Beef liver catalase was immobilized on the strongly basic ion-exange resin
Amberlite IRA-410, and used to study the kinetics of the reaction of hydrogen
peroxide decomposition. The process of the immobilization was also followed.
Rate constants for the enzymatic reaction were determined for the initial period
and for the reaction as a whole. Reuse of the immobilized enzyme was also examined.
Rate constants at four temperatures in the range 20—40 °C were determined
and the energy and entropy of activation were calculated from rate data.
Source:
J. Serb. Chem. Soc., 1988, 53, 11, 625-630
Publisher:
Srpsko hemijsko društvo
Funding / projects:
Research Fund of S.R. Serbia (Grant No.6447/3 /1986)
TY - JOUR
AU - Mijin, Dušan
AU - Nikolić, Vesna
AU - Mišić-Vuković, Milica
AU - Vuković, Dragoljub V.
PY - 1988
UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/5122
AB - Beef liver catalase was immobilized on the strongly basic ion-exange resin
Amberlite IRA-410, and used to study the kinetics of the reaction of hydrogen
peroxide decomposition. The process of the immobilization was also followed.
Rate constants for the enzymatic reaction were determined for the initial period
and for the reaction as a whole. Reuse of the immobilized enzyme was also examined.
Rate constants at four temperatures in the range 20—40 °C were determined
and the energy and entropy of activation were calculated from rate data.
PB - Srpsko hemijsko društvo
T2 - J. Serb. Chem. Soc.
T1 - The kinetic behavior of catalase immobilized on Amberlite IRA-410
EP - 630
IS - 11
SP - 625
VL - 53
UR - https://hdl.handle.net/21.15107/rcub_technorep_5122
ER -
@article{
author = "Mijin, Dušan and Nikolić, Vesna and Mišić-Vuković, Milica and Vuković, Dragoljub V.",
year = "1988",
abstract = "Beef liver catalase was immobilized on the strongly basic ion-exange resin
Amberlite IRA-410, and used to study the kinetics of the reaction of hydrogen
peroxide decomposition. The process of the immobilization was also followed.
Rate constants for the enzymatic reaction were determined for the initial period
and for the reaction as a whole. Reuse of the immobilized enzyme was also examined.
Rate constants at four temperatures in the range 20—40 °C were determined
and the energy and entropy of activation were calculated from rate data.",
publisher = "Srpsko hemijsko društvo",
journal = "J. Serb. Chem. Soc.",
title = "The kinetic behavior of catalase immobilized on Amberlite IRA-410",
pages = "630-625",
number = "11",
volume = "53",
url = "https://hdl.handle.net/21.15107/rcub_technorep_5122"
}
Mijin, D., Nikolić, V., Mišić-Vuković, M.,& Vuković, D. V.. (1988). The kinetic behavior of catalase immobilized on Amberlite IRA-410. in J. Serb. Chem. Soc.
Srpsko hemijsko društvo., 53(11), 625-630.
https://hdl.handle.net/21.15107/rcub_technorep_5122
Mijin D, Nikolić V, Mišić-Vuković M, Vuković DV. The kinetic behavior of catalase immobilized on Amberlite IRA-410. in J. Serb. Chem. Soc.. 1988;53(11):625-630.
https://hdl.handle.net/21.15107/rcub_technorep_5122 .
Mijin, Dušan, Nikolić, Vesna, Mišić-Vuković, Milica, Vuković, Dragoljub V., "The kinetic behavior of catalase immobilized on Amberlite IRA-410" in J. Serb. Chem. Soc., 53, no. 11 (1988):625-630,
https://hdl.handle.net/21.15107/rcub_technorep_5122 .
