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  Proceedings of the Estonian Academy of Sciences. Chemistry

 

ISSN 1406-0124

Published since 1952 to 2007

Proceedings of the Estonian Academy of Sciences. Chemistry

 

ISSN 1406-0124

Published since 1952 to 2007

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Purification and properties of amine oxidase from pea seedlings; 164–171

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Authors

Kairi Kivirand, Toonika Rinken

Abstract

Amine oxidase (EC 1.4.3.6) was purified from pea (Pisum sativum) seedlings with the aim of characterizing its catalytic properties. The specific activity and selectivity of the enzyme were studied with an oxygen sensor by following the kinetics of the amine oxidation reaction, catalysed by the enzyme. The enzyme catalytic constants were calculated from the transient signal of the oxygen sensor with the help of a model proposed earlier for amperometric biosensors. The pea seedlings amine oxidase had the highest activity towards putrescine and cadaverine; a very low or zero activity was registered towards other studied amines. To characterize different steps of the purification process, we compared the activity of enzyme preparations towards 0.15 mM cadaverine. The molecular mass of the purified enzyme was 184.0 ± 2.6 kDa.

Keywords

amine oxidase, Pisum sativum, purification, enzyme activity, oxygen sensor.

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Current Issue: Vol. 56, Issue 4, 2007




Publishing schedule:
No. 1: 20 March
No. 2: 20 June
No. 3: 20 September
No. 4: 20 December