Screening of phenylalanine ammonia lyase in plant tissues, and retention of activity during dehydration
Screening of phenylalanine ammonia lyase in plant tissues, and retention of activity during dehydration
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DOI:
10.1002/jsfa.3126
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发表时间:
2008-03-01
影响因子:
4.1
通讯作者:
Kermode, Allison
中科院分区:
文献类型:
--
作者:
Goldson, Andrea;Lam, Melanie;Kermode, Allison
BACKGROUND: Oral therapy with phenylalanine ammonia lyase (PAL), naturally encapsulated in plant cells, may provide a potential alternative treatment for hyperphenylalaninemic patients, including those with phenylketonuria. Therefore different sources of plant tissue were investigated for PAL activity.RESULTS: Enzyme activity was highest in grain seedlings, with maximal enzyme activity in 7-day-old red spring wheat (Triticum aestivum L.) seedlings. The PAL activities of leaves and roots/endosperm of wheat seedlings were 11.90 +/- 2.64 and 6.48 +/- 1.59 mu mol h(-1) g(-1) dry weight respectively. Three PAL-related polypeptides with molecular weights of 74, 83 and 103 kDa were identified in wheat seedling leaf tissues, while only the 74 kDa polypeptide was detected in root/endosperm tissues. Dehydration was investigated as a method of concentrating PAL in wheat seedlings. Freeze-drying was found to retain the most PAL activity (> 90% recovery on a dry weight basis) compared with air drying and vacuum microwave drying for both leaf and root/endosperm samples.CONCLUSION: This study has led to a better understanding of PAL activity and stability in plant tissues and provides the basis for developing a natural plant preparation as a dietary supplement for the treatment of hyperphenylalaninemia. (c) 2007 Society of Chemical Industry.