Journal
INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY
Volume 51, Issue 7, Pages 1604-1609Publisher
WILEY-BLACKWELL
DOI: 10.1111/ijfs.13130
Keywords
Angiotensin I-converting enzyme inhibitory activity; Bacillus subtilis A26 hydrolysate; mass spectrometry; proteomics; thornback ray
Categories
Funding
- Ministry of Higher Education and Scientific Research of Tunisia
- Conselleria d'Educacio Cultura i Sport of Generalitat Valenciana [Prometeo/2012/001]
Ask authors/readers for more resources
Angiotensin I-converting enzyme (ACE) inhibitory peptides have been searched in thornback ray (Raja clavata) muscle hydrolysed with Bacillus subtilis A26 proteases until a hydrolysis degree of 18.35%. The hydrolysate showed an IC50 of 0.83mgmL(-1). To identify peptides responsible for this activity, the extract was eluted through size-exclusion chromatography and fractions collected. The highest ACE inhibitory activity was found for fractions F2 and F3 which had IC50 of 0.42 and 0.51mgmL(-1), respectively. These fractions were analysed by nano-liquid chromatography coupled to tandem mass spectrometry (nLC-MS/MS). A total of 131 and 108 peptide sequences mainly derived from actin, myosin heavy chain and procollagen alpha 1 chain proteins were identified in fractions F2 and F3, respectively. FQPSF and LKYPI showed the best results with an IC50 of 12.56 and 27.07M, respectively. These results prove the potential of thornback ray muscle hydrolysate as a source of ACE inhibitory peptides.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available