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Publication Type
Journal Article
UWI Author(s)
Author, Analytic
Goldson Barnaby, Andrea; Lam, M; Scaman, C; Clemens, S; Kermode, A.
Author Affiliation, Ana.
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Article Title
Screening of phenylalanine ammonia lyase in plant tissues, and retention of activity during dehydration.
Medium Designator
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Connective Phrase
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Journal Title
Journal of the Science of Food and Agriculture
Translated Title
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Reprint Status
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Date of Publication
2008
Volume ID
88
Issue ID
4
Page(s)
619-625
Language
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Connective Phrase
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Location/URL
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ISSN
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Notes
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Abstract
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 Ámol 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. Screening of phenylalanine ammonia lyase in plant tissues, and retention of activity during dehydration.....
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