FN Archimer Export Format
PT J
TI Optimization of common cuttlefish (Sepia officinalis) protein hydrolysate using Pepsin by Response Surface Methodology
BT 
AF KECHAOU, Emna
   BERGE, Jean-Pascal
   JAOUEN, Pascal
   BEN AMAR, Raja
AS 1:1,3;2:2;3:1;4:3;
FF 1:PDG-RBE-BRM-STBM;2:PDG-RBE-BRM-BIORAPHE;3:;4:;
C1 Univ Nantes, GEPEA UMR CNRS, F-44602 St Nazaire, France.
   IFREMER, Dept STAM, Nantes, France.
   Fac Sci Sfax Lab Mat Sci & Environm, Sfax, Tunisia.
C2 UNIV NANTES, FRANCE
   IFREMER, FRANCE
   UNIV SFAX, TUNISIA
SI NANTES
SE PDG-RBE-BRM-STBM
   PDG-RBE-BRM-BIORAPHE
IN WOS Ifremer jusqu'en 2018
   copubli-france
   copubli-univ-france
   copubli-int-hors-europe
   copubli-sud
IF 0.673
TC 4
UR https://archimer.ifremer.fr/doc/00182/29285/27715.pdf
LA English
DT Article
DE ;cuttlefish protein hydrolysate (CPH);amino acid;enzyme;Sepia officinalis
AB Protein hydrolysate was prepared from common cuttlefish Sepia officinalis by Pepsin. Hydrolysis conditions (time, temperature, and enzyme activity) were optimized by response surface methodology (RSM) using a factorial design. The regression coefficient was close to 0.999, observed during both experimental and validation runs, and indicated the validity of prediction model. An enzyme activity to substrate ratio (X1), 0.04 AU/g protein; time (X2), 85 minutes; and temperature (X3), 45 °C were found to be the optimum conditions for a higher degree of hydrolysis (21%) and nitrogen recovery (90%) using Pepsin. According to amino acid analysis results and chemical score, methionine and histidine are the limiting amino acids in the hydrolysates, in that order. All other amino acids are present in sufficient quantity as required.
PY 2015
PD APR
SO Journal Of Aquatic Food Product Technology
SN 1049-8850
PU Taylor & Francis Inc
VL 24
IS 3
UT 000351765500007
BP 270
EP 282
DI 10.1080/10498850.2013.773116
ID 29285
ER

EF