Mechanism-Based Irreversible Inactivation of Horseradish Peroxidase at 500 MPa
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- 作者：Avelina Ferná ; ndez Garcí ; a ; Peter Butz ; and Bernhard Tauscher
- 刊名：Biotechnology Progress
- 出版年：2002
- 出版时间：October 2002
- 年：2002
- 卷：18
- 期：5
- 页码：1076 - 1081
- 全文大小：113K
- 年卷期：v.18,no.5(October 2002)
- ISSN：1520-6033
文摘
The effects of high-pressure treatment on the reaction rates of horseradish peroxidase(HRP) with guaethol or guaiacol as a hydrogen donor were evaluated from directtransmission measurements in a high-pressure optical cell at 435 nm. Peroxidasesare known to be very barostable and insensitive to heat. With guaethol the reactionvelocity was independent of pressure up to 500 MPa, but with guaiacol the cytochromec oxidase underwent a mechanism-based irreversible inhibition of catalytic activitywhen subjected to pressure; in the resting states (fully oxidized or reduced), it wasinsensitive to pressure. The enzyme inactivation took place with an inactivation rateconstant of 5.15 × 10-1 min-1 at 500 MPa, 25 
C and pH 7. The degree of inactivationwas correlated to the concentration of guaiacol. This is the first report on a mechanism-based pressure inactivation of HRP triggered at moderate pressure and temperatureand mediated by the hydrogen donor.
C and pH 7. The degree of inactivationwas correlated to the concentration of guaiacol. This is the first report on a mechanism-based pressure inactivation of HRP triggered at moderate pressure and temperatureand mediated by the hydrogen donor.