Journal
FOOD SCIENCE & NUTRITION
Volume 7, Issue 7, Pages 2381-2390Publisher
WILEY
DOI: 10.1002/fsn3.1097
Keywords
angiotensin-converting enzyme inhibitory; antibacterial activity; antioxidant activity; Chlorella sorokiniana
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Funding
- Ministry of Science and Technology, Taiwan [106-2311-B-019-001]
- Department of Science and Technology
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Chlorella sorokiniana protein isolates were enzymatically hydrolyzed using pepsin, bromelain, and thermolysin, with their molecular characteristics and bioactivities determined. Thermolysin hydrolysates exhibited the highest degree of hydrolysis (18.08% +/- 1.13%). The sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) results showed that peptides with molecular weights <10 kDa were found in the hydrolysates compared to the protein isolates. Bioactivity assays revealed that pepsin peptide fraction <5 kDa showed the highest angiotensin-converting enzyme (ACE)-inhibitory (34.29% +/- 3.45%) and DPPH radical scavenging activities (48.86% +/- 1.95%), while pepsin peptide fraction <10 kDa demonstrated the highest reducing power with 0.2101% +/- 0.02% absorbance. Moreover, antibacterial assessment revealed that pepsin hydrolysate and peptide fractions displayed inhibition to the test microorganisms. Overall, the present findings suggest that C. sorokiniana protein hydrolysates can be valuable bio-ingredients with pharmaceutical and nutraceutical application potentials.
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