| Autor: |
Castañeda MT; Research and Development Center for Industrial Fermentations (CINDEFI; UNLP, CONICET La Plata), School of Science, La Plata National University, 47 y 115, B1900ASH, La Plata, Argentina., Adachi O; Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Yamaguchi, 753-8515, Japan., Hours RA; Research and Development Center for Industrial Fermentations (CINDEFI; UNLP, CONICET La Plata), School of Science, La Plata National University, 47 y 115, B1900ASH, La Plata, Argentina. hours@biotec.org.ar.; Department of Chemical Engineering, National Technological University-La Plata Regional Faculty (UTN-FRLP), 60 y 124, La Plata, Argentina. hours@biotec.org.ar. |
| Abstrakt: |
L-Phenylalanine ammonia-lyase (PAL, EC 4.3.1.25) from Rhodosporidium toruloides was utilized to remove L-phenylalanine (L-Phe) from different commercial protein hydrolysates. A casein acid hydrolysate (CAH, L-Phe ~2.28 %) was employed as a model substrate. t-Cinnamic acid resulting from deamination of L-Phe was extracted, analyzed at λ = 290 nm, and used for PAL activity determination. Optimum reaction conditions, optimized using successive Doehlert design, were 35 mg mL(-1) of CAH and 800 mU mL(-1) of PAL, while temperature and pH were 42 °C and 8.7, respectively. Reaction kinetics of PAL with CAH was determined under optimized conditions. Then, removal of L-Phe from CAH was tested. Results showed that more than 92 % of initial L-Phe was eliminated. Similar results were obtained with other protein hydrolysates. These findings demonstrate that PAL is a useful biocatalyst for L-Phe removal from protein hydrolysates, which can be evaluated as potential ingredients in foodstuffs for PKU patients. |
