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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 IC 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.
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8469795 | PMC |
http://dx.doi.org/10.3390/foods10092099 | DOI Listing |
Food Res Int
November 2025
Ciência e Tecnologia de Alimentos, Centro de Ciências Agrárias, Universidade Estadual de Londrina, Celso Garcia Cid, PR-445, Km 380 - University Campus, Londrina, PR 86057-970, Brazil. Electronic address:
The objective of the research was to employ extrusion to increase the yield of simulated gastrointestinal digestion of protein corn gluten meal (CG). A single-screw extruder and a full factorial design with two center points were used. The optimal extrusion parameters were 40 % sample moisture, 140 °C and 54 rpm, resulting in a gastrointestinal digestion yield of 37.
View Article and Find Full Text PDFFood Chem
August 2025
Key Laboratory of Food Nutrition and Health in Universities of Shandong, College of Food Science and Engineering, Shandong Agricultural University, 61 Daizong Street, Tai'an, Shandong 271018, PR China. Electronic address:
This study aimed to explore the potential of garlic proteins for producing multifunctional salty peptides. Three novel salty peptides (SNDPGR, SASDPNF, and ASTCMAR) were identified through simulated hydrolysis and in silico screening. Sensory evaluation and electronic tongue analysis confirmed their potent saltiness, with dose-dependent salt-enhancing effects further validated by the electronic tongue.
View Article and Find Full Text PDFFood Chem
August 2025
College of Food Science and Engineering, Ocean University of China, Qingdao 266404, China. Electronic address:
Food-derived angiotensin-converting enzyme (ACE)-inhibitory peptide plays key roles in hypertension prevention, however, their activity is dependent on specific sequence composition. This study aims to enhance peptide activity using a module substitution strategy. Molecular docking and activity assays identified MF as a low- and FP as a high-contribution dipeptide module within MFPWP.
View Article and Find Full Text PDFFood Chem
September 2025
Institute of Food and Drug Research for One Health, Ludong University, Yantai, People's Republic of China; School of Food Engineering, Ludong University, Yantai, People's Republic of China. Electronic address:
Food-derived bioactive peptides exhibit therapeutic potentials in hypertension management in recent years. This review firstly synthesizes findings from a total of 62 relevant studies concerning the potentials of both plant- and animal-derived peptides. Secondly, the molecular targets and acting mechanisms underlying the antihypertensive effects of food-derived peptides are discussed.
View Article and Find Full Text PDFPrev Nutr Food Sci
August 2025
Department of Pharmaceutical Biology, School of Pharmacy, Bandung Institute of Technology, West Java 40132, Indonesia.
Peptides produced from soybean tempeh that inhibit angiotensin-converting enzyme (ACE) provide a promising source of novel antihypertensive agents. This study utilized two cysteine proteases (papain and bromelain) to generate ACE inhibitory peptides from the protein hydrolysate of soybean tempeh. The trials were arranged using a Box-Behnken design to achieve optimal hydrolysis conditions.
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