Effects of hydrolysis and digestion in vitro on the activity of bovine plasma hydrolysates as inhibitors of the angiotensin I converting enzyme

Abstract

The angiotensin I-converting enzyme (ACE) inhibiting activity of bovine plasma hydrolyzates obtained by Alcalase 2.4 L at different degrees of hydrolysis (DH) was evaluated. For the evaluation of ACE inhibition (ACEI), HippurylHis-Leu was used as substrate and the amount of hippuric acid liberated by non-inhibiting ACE was determined by spectrophotometry at 228 nm. The results showed that the enzymatic hydrolysis increased the ACEI activity as compared with the un-hydrolyzed plasma. The highest activity was onbtained with a DH of 6.7%. The peptide fractions with the maximum activity were isolated using ultrafiltration membranes, ion exchange chromatography and high performance liquid chromatography on reverse phase (RP-HPLC

Use of Alcalase in the production of bioactive peptides: A review

“…In this study, the results showed that peptides with the highest angiotensin I-converting enzyme inhibition activities were produced after five hours of hydrolysis, using 10% Alcalase enzyme [510]. In another research, hydrolysates from bovine plasma were obtained by Alcalase at different degrees of hydrolysis [511]. The highest angiotensin I-converting enzyme inhibition activity was obtained with a hydrolysis degree of 6.7%.…”

Production and characterization of chicken blood hydrolysate with antihypertensive properties

“… Deng et al. (2014) reported that porcine hemoglobin hydrolyzed by pepsin exhibited the highest ACE-inhibitory activity at a 9.3%DH, whereas Sampedro and Montoya (2014) found that bovine plasma hydrolysates obtained from Alcalase 2.4 L showed the maximum ACE-inhibitory activity of 50.2% at a 6.7% DH. The porcine BC hydrolyzed by a mixture of thermolysin, chymotrypsin, and trypsin also had an IC 50 value for ACE-inhibitory activity of 0.58 mg/mL ( Wei and Chiang, 2009 ).…”

“…The ACE-inhibitory peptides of the BCH-III digesta could play an important role in the antihypertensive effect. The digesta of bovine plasma and porcine globin also showed an ACE inhibition that was compared with that of their parent hydrolysates ( Yu et al., 2006 ; Sampedro and Montoya, 2014 ).…”

“…The optimal hydrolysis condition is varied with blood proteins and proteases applied. Sampedro and Montoya (2014) reported that Alcalase-hydrolyzed bovine plasma showed the highest ACE-inhibiting activity, with a degree of hydrolysis ( DH ) of 6.7%, whereas the hydrolysate of red blood cells obtained from a mixture of trypsin, chymotrypsin, and thermolysin showed the highest ACE-inhibitory activity, with the half maximal inhibitory concentration ( IC 50 ) of 0.58 mg/mL ( Wei and Chiang, 2009 ). In addition, the pepsin hydrolysate obtained by hydrolyzing porcine hemoglobin at a pH of 2.0 and a temperature of 37°C for 6 h exhibited the highest ACE-inhibitory activity, with an IC 50 of 0.02 mg/mL ( Deng et al., 2014 ).…”

Preparation and purification of angiotensin‐converting enzyme inhibitory peptides from hydrolysate of shrimp (Litopenaeus vannamei) shell waste

“…Various ACE inhibitory peptides have been isolated from food proteins, such as bone protein (Cheng et al, 2008), soya protein (Rho et al, 2009), pea protein (Barbana & Boye, 2010), bovine plasma (Sampedro & Montoya, 2014) and skate skin (Ngo et al, 2014). Proteases such as neutral protease, alcalase, papain, flavourzyme and bromelain are frequently used in the hydrolysis to produce ACE inhibitory peptides (Qu et al, 2010;Deng et al, 2014;Mohtar et al, 2014).…”