Whey protein gelation induced by enzymatic hydrolysis and heat treatment: Comparison of creep and recovery behavior

2017 ◽  
Vol 63 ◽  
pp. 696-704 ◽  
Author(s):  
Maria Julia Spotti ◽  
Özgür Tarhan ◽  
Sam Schaffter ◽  
Carlos Corvalan ◽  
Osvaldo H. Campanella
2016 ◽  
Vol 61 ◽  
pp. 211-220 ◽  
Author(s):  
Ozgur Tarhan ◽  
Maria Julia Spotti ◽  
Sam Schaffter ◽  
Carlos M. Corvalan ◽  
Osvaldo H. Campanella

2020 ◽  
Vol 50 (3) ◽  
pp. 460-469
Author(s):  
Damir Zyaitdinov ◽  
Alexandr Ewteew ◽  
Anna Bannikova

Introduction. Bioactive compounds are a very popular topic of modern food science, especially when it concerns obtaining polyphenols from cereals. The antiradical, antioxidant, and anti-inflammatory properties of these ingredients allow them to inhibit and prevent coronary, artery, and cardiovascular diseases, as well as several types of cancer. Encapsulation is an effective technology that protects bioactive ingredients during processing and storage. In addition, it also prevents any possible interaction with other food constituents. The research objective was to obtain effective tools of controlled delivery of bioactive compounds. The study featured whey protein as a wall material in combination with maltodextrin to encapsulate the bioactives from oat bran. Study objects and methods. The processed material was oat bran. The technology of its biotransformation was based on ultrasound processing and enzymatic hydrolysis. The antioxidant properties were determined using a coulometer of Expert – 006-antioxidants type (Econix-Expert LLC, Moscow, Russia). Separation and quantitative determination of extract were followed using a Stayer HPLC device (Akvilon, Russia) and a system column Phenomenex Luna 5u C18(2) (250×4.6 mm). The total phenolic content was measured by a modified Folin-Ciocalteu method. To prepare microcapsules, whey protein concentrate (WPC) and maltodextrin (MD) solutions were mixed at ratios 6:4, 4:6, and 5:5. After that, the mixes were treated by ultrasonication and 10% w/w of guar gum solution as double wall material. The encapsulation efficiency (EE) was determined as a ratio of encapsulated phenolic content to total phenolic content. A digestion protocol that simulates conditions of the human gastric and intestinal tract was adapted to investigate the release kinetics of the extracts. Results and discussion. Ferulic acid is the main antioxidant in cereals. Its amount during extraction was consistent with published data: 9.2 mg/mL after ultrasound exposure, 9.0 mg/mL after enzymatic extraction, and 8.6 mg/mL after chemical treatment. The antioxidant activity of the obtained polyphenols was quite high and reached 921 cu/mL. It depended on the concentration of the preparation in the solution and the extraction method. The polyphenols obtained by ultrasonic exposure and enzyme preparations proved to have a more pronounced antioxidant activity. The highest EE (95.28%) was recorded at WPC:MD ratio of 60:40. In vitro enzymatic hydrolysis protocol simulating digestion in the gastrointestinal tract was used to study the effect of capsule structural characteristics on the kinetics of polyphenol release. The percentage of o polyphenols released from capsules ranged from 70% to 83% after two hours of digestion, which confirmed the effectiveness of microencapsulation technology. Conclusion. The research confirmed the possibility of using polyphenols obtained by the biotechnological method from oat bran as functional ingredients. Eventually, they may be used in new functional products with bifidogenic properties. Whey protein can be used to encapsulate polyphenols as the wall material of microcapsules.


2013 ◽  
Vol 411-414 ◽  
pp. 3205-3209
Author(s):  
Fang Qian ◽  
Lei Zhao ◽  
Shu Juan Jiang ◽  
Guang Qing Mu

Based on single factor analysis for the enzymatic hydrolysis of whey protein, papain was selected as the optimal enzyme and its enzymatic hydrolysis conditions were optimized by the quadratic regression orthogonal rotary test. The orthogonal regression model for degree of hydrolysis (DH) to three factors including temperature (X1), time (X2), enzyme dosage (X3) was established as follow: DH=10.40+0.22X1+0.30X2+1.31X3+0.019X1X2+0.011X1X3-0.039X2X3-0.39X12-0.16X22-0.40X32, Verification test showed a DH of 11.7% was obtained at the optimal hydrolysis condition of 56.6°C, 113.8 min and enzyme 8213.7 U /g protein, which basically consisted with the model theoretical value.


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

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.


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