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jcoagri-1727
CHARACTERIZATION OF PHENYLALANINE AMMONIA LYASE PURIFIED FROM LOCALLY CULTIVATED GRAPE SEEDS (Vitis vinifera L.)
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This study was conducted to investigate certain characteristics of the purified Phenylalanine ammonia lyase (PAL). The results revealed that the molecular weight was 180 kDa by gel filtration and Native-PAGE. The optimal pH and temperature for enzyme activity were 7 and 40 °C respectively. The enzyme activity was stable against pH values range of 6-8. The enzyme retained 79% of its total activity after incubation for one hour at 50 °C and retained 7% (lost 93%) of its activity at 70 °C. The entire activity was completely lost when the enzyme was incubated for 1 hour at temperatures over 70 °C. Carbohydrate content of the purified enzyme was estimated to be 24.61%. Km, Kcat and Vmax were estimated with phenylalanine as substrate, the values were 0.021 mM, 20.67 sec-1 and 4.13 mM/min respectively.

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