scholarly journals Production of ACE Inhibitory Peptides from Whey Proteins Modified by High Intensity Ultrasound Using Bromelain

Foods ◽  
2021 ◽  
Vol 10 (9) ◽  
pp. 2099
Author(s):  
Lucía Abadía-García ◽  
Eduardo Castaño-Tostado ◽  
Anaberta Cardador-Martínez ◽  
Sandra Teresita Martín-del-Campo ◽  
Silvia L. Amaya-Llano
Keyword(s):  
Protein Structure ◽  
Enzymatic Hydrolysis ◽  
Whey Protein ◽  
High Intensity ◽  
Whey Proteins ◽  
High Intensity Ultrasound ◽  
Peptide Profile ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

High Intensity Ultrasound (HIUS) can induce modification of the protein structure. The combination of enzymatic hydrolysis and ultrasound is an interesting strategy to improve the release of the Angiotensin-Converting Enzyme (ACE) inhibitory peptides. In this study, whey proteins were pretreated with HIUS at two levels of amplitude (30 and 50%) for 10 min, followed by hydrolysis using the vegetable protease bromelain. The hydrolysates obtained were ultrafiltrated and their fractions were submitted to a simulated gastrointestinal digestion. The conformational changes induced by HIUS on whey proteins were analyzed using Fourier-transform infrared spectroscopy by attenuated total reflectance (FTIR-ATR) and intrinsic spectroscopy. It was found that both levels of ultrasound pretreatment significantly decreased the IC50 value (50% Inhibitory Concentration) of the hydrolysates in comparison with the control (α = 0.05). After this treatment, HIUS-treated fractions were shown as smaller in size and fractions between 1 and 3 kDa displayed the highest ACE inhibition activity. HIUS promoted significant changes in whey protein structure, inducing, unfolding, and aggregation, decreasing the content of α-helix, and increasing β-sheets structures. These findings prove that ultrasound treatment before enzymatic hydrolysis is an innovative and useful strategy that modifies the peptide profile of whey protein hydrolysates and enhances the production of ACE inhibitory peptides.

Optimization of the Enzymatic Hydrolysis of Lupin (Lupinus) Proteins for Producing ACE-Inhibitory Peptides

2014 ◽  
Vol 62 (8) ◽  
pp. 1846-1851 ◽  
Author(s):  
Giovanna Boschin ◽  
Graziana Maria Scigliuolo ◽  
Donatella Resta ◽  
Anna Arnoldi
Keyword(s):  
Enzymatic Hydrolysis ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Hydrolysis Of ◽  
Ace Inhibitory

scholarly journals Enzymatic Hydrolysis of Ethanol-insoluble Proteins from Royal Jelly and Identification of ACE Inhibitory Peptides

2006 ◽  
Vol 53 (4) ◽  
pp. 200-206 ◽  
Author(s):  
Toshiro Matsui ◽  
Akiko Yukiyoshi ◽  
Shima Doi ◽  
Hiroya Ishikawa ◽  
Kiyoshi Matsumoto
Keyword(s):  
Enzymatic Hydrolysis ◽  
Royal Jelly ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Hydrolysis Of ◽  
Ace Inhibitory

Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides

2000 ◽  
Vol 67 (1) ◽  
pp. 53-64 ◽  
Author(s):  
ANNE PIHLANTO-LEPPÄLÄ ◽  
PÄIVI KOSKINEN ◽  
KATI PIILOLA ◽  
TUOMO TUPASELA ◽  
HANNU KORHONEN
Keyword(s):  
Whey Protein ◽  
Phase Method ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory Peptides ◽  
Protein Digests ◽  
Β Lactoglobulin ◽  
Ace Inhibitory

The aim of this study was to identify whey-derived peptides with angiotensin I-converting enzyme (ACE) inhibitory activity. The bovine whey proteins α-lactalbumin and β-lactoglobulin were hydrolysed with pepsin, trypsin, chymotrypsin, pancreatin, elastase or carboxypeptidase alone and in combination. The total hydrolysates were fractionated in a two step ultrafiltration process, first with a 30 kDa membrane and then with a 1 kDa membrane. Inhibition of ACE was analysed spectrophotometrically. The peptides were isolated by chromatography and identified by mass and sequencing analysis. The most potent inhibitory peptides were synthesized by the 9-fluorenylmethoxycarbonyl solid phase method. Inhibition of ACE was observed after hydrolysis with trypsin alone, and with an enzyme combination containing pepsin, trypsin and chymotrypsin. Whey protein digests gave a 50 % inhibition (IC50) of ACE activity at concentration ranges within 345–1733 μg/ml. The IC50 values for the 1–30 kDa fractions ranged from 485 to 1134 μg/ml and for the <1 kDa fraction from 109 to 837 mg/ml. Several ACE-inhibitory peptides were isolated from the hydrolysates by reversed-phase chromatography, and the potencies of the purified peptide fractions had IC50 values of 77–1062 μM. The ACE-inhibitory peptides identified were α-lactalbumin fractions (50–52), (99–108) and (104–108) and β-lactoglobulin fractions (22–25), (32–40), (81–83), (94–100), (106–111) and (142–146).

scholarly journals Identification of the Major ACE-Inhibitory Peptides Produced by Enzymatic Hydrolysis of a Protein Concentrate from Cuttlefish Wastewater

Marine Drugs ◽  
2014 ◽  
Vol 12 (3) ◽  
pp. 1390-1405 ◽  
Author(s):  
Isabel Amado ◽  
José Vázquez ◽  
Pilar González ◽  
Diego Esteban-Fernández ◽  
Mónica Carrera ◽  
...  
Keyword(s):  
Enzymatic Hydrolysis ◽  
Protein Concentrate ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Hydrolysis Of ◽  
Ace Inhibitory
Sign in / Sign up

Export Citation Format

Share Document