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| Study on Thermal Stability and Catalytic Specificity of Monoamine Oxidase in Oat Seedlings |
| ZHANG Yong-ming1,2, CUI Zhi-feng2, HIRASAWA Ei-ji2, WU Hai-xia3, LI Guo-long4 |
1. College of Life Science and Technology, Inner Mongolia Normal University, Hohhot 010022, China;
2. Department of Bio-GeoSciences, Osaka City University, Osaka 558-8585, Japan;
3. Institute of Inner Mongolia Water Resources, Hohhot 010020, China;
4. College of Agriculture, Inner Mongolia Agriculture University, Hohhot 010019, China |
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Abstract FAD-containing monoamine oxidase (MAO; EC 1.4.3.4) oxidises monoamines to their corresponding aldehydes, H2O2, and NH3 in organism. There are seldom reports about MAOs in plants. MAO activity was detected in oat seedlings during germination using benzylamine as substrate. The activities of oat seedlings growing in dark were higher than in light conditions. The activity, reached a peak after germinated for 3 days, was 2.5pKat/mg. and there are little difference about MAO activity in three parts of seedlings, shoots > roots > grains. The results of thermal stability shown oat MAO was unstable in room temperature after purified to homogenate successfully. 50% and 75% of oat MAO activity were lost after the 90-min incubation. Oat MAO shows high substrate specificities for benzylamine and phenethylamine, which are traditional MAO B specific substrates and are oxidised to benzaldehyde and phenylacetaldehde, but not for tyramine, serotonin, histamine or dopamine. The Km values for benzylamine and phenethylamine were 265μM and 705μM, respectively. Catalytic efficiency of oat MAO was lower than human MAO B and Aspergillus niger MAO.
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Received: 16 February 2012
Published: 25 July 2012
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