyme electrodes. These electrodes retained enzymatic activity and, more importantly, gave an electrochemical response to the enzyme substrate in the presence of an appropriate electron transfer mediator. Our results demonstrate the utility of colloidal gold as a biocompatible enzyme immobilization matrix suitable for the fabrication of enzyme electrodes.
葡萄糖氧化酶、辣根过氧化物酶、黄嘌呤氧化酶和碳酸酐酶已被吸附到胶体金溶胶上，酶活性得到了良好保留。通过用化学计量抑制剂蝶呤醛进行活性位点滴定以及测定表观米氏常数（K'(M)）来确定，黄嘌呤氧化酶吸附在胶体金上不会导致酶活性发生变化。吸附了葡萄糖氧化酶、辣根过氧化物酶和黄嘌呤氧化酶的金溶胶也已被电沉积到导电基质（铂丝网和/或玻碳）上以制备酶电极。这些电极保留了酶活性，更重要的是，在存在合适的电子转移介质的情况下，对酶底物产生了电化学响应。我们的结果证明了胶体金作为一种生物相容性酶固定化基质在制备酶电极方面的实用性。
