enzyme hydrolysates from stichopus horrens as a new source for angiotensin-converting enzyme inhibitory peptides

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ID: 231261
2012
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Abstract
Stichopus horrens flesh was explored as a potential source for generating peptides with angiotensin-converting enzyme (ACE) inhibitory capacity using 6 proteases, namely alcalase, flavourzyme, trypsin, papain, bromelain, and protamex. Degree of hydrolysis (DH) and peptide profiling (SDS-PAGE) of Stichopus horrens hydrolysates (SHHs) was also assessed. Alcalase hydrolysate showed the highest DH value (39.8%) followed by flavourzyme hydrolysate (32.7%). Overall, alcalase hydrolysate exhibited the highest ACE inhibitory activity (IC50 value of 0.41 mg/mL) followed by flavourzyme hydrolysate (IC50 value of 2.24 mg/mL), trypsin hydrolysate (IC50 value of 2.28 mg/mL), papain hydrolysate (IC50 value of 2.48 mg/mL), bromelain hydrolysate (IC50 value of 4.21 mg/mL), and protamex hydrolysate (IC50 value of 6.38 mg/mL). The SDS-PAGE results showed that alcalase hydrolysate represented a unique pattern compared to others, which yielded potent ACE inhibitory peptides with molecular weight distribution lower than 20 kDa. The evaluation of the relationship between DH and IC50 values of alcalase and flavourzyme hydrolysates revealed that the trend between those parameters was related to the type of the protease used. We concluded that the tested SHHs would be used as a potential source of functional ACE inhibitory peptides for physiological benefits.
Reference Key
forghani2012evidence-basedenzyme Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Bita Forghani;Afshin Ebrahimpour;Jamilah Bakar;Azizah Abdul Hamid;Zaiton Hassan;Nazamid Saari
Journal ACS applied materials & interfaces
Year 2012
DOI
10.1155/2012/236384
URL
http://dx.doi.org/10.1155/2012/236384
Keywords
Other systems of medicine

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