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Effect of power ultrasound pretreatment on peptidic profiles and angiotensin converting enzyme inhibition of milk protein concentrate hydrolysates
Author(s) -
Uluko Hankie,
Liu Lu,
Li Hongjuan,
Cui Wenming,
Zhang Shuwen,
Zhao Lili,
Xue Haixiao,
Lv Jiaping
Publication year - 2014
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.6572
Subject(s) - hydrolysate , chemistry , peptide , chromatography , hydrolysis , enzyme , ultrasound , enzymatic hydrolysis , renin–angiotensin system , angiotensin converting enzyme , biochemistry , endocrinology , biology , medicine , radiology , blood pressure
BACKGROUND The use of power ultrasound as a pretreatment to enhance the hydrolysis of milk protein concentrate ( MPC ) and subsequent angiotensin converting enzyme ( ACE ) inhibitory activity has been studied. Liquid chromatography was used to analyse peptide profiles of Neutrase‐derived MPC hydrolysates after pretreatment at 0, 1, 3, 5 and 8 min at an ultrasound power level of 800 W. RESULTS The peptide profiles indicated an increase in number of peptides when ultrasound pretreatment was applied. There was also an increase in the degree of hydrolysis of MPC hydrolysates. The profiles indicated that new small peptides in ultrasound pretreated samples (1–5 min) which were not present in the control samples and 8 min pretreated samples, could be responsible for increased ACE inhibitory activity. These small peptides were digested in the 8 min pretreated samples. CONCLUSION Ultrasound pretreatment of MPC increases the ACE inhibitory activity of the hydrolysates because of the production of new small peptides. This can be used as a means to derive potent ACE inhibitory peptides at industrial scale in complex protein sources. © 2014 Society of Chemical Industry