TY  - JOUR
T1  - Removal of Phenylalanine from Protein Hydrolysates Prepared with Rice
AU - , Daniella Cristine Fialho Lopes AU - , Carolina Schaper Bizzotto AU - , Raquel Linhares Carreira AU - , Wendel de Oliveira Afonso AU - , Carlos de Oliveira Lopes Jr AU - , Marialice Pinto Coelho Silvestre 
JO  - Journal of Food Technology
VL  - 6
IS  - 2
SP  - 57
EP  - 65
PY  - 2008
DA  - 2001/08/19
SN  - 1684-8462
DO  - jftech.2008.57.65
UR  - https://makhillpublications.co/view-article.php?doi=jftech.2008.57.65
KW  - Protein hydrolysates
KW  -rice
KW  -pancreatin
KW  -activated carbon
KW  -phenylalanine
AB  - Aiming the  preparation of  low-phenylalanine protein hydrolysates from rice, 2 pancreatins were used for the hydrolytic process and the activated carbon was used as adsorbent. Second derivative spectrophotometry was used to evaluate the efficiency of Phenylalanine (Phe) removal. Also, the peptide profiles of the protein hydrolysates were analysed. Initially, rice proteins were extracted by an alkaline process, varying the pH (9.0, 10.0 or 12.0), the stirring time (15 or 60 min) and the velocity of centrifugation (106, 425 or 2,660×g). Then,  12  protein  hydrolysates  were  prepared  using  2  different  Enzyme:  Substrate  (E:S) ratios (1 and 2%) and Rice Protein Extract (REP) concentrations (1-3 g/100  mL). The protein content of extracts changed from 19.63-77.92% and the highest extraction yield (84.74%) was obtained at pH 12.0, after stirring for 60 min and  centrifuging  at  425×g.   The   Phe   removal   was   similar   for   both   pancreatins,  varying  from 72-100% and giving final Phe contents from  0.28-95 mg/100 g of product. For pancreatin 1, the best results were obtained with REP concentration of  3% and E:S of 2%, while for pancreatin 2 REP concentrations as well as E:S of 1 and 2% produced the smallest Phe content. The peptide profile obtained with pancreatin 2 was more advantageous than pancreatin 1, since it produced much smaller large peptide and little higher oligopeptide contents.
ER  -