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http://krishi.icar.gov.in/jspui/handle/123456789/20637
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DC Field | Value | Language |
---|---|---|
dc.contributor.author | Elavarasan, K. | en_US |
dc.contributor.author | Shamasundar, B.A. | en_US |
dc.contributor.author | Badii, F. | en_US |
dc.contributor.author | Howell, N. | en_US |
dc.date.accessioned | 2019-06-19T08:08:07Z | - |
dc.date.available | 2019-06-19T08:08:07Z | - |
dc.date.issued | 2016-09-01 | - |
dc.identifier.citation | Elavarasan, K.,Shamasundar, B.A.,Badii, F. and Howell, N.(2016)-Angiotensin I-converting enzyme (ACE) inhibitory activity and structural properties of oven- and freeze-dried protein hydrolysate from fresh water fish (Cirrhinus mrigala). Food Chemistry. 206:210–216 | en_US |
dc.identifier.issn | 0308-8146 | - |
dc.identifier.uri | http://krishi.icar.gov.in/jspui/handle/123456789/20637 | - |
dc.description | Not Available | en_US |
dc.description.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 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.description.sponsorship | Not Available | en_US |
dc.language.iso | English | en_US |
dc.publisher | Elsevier | en_US |
dc.relation.ispartofseries | Not Available; | - |
dc.subject | Oven-drying | en_US |
dc.subject | ACE-inhibitory activity | en_US |
dc.subject | Mrigal protein hydrolysate | en_US |
dc.subject | FT-IR spectra | en_US |
dc.subject | Bioactive peptide | en_US |
dc.title | Angiotensin 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.title.alternative | Not Available | en_US |
dc.type | Research Paper | en_US |
dc.publication.projectcode | Not Available | en_US |
dc.publication.journalname | Food Chemistry | en_US |
dc.publication.volumeno | 206 | en_US |
dc.publication.pagenumber | 210–216 | en_US |
dc.publication.divisionUnit | Not Available | en_US |
dc.publication.sourceUrl | https://doi.org/10.1016/j.foodchem.2016.03.047 | en_US |
dc.publication.authorAffiliation | Department of Fish Processing Technology, Karnataka Veterinary, Animal and Fisheries Sciences University, Bidar, College of Fisheries, Mangalore | en_US |
dc.publication.authorAffiliation | Department of Nutrition and Food Safety, Faculty of Health and Medical Sciences, University of Surrey, Guildford GU2 7XH, UK | en_US |
dc.publication.authorAffiliation | ICAR::Central Institute of Fisheries Technology | en_US |
dc.ICARdataUseLicence | http://krishi.icar.gov.in/PDF/ICAR_Data_Use_Licence.pdf | en_US |
dc.publication.naasrating | 12.31 | en_US |
Appears in Collections: | FS-CIFT-Publication |
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