Premium
Determination of reaction kinetics of hydrolysis of tilapia ( O reochromis niloticus ) protein for manipulating production of bioactive peptides with antioxidant activity, angiotensin‐ I ‐converting enzyme inhibitory activity and C a‐binding properties
Author(s) -
Charoenphun Narin,
Youravong Wirote,
Cheirsilp Benjamas
Publication year - 2013
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/j.1365-2621.2012.03204.x
Subject(s) - chemistry , hydrolysis , antioxidant , kinetics , peptide , enzyme kinetics , enzyme , biochemistry , substrate (aquarium) , active site , biology , ecology , physics , quantum mechanics
Summary To manipulate enzymatic hydrolysis of tilapia ( O reochromis niloticus ) muscle protein for production of bioactive peptides, its reaction kinetics was intensively studied. The study showed that the production of peptides with different bioactive properties including antioxidant activity, angiotensin‐ I ‐converting enzyme ( ACE ) inhibition and C a‐binding property and their kinetics were affected by the degree of hydrolysis and substrate concentration. A comparative study on reaction kinetics found that the kinetic parameters for the production of each bioactive peptide are unique, that is, the maximum initial velocity, V max , for hydrolysis of protein was as high as 1.07 mg mL −1 min −1 , but that for the production of peptides with antioxidant activity and C a‐binding property were very low, range of 7.14–66.7 μg mL −1 min −1 , and that for the production of peptides with ACE inhibitory activity was the lowest, at 2.57 μg mL −1 min −1 . This knowledge of reaction kinetics of protein hydrolysis would be useful for manipulating and optimising the production of peptides with desired bioactive properties.