Screening of phenylalanine ammonia lyase in plant tissues,and retention of activity during dehydration

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 µmol 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. Copyright © 2007 Society of Chemical Industry