| dc.creator | Castañeda, María Teresita | |
| dc.creator | Adachi, Osao | |
| dc.creator | Hours, Roque Alberto | |
| dc.date | 2015-10 | |
| dc.date | 2022-05-27T18:36:36Z | |
| dc.date.accessioned | 2023-07-15T05:10:53Z | |
| dc.date.available | 2023-07-15T05:10:53Z | |
| dc.identifier | http://sedici.unlp.edu.ar/handle/10915/136963 | |
| dc.identifier | issn:1476-5535 | |
| dc.identifier | issn:1367-5435 | |
| dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/7472388 | |
| dc.description | L-Phenylalanine ammonia-lyase (PAL, EC 4.3.1.25) from <i>Rhodosporidium toruloides</i> 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. | |
| dc.description | Centro de Investigación y Desarrollo en Fermentaciones Industriales | |
| dc.format | application/pdf | |
| dc.format | 1299-1307 | |
| dc.language | en | |
| dc.rights | http://creativecommons.org/licenses/by-nc-sa/4.0/ | |
| dc.rights | Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) | |
| dc.subject | Ciencias Exactas | |
| dc.subject | Phenylketonuria | |
| dc.subject | Phenylalanine ammonialyase | |
| dc.subject | Rhodosporidium toruloides | |
| dc.subject | Casein acid hydrolysate | |
| dc.subject | L-Phe removal | |
| dc.title | Reduction of L-phenylalanine in protein hydrolysates using L-phenylalanine ammonia-lyase from <i>Rhodosporidium toruloides</i> | |
| dc.type | Articulo | |
| dc.type | Articulo | |
