| Literature DB >> 27041318 |
K Elavarasan1, B A Shamasundar2, Faraha Badii3, Nazlin Howell3.
Abstract
The 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 β-sheet in FD-FPH samples. The approximate molecular weight of peptides in OD-FPH and FD-FPH was in the range of 7030-339Da. The IC50 values for ACE inhibition by OD-FPH and FD-FPH samples were found to be 1.15 and 1.53mg of proteinml(-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.Entities:
Keywords: ACE-inhibitory activity; Bioactive peptide; FT-IR spectra; Mrigal protein hydrolysate; Oven-drying
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Year: 2016 PMID： 27041318 DOI： 10.1016/j.foodchem.2016.03.047
Source DB: PubMed Journal: Food Chem ISSN： 0308-8146 Impact factor: 7.514