Isolation and characterisation of a novel angiotensin I-converting enzyme (ACE) inhibitory peptide from the algae protein waste
By I. Sheih, T. J. Fang, Tung-Kung Wu. 2009
265 citations recorded by the source corpus.
Subfields: Aquatic Science, Insect Science, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/afa5b32c48df468d3ba9e508d32e8d5dbecb0340
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In Aquatic Science
In Molecular Biology
Citations in the corpus
- Purification and identification of novel angiotensin-I converting enzyme (ACE) inhibitory peptides from cultured marine microalgae (Nannochloropsis oculata) protein hydrolysate (2013, background): “Sheih et al. (2009) has reported a purified peptide from Chlorella vulgaris protein waste with an IC50 value of 29.6 μM (Val-Glu-Cys-Tyr-GlyPro-Asn-Arg-Pro-Gln-Phe) and another study with the same microalga, isolated peptides from the pepsin hydrolysate, with IC50 values of 315.3, 63.8, 26.3, 57.1,…”