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牛肝过氧化氢酶作为催化剂裂解持续添加到缓冲溶液中的过氧化氢的效率。

Efficiency of bovine liver catalase as a catalyst to cleave H2O2 added continually to buffer solutions.

作者信息

Ibrahim M, Schlegel H G

出版信息

Biotechnol Bioeng. 1980 Sep;22(9):1895-1906. doi: 10.1002/bit.260220909.

Abstract

Empirical estimations of H2O2 concentration in a system containing bovine liver catalase and continually supplied with H2O2 were done to evaluate the efficiency of the enzyme to cleave H2O2. It was found that the continuous addition of H2O2 leads to the formation of steady-state concentrations of H2O2 in the medium. At a constant catalase concentration both the level and the duration of the steady state are dependent on the flow rate of H2O2. The increase of the catalase concentration in the medium does not change the steady-state level, it merely leads to the maintenance of the steady state for longer durations. At higher flow rates of H2O2, no steady state could be maintained, even when catalase was present in high excess. The incomplete cleavage of H2O2 by catalase under these conditions is due to the low affinity of catalase toward H2O2 (high K m value, apparent K m = 0.1M H2O2) and to the rapid inactivation of the enzyme during the continuous addition of H2O2.

摘要

为了评估牛肝过氧化氢酶裂解过氧化氢的效率,对含有该酶且持续供应过氧化氢的体系中的过氧化氢浓度进行了经验估计。结果发现,持续添加过氧化氢会导致培养基中过氧化氢形成稳态浓度。在过氧化氢酶浓度恒定的情况下,稳态的水平和持续时间均取决于过氧化氢的流速。培养基中过氧化氢酶浓度的增加不会改变稳态水平,只会使稳态维持更长时间。在过氧化氢流速较高时,即使存在大量过量的过氧化氢酶,也无法维持稳态。在这些条件下,过氧化氢酶对过氧化氢的不完全裂解是由于过氧化氢酶对过氧化氢的亲和力较低(米氏常数较高,表观米氏常数 = 0.1M过氧化氢)以及在持续添加过氧化氢过程中酶的快速失活。

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