Angiotensin I-converting enzyme (ACE) inhibitory activity and structural properties of oven- and freeze-dried protein hydrolysate from fresh water fish (Cirrhinus mrigala)

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dc.contributor.authorElavarasan, K.
dc.contributor.authorShamasundar, B.A.
dc.contributor.authorBadii, F.
dc.contributor.authorHowell, N.
dc.date.accessioned2016-10-21T06:56:01Z
dc.date.available2016-10-21T06:56:01Z
dc.date.issued2016
dc.description.abstractThe angiotensin I-converting enzyme (ACE) inhibitory activity and structural properties of oven-dried (OD-FPH) and freeze-dried (FD-FPH) protein hydrolysates derived from fresh water fish (Cirrhinus mrigala) muscle, using papain, were investigated. Amino acid profiles indicated a higher proportion of hydrophobic residues in OD-FPH and hydrophilic residues in FD-FPH samples. Fourier transform infrared (FT-IR) spectra revealed random coil structure in OD-FPH and b-sheet in FD-FPH samples. The approximate molecular weight of peptides in OD-FPH and FD-FPH was in the range of 7030–339 Da. The IC50 values for ACE inhibition by OD-FPH and FD-FPH samples were found to be 1.15 and 1.53 mg of protein ml 1, respectively. The ACE-inhibitory activity of OD-FPH was more stable (during sequential digestion, using pepsin and pancreatin) than that of FD-FPH sample. The study suggested that the ACE inhibitory activity of protein hydrolysate was not affected by oven-drying.en_US
dc.identifier.citationFood Chemistry 206 (2016) 210–216en_US
dc.identifier.urihttp://hdl.handle.net/123456789/2331
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.subjectOven-dryingen_US
dc.subjectACE-inhibitory activityen_US
dc.subjectMrigal protein hydrolysateen_US
dc.subjectFT-IR spectraen_US
dc.subjectBioactive peptideen_US
dc.titleAngiotensin I-converting enzyme (ACE) inhibitory activity and structural properties of oven- and freeze-dried protein hydrolysate from fresh water fish (Cirrhinus mrigala)en_US
dc.typeArticleen_US
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