Antioxidant and angiotensin I converting enzyme (ACE) inhibitory activities of date seed protein hydrolysates prepared using Alcalase, Flavourzyme and Thermolysin

Abstract

A B S T R A C TDate seed flour was used to produce protein hydrolysates using Alcalase (AL), Flavourzyme (FL) and Thermolysin (TH). Enzymes were used individually or in combination at a constant pH and temperature. The degree of hydrolysis ranged between 11 and 14%. The molecular weights of peptides determined, using a quadrupole orthogonal time-of-flight hybrid tandem mass spectrometer, ranged from 2062.9 ± 0.0 to 116,803.8 ± 0.4 Da. AL hydrolysate showed the lowest reducing power and ABTS radical scavenging activity, but a higher ACE inhibition and hydroxyl radical scavenging. Among all treatments, hydrolysates prepared using a combination of AL and FL exhibited the highest reducing power and metal chelation and high scavenging for ABTS, DPPH, hydroxyl radicals as well as ACE inhibitory activity. Combinations of AL and TH exhibited the highest ACE inhibitory activity with an IC50 value of 0.53 mg/mL. These results indicate that date seed protein hydrolysate could be used as a potential health promoting ingredient with antioxidant and ACE inhibitory activities.

Thermal and single frequency counter‐current ultrasound pretreatments of sodium caseinate: enzymolysis kinetics and thermodynamics, amino acids composition, molecular weight distribution and antioxidant peptides

“…Reducing power reflects the electron donating ability of antioxidant . The reducing powers of the control, HT and SFCU hydrolysates are significantly ( P < 0.5) different (Fig.…”

Phenolic Profile of Peanut By‐products: Antioxidant Potential and Inhibition of Alpha‐Glucosidase and Lipase Activities

“…Phenolic extracts were tested for their scavenging activity against hydroxyl radicals. The extracts were removed from their original solvent (methanol) under a stream of nitrogen and diluted in 75 mM phosphate buffer [16]. Experimental procedure and equipment parameters were the same as those described by de Camargo et al [10].…”

Identification and synthesis of multifunctional peptides from wheat germ hydrolysate fractions obtained by proteinase K digestion

“…The 12 peptide fractions obtained by RP‐HPLC were tested for in vitro antioxidant and ACE‐inhibitory activities. The ABTS assay was found to be more sensitive than the DPPH assay, possibly because the ABTS radical is able to react with any hydroxylated aromatic compound and thus can be applied to assess the antioxidant activity of both lipophilic and hydrophilic molecules (Ambigaipalan et al, ). The F 1 –F 12 fractions (numbered in order of elution in RP‐HPLC) displayed ABTS scavenging and ACE‐inhibitory activities in the 5%–89% and 8%–70% range, respectively (Figure ).…”

“…Globally, Table 3 shows a predominance of hydrophobic (Ala, Val, Ile, Leu, Met, Phe, Pro, Gly) and aromatic (Phe, Trp, Tyr) residues (31.73% and 21.64%, respectively). Both classes of amino acid side chains can donate protons to electron-deficient radicals hence affect antioxidant activity (Silva et al, 2017); other side chains such as Met, Lys, Cys, and His have also been reported to enhance antioxidant activity (Ambigaipalan, Al-Khalifa, & Shahidi, 2015). Girgih et al (2014) indicated that the presence of hydrophobic amino acids affected antihypertensive activity positively.…”