Purification and Characterization of Phenylalanine Ammonia Lyase from Trichosporon cutaneum

Table 2

Purification of the PAL enzyme from Trichosporon cutaneum ^a.

Method	Total activity^b (U)	Total protein (mg)	Specific activity (U/mg)	Purification fold	Yield (%)
Anion exchange
Crude	0.05±0.01	0.38±0.09	0.15±0.00	—	100
Post	0.01±0.00	0.001±0.00	7.39±0.73	49.6	20
Acid precipitation
Crude	0.16±0.03	1.04±0.74	0.20±0.10	—	100
Post	0.15±0.04	0.61±0.28	0.26±0.06	1.3	94
Aqueous two-phase^c
Crude	0.07±0.03	0.39±0.14	0.21±0.05	—	100
PEG/Na2SO4	0.02±0.00	0.08±0.00	0.33±0.03	1.5	28
PEG/(NH4)2SO4	0.02±0.00	0.10±0.08	0.10±0.04	0.5	28
PEG/ Na2CO3	0.01±0.00	0.31±0.04	0.02±0.01	0.1	14

 ^aResults are the average ± range of two independent trials. Crude samples are cell culture extracts obtained from a PD-10 column. ^b1 U of activity = 1 𝜇moL of released tran-cinnamic acid per min. ^cFor aqueous two-phase partitioning, the same crude enzyme extraction was used for each of the PEG/salt systems.