@article {181,
	title = {Reduction of l-phenylalanine in protein hydrolysates using l-phenylalanine ammonia-lyase from Rhodosporidium toruloides},
	journal = {Journal of Industrial Microbiology \& Biotechnology},
	volume = {42},
	year = {2015},
	pages = {1299{\textendash}1307},
	abstract = {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~{\textasciitilde}2.28~\%) was employed as a model substrate. t-Cinnamic acid resulting from deamination of l-Phe was extracted, analyzed at ${\l}ambda$~=~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~{\textdegree}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.},
	issn = {1476-5535},
	doi = {10.1007/s10295-015-1664-z},
	url = {http://dx.doi.org/10.1007/s10295-015-1664-z},
	author = {Casta{\~n}eda, Mar{\'\i}a T. and Adachi, Osao and Hours, Roque A.}
}
