Isolation and characterization of angiotensin I-converting enzyme (ACE) inhibitory peptides from Ulva rigida C. Agardh protein hydrolysate

Paiva, Lisete; Lima, Elisabete; Neto, Ana I.; Baptista, José

doi:10.1016/j.jff.2016.07.006

Cited by 77 publications

(53 citation statements)

References 44 publications

(54 reference statements)

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“…Pool‐2 exhibited a stronger ACE‐inhibitory activity (50%) than Pool‐1 (17%) at a concentration of 5 µg peptide mL −1 . In accordance with other studies, Pool‐1 eluted early because it contained a group of larger peptides than Pool‐2, confirming that smaller peptides have stronger ACE inhibitory activity (Chen et al , ; Rui et al , ; Paiva et al , ).…”

Section: Resultssupporting

confidence: 88%

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Angiotensin‐I‐converting enzyme (ACE)‐inhibitory peptides from Thai jasmine rice bran protein hydrolysates

Suwannapan

Wachirattanapongmetee

Thawornchinsombut

et al. 2020

Int J of Food Sci Tech

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Rice bran protein hydrolysate (<50 kDa RBPH) from Thai jasmine variety demonstrating a high Angiotensin I converting enzyme (ACE) inhibitory activity was purified and characterised. ACE inhibitory peptides were obtained from a two-step purification process: gel filtration and preparative reverse-phase high-performance chromatography (RP-HPLC) and then identified by mass spectrometer hybrid quadrupole-time-of-flight. A novel peptide GSGYF in the RBPH was firstly identified and found to have a partial sequence homology of Oryza sativa Japonica Group. This sequence was further synthesised to exhibit as good an inhibition potency with IC 50 value of 2.11 µg mL À1 as Captopril (1.15 µg mL À1 ). The cytotoxicity test revealed that this RBPH is non-toxic against Vero cells. In addition, the <50 kDa RBPH was resistant to in vitro digestion by pepsin and trypsin. These findings suggest that the RBPH containing ACE inhibitory peptides is likely to be safer and healthier than synthetic drugs and can be an effective food supplement for lowering blood pressure.

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Section: Resultssupporting

confidence: 88%

“…Our previous study showed that the <50 kDa RBPH contained two major bands with molecular sizes between 15.6–29 kDa and 3.7–10.5 kDa (Kaewjumpol, ). These results suggest that the potency of ACE‐inhibitory activity depends essentially on the size of the peptides (Chen et al , ; Rui et al , ; Paiva et al , ).…”

Section: Resultsmentioning

confidence: 96%

Angiotensin‐I‐converting enzyme (ACE)‐inhibitory peptides from Thai jasmine rice bran protein hydrolysates

Suwannapan

Wachirattanapongmetee

Thawornchinsombut

et al. 2020

Int J of Food Sci Tech

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“…As to the knowledge of the researchers, there are no reports on the ACE‐inhibitory activities of hydrolysates from microalgae using bromelain and thermolysin. However, for macroalgae, Paiva, Lima, Neto, and Baptista () stated that bromelain hydrolysate from Ulva rigida showed the highest ACE‐inhibitory activity among other hydrolysates in the study. Moreover, Ghanbari et al () accounted that the bromelain hydrolysate from sea cucumber exhibited one of the highest ACE‐inhibitory activities among other hydrolysates produced using various proteases.…”

Section: Resultsmentioning

confidence: 82%

Bioactivities of enzymatic protein hydrolysates derived from Chlorella sorokiniana

Tejano

Peralta

Yap

et al. 2019

Food Science & Nutrition

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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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“…to the reports that peptides in the lowest molecular size fractions of protein hydrolysates from black soybean, [14] gram flour [35] and macroalgae [36] had the highest ACE inhibitory activities. Then, the U-I was further separated with gel filtration chromatography (Sephadex G-25) into four fractions (FI, FII, FIII, and FIV).…”

Section: Purification Of the Ace Inhibitory Peptidesmentioning

confidence: 70%

Isolation and identification of the angiotensin-I converting enzyme (ACE) inhibitory peptides derived from cottonseed protein: optimization of hydrolysis conditions

Gao

Zhang²,

Ma³

et al. 2019

International Journal of Food Properties

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Peptides derived from food proteins have exhibited significant antihypertensive effects without side effects. In this study, the cottonseed protein was hydrolyzed by papain for preparing peptide with angiotensin I converting enzyme (ACE) inhibitory activity. The influence of hydrolysis temperature (33°C, 40°C, and 47°C), pH (6.5, 7.0, and 7.5), and enzyme to substrate (E/S) ratio (0.9%, 1.2%, and 1.5%) on the degree of hydrolysis (DH) and ACE-inhibitory activity were analyzed. The hydrolysis conditions were further optimized by central composite design (CCD) and response surface methodology (RSM). The DH of cottonseed protein and ACE inhibitory rate of hydrolysates reached 25.7% and 88.2%, respectively, under the optimal hydrolysis conditions (hydrolysis temperature 39°C, pH 7.5, and E/S ratio 1.04%). We further separated the cottonseed protein hydrolysates (CPH) using a combined strategy of ultrafiltration membrane bioreactor system, sephadex G-25 gel filtration chromatography and reversed-phase high-performance liquid chromatography (RP-HPLC). An ACE inhibitory peptide, named as FII-2-P, with ACE inhibitory IC 50 value of 46.7 μg/mL, was obtained. MALDI-TOF-TOF mass spectrometry analysis revealed that the molecular weight of FII-2-P was 763.4 Da and its amino acids sequence was Phe-Pro-Ala-Ile-Gly-Met-Lys. These results demonstrated that the cottonseed protein is a potential source of ACE inhibitory ingredients to be used in the development of functional foods.

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Isolation and characterization of angiotensin I-converting enzyme (ACE) inhibitory peptides from Ulva rigida C. Agardh protein hydrolysate

Cited by 77 publications

References 44 publications

Angiotensin‐I‐converting enzyme (ACE)‐inhibitory peptides from Thai jasmine rice bran protein hydrolysates

Angiotensin‐I‐converting enzyme (ACE)‐inhibitory peptides from Thai jasmine rice bran protein hydrolysates

Bioactivities of enzymatic protein hydrolysates derived from Chlorella sorokiniana

Isolation and identification of the angiotensin-I converting enzyme (ACE) inhibitory peptides derived from cottonseed protein: optimization of hydrolysis conditions

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