Optimization of some conditions of Neutrase-catalyzed plastein reaction to mediate ACE-inhibitory activity in vitro of casein hydrolysate prepared by Neutrase.
J Food Sci Technol
; 51(2): 276-84, 2014 Feb.
Article
em En
| MEDLINE
| ID: mdl-24493884
ABSTRACT
Casein hydrolysate was prepared by hydrolyzing casein with Neutrase and then modified by a Neutrase-catalyzed plastein reaction. The prepared hydrolysate had a degree of hydrolysis of 13.0% and exhibited ACE inhibition in vitro with an IC50 value of 40.4 µgâ
mL(-1). With the decreased amount of free amino groups of the modified hydrolysate as the response, some conditions of the plastein reaction including substrate concentration, enzyme to substrate ratio, reaction temperature and time were studied by single factor experiments and response surface methodology, and optimized finally as 62% (w/w), 3.0 kUâ
g(-1) peptides, 30 °C and 6.3 h, respectively. The maximum decreased amount of free amino groups of the modified hydrolysate prepared under these optimized conditions was 210.0 µmolâ
g(-1) peptides, while corresponding IC50 value was lowered to 14.7 µgâ
mL(-1). The present result indicates that Neutrase-catalyzed plastein reaction was capable of enhancing ACE-inhibitory activity in vitro of casein hydrolysate, and also highlights the importance of a forthcoming study to investigate the peptide compositions of the modified hydrolysate and the role of protease used in the plastein reaction.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Idioma:
En
Revista:
J Food Sci Technol
Ano de publicação:
2014
Tipo de documento:
Article