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Angiotensin I ‐converting enzyme inhibitory and C a‐binding activities of peptides prepared from tuna cooking juice and spleen proteases
Author(s) -
Kasiwut Jirawadee,
Youravong Wirote,
Adulyatham Pittaya,
Sirinupong Nualpun
Publication year - 2015
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/ijfs.12639
Subject(s) - chemistry , tuna , hydrolysate , proteases , food science , ultrafiltration (renal) , protease , chromatography , hydrolysis , enzyme , biochemistry , fish <actinopterygii> , biology , fishery
Summary Tuna cooking juice is a by‐product from the tuna canning industry. In this study, tuna cooking juice was hydrolysed by proteases extracted from the spleen. Tuna cooking juice showed the highest ACE inhibitory and Ca‐binding activities after hydrolysis for 270 and 180 min, respectively. The hydrolysate was further fractionated by ultrafiltration. The permeate exhibited highest ACE inhibitory and Ca‐binding activities when passed through 1 and 5 kDa cut‐off membranes, respectively. Gel filtration chromatography was used to determine the MW of bioactive peptides that exhibited highest ACE inhibitory and Ca‐binding activities. Those peptides that exhibited highest ACE inhibitory and Ca‐binding activities were the MW range of 238–829 Da and 1355–1880 Da, respectively. These results suggest that the tuna cooking juice and the spleen protease extract are a potential source of bioactive peptides that can be utilised as bioactive ingredients in functional food and nutraceuticals.