Angiotensin-I-Converting Enzyme Inhibitory and Antioxidant Activity of Tryptic Spirulina Platensis Protein Hydrolysates: Effect of Hydrolysis and in Vitro Gastrointestinal Digestion

Abstract

In this study, protein hydrolysates derived from Spirulina platensis protein (SPPHs) using trypsin were investigated in terms of angiotensin I-converting enzyme (ACE) inhibitory activity, antioxidant activity and total phenolic content (TPC) and subjected to an in vitro digestion model using human gastric and duodenal fluids. Moreover, the effects of hydrolysis time and enzyme/substrate (E/S) ratio on the degree of hydrolysis (DH) of the hydrolysates were determined. The maximum DH (%) was found as 25.03±0.89% with the combination of E/S ratio of 3:100, hydrolysis time of 8 hours (p<0.05). The highest ACE inhibitory activity value was observed as 21.79±1.52% for initial SPPHs, prepared within the hydrolysis conditions of E/S ratio of 3:100 and hydrolysis time of 8 h. In general, the increase in E/S ratio and hydrolysis time resulted in an increase in the DH and in an improved ACE inhibitory activity of both initial and the GI digested samples (p<0.05). After digestion by pepsin, TPC of the digests was in the range of 28.87±0.32 and 40.28±1.05mg caffeic acid equivalent/g dry weight. However, further digestion by pancreatin led TPC of the final GI digest between 19.85±1.24 and 29.00±1.00mg caffeic acid equivalent/g dry weight. Moreover, the antioxidant activity of further digested SPPHs by gastric and intestinal proteases remained generally stable after in vitro treatment.

Bioactivities of enzymatic protein hydrolysates derived from Chlorella sorokiniana

“…The presence of the essential amino acids greatly determines the quality and nutritive value of proteins to meet the requirements for animal body functions (Brown, Jeffrey, Volkman, & Dunstan, ; Yücetepe & Özçelik, ). It is observed in Table that the amino acid profiles of the protein isolates and hydrolysates were almost identical, suggesting that their protein quality is similar (Brown et al, ).…”