In this work, the partitioning of phenylalanine ammonia-lyase was investigated in different systems of PEG1000, PEG2000, PEG3350, PEG6000 and PEG8000 with (NH4)2SO4, Na2SO4, Na2CO3 and potassium phosphate. The results showed that the partition of phenylalanine ammonia-lyase in PEG/salt aqueous two-phase systems was mainly influenced by hydrophobicity, excluded volume effect and salting-out effect; compared with other PEG/salt systems, PEG1000/Na2SO4 was the most effective for phenylalanine ammonia-lyase partitioning. The result further supports that PEG/salt aqueous two-phase system provides a new and applicable route for the purification of phenylalanine ammonia-lyase, as shown in our published paper.1
<div><p>An efficient enzymatic process was developed to produce optically pure D-phenylalanine throu...
An efficient enzymatic process was developed to produce optically pure D-phenylalanine through asymm...
Phenylalanine ammonia-lyase (RgPAL) from Rhodotorula glutinis JN-1 stereoselectively catalyzes the c...
In this work, the partitioning of phenylalanine ammonia-lyase was investigated in different systems ...
Background: Phenylalanine dehydrogenase (PheDH; EC 1.4.1.20) is a NAD +-dependent enzyme that perfor...
Phenylalanine ammonia lyase (PAL) catalyzes the nonoxidative deamination of L-phenylalanine to form ...
The fermentation of phenylalanine ammonia lyase (PAL) by Rhodotorula mucilaginosa (R. mucilaginosa) ...
Aqueous two-phase system (ATPS) is an efficient, cost effective, fast, simple and ecofriendly method...
l-Phenylalanine ammonia-lyase (PAL, EC 4.3.1.25) from Rhodosporidium toruloides was utilized to remo...
Phenylalanine ammonia lyase (PAL) from Arabidopsis thaliana (AtPAL2) was comparatively characterized...
l-Phenylalanine ammonia-lyase (PAL, EC 4.3.1.25) from Rhodosporidium toruloides was utilized to remo...
Phenylalanine ammonia lyase (PAL, EC 4.3.1.24) catalyzes the conversion of phenylalanine (Phe) to tr...
AbstractPhenylalanine ammonia-lyase (RgPAL) from Rhodotorula glutinis JN-1 stereoselectively catalyz...
L-Phenylalanine ammonia-lyase (PAL, EC 4.3.1.25) from Rhodosporidium toruloides was utilized to remo...
Phenylalanine ammonia-lyase (EC 4.3.1.5) was purified to homogeneity from the acetone-dried powders ...
<div><p>An efficient enzymatic process was developed to produce optically pure D-phenylalanine throu...
An efficient enzymatic process was developed to produce optically pure D-phenylalanine through asymm...
Phenylalanine ammonia-lyase (RgPAL) from Rhodotorula glutinis JN-1 stereoselectively catalyzes the c...
In this work, the partitioning of phenylalanine ammonia-lyase was investigated in different systems ...
Background: Phenylalanine dehydrogenase (PheDH; EC 1.4.1.20) is a NAD +-dependent enzyme that perfor...
Phenylalanine ammonia lyase (PAL) catalyzes the nonoxidative deamination of L-phenylalanine to form ...
The fermentation of phenylalanine ammonia lyase (PAL) by Rhodotorula mucilaginosa (R. mucilaginosa) ...
Aqueous two-phase system (ATPS) is an efficient, cost effective, fast, simple and ecofriendly method...
l-Phenylalanine ammonia-lyase (PAL, EC 4.3.1.25) from Rhodosporidium toruloides was utilized to remo...
Phenylalanine ammonia lyase (PAL) from Arabidopsis thaliana (AtPAL2) was comparatively characterized...
l-Phenylalanine ammonia-lyase (PAL, EC 4.3.1.25) from Rhodosporidium toruloides was utilized to remo...
Phenylalanine ammonia lyase (PAL, EC 4.3.1.24) catalyzes the conversion of phenylalanine (Phe) to tr...
AbstractPhenylalanine ammonia-lyase (RgPAL) from Rhodotorula glutinis JN-1 stereoselectively catalyz...
L-Phenylalanine ammonia-lyase (PAL, EC 4.3.1.25) from Rhodosporidium toruloides was utilized to remo...
Phenylalanine ammonia-lyase (EC 4.3.1.5) was purified to homogeneity from the acetone-dried powders ...
<div><p>An efficient enzymatic process was developed to produce optically pure D-phenylalanine throu...
An efficient enzymatic process was developed to produce optically pure D-phenylalanine through asymm...
Phenylalanine ammonia-lyase (RgPAL) from Rhodotorula glutinis JN-1 stereoselectively catalyzes the c...