Vasudevan P T, Thakur D S
Department of Chemical Engineering, University of New Hampshire, Durham 03824.
Appl Biochem Biotechnol. 1994 Dec;49(3):173-89. doi: 10.1007/BF02783056.
This article examines the effect of pressure on the steady-state kinetics and long-term deactivation of the enzyme catalase supported on porous alumina. The reaction studied is the decomposition of hydrogen peroxide. The results of studies carried out in a continuous stirred-tank reactor under isothermal conditions are presented and compared with results obtained for soluble catalase. For soluble catalase, it is found that in the range of pressures studied, the oxygen flow rate increases with increase in pressure up to a certain value and then decreases. Hydrogen peroxide concentration appears to have a strong influence on pressure effects. With immobilized catalase, the pressure effects are not as prominent. Fluorescent microscopy studies of the immobilized enzyme suggest that this is probably because of pore diffusional limitations.
本文研究了压力对负载于多孔氧化铝上的过氧化氢酶的稳态动力学和长期失活的影响。所研究的反应是过氧化氢的分解。给出了在连续搅拌釜式反应器中在等温条件下进行的研究结果，并与可溶性过氧化氢酶的结果进行了比较。对于可溶性过氧化氢酶，发现在所研究的压力范围内，氧气流速随压力增加而增加，直至达到某一值，然后下降。过氧化氢浓度似乎对压力效应有很大影响。对于固定化过氧化氢酶，压力效应不那么显著。对固定化酶的荧光显微镜研究表明，这可能是由于孔扩散限制。
