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Ultrasound‐assisted generation of ACE‐inhibitory peptides from casein hydrolyzed with nanoencapsulated protease
Author(s) -
Madadlou Ashkan,
Sheehan David,
EmamDjomeh Zahra,
Mousavi Mohammad E
Publication year - 2011
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.4438
Subject(s) - casein , chemistry , aspergillus oryzae , sonication , protease , hydrolysis , ultrafiltration (renal) , enzyme , chromatography , enzymatic hydrolysis , biochemistry , hydrolyzed protein
BACKGROUND: Bioactive peptides generated from milk proteins are eminent ingredients for functional foods and nutraceuticals. Amongst several approaches to release these peptides, hydrolysis of milk proteins with proteolytic enzymes is a promising choice. It is, however, required to inactivate the enzyme after a predetermined time, which leads to impurity of the final product. Immobilization of enzyme molecules can overcome this problem as it simplifies enzyme separation from the reaction mixture. A fungal protease from Aspergillus oryzea was encapsulated within nanoparticles yielded via silicification of polyamidoamine dendrimer template generation 0. It was used to hydrolyze the dominant milk protein (casein) in the absence or presence of sonication. The production of angiotensin converting enzyme (ACE)‐inhibitory peptides was monitored during hydrolysis. RESULTS: Sonication did not affect maximum ACE‐inhibitory activity but shortened the process sixfold. Ultrafiltration permeate of the centrifugal supernatant of casein solution hydrolyzed during sonication inhibited ACE activity as efficiently as the supernatant obtained from it. CONCLUSION: The protease from Aspergillus oryzea encapsulated within nanospheres is suitable for generation of ACE‐inhibitory peptides from casein. The nanoncapsulation procedure is simple, rapid and efficient. This may enable the industrial production of functional products from milk. Copyright © 2011 Society of Chemical Industry