Structural changes and cholesterol-lowering in denatured whey protein isolate: Malic acid combined enzymolysis

Lin, Min; Fu, Qian; Guo, Tingting; Ji, Qiuya; Zhou, Yibin

doi:10.1016/j.foodhyd.2022.107502

Cited by 16 publications

(23 citation statements)

References 95 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…After SDS and β-mercaptoethanol treatment, the secondary and tertiary structures of OVA and its hydrolysates were destroyed, and the intermolecular and intramolecular disulfide bonds were broken. The mobilities of OVA and its hydrolysates were only affected by the molecular weight. , Compared with OVA (lane 1), the hydrolysates showed a significantly shallower band at approximately 45 kDa and a clear band at approximately 25 kDa. Furthermore, all the hydrolysates showed multiple clear bands at <14.4 kDa.…”

Section: Resultsmentioning

confidence: 94%

“…The fluorescence intensity was determined using a fluorescence spectrometer (F-2700, Hitachi, Tokyo, Japan). 21 The fluorescence intensity of the samples of the excitation wavelength was 280 nm, the emission wavelength was from 290 to 500 nm, and the scanning speed was 1500 nm/min. Determination of Surface Hydrophobicity (H 0 ).…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

“…The final precipitate was dissolved in 4 mL of Tris-Gly standard containing 8 mol/L urea, 20 μL of Ellman's reagent was added and mixed well, then reacted at 25 °C for 30 min, and its absorbance was measured at 412 nm. 21 Mouse Model of Food Allergy. The allergy mouse model followed by Li et al 13 Sixty BALB/c mice (female, 3−4 weeks old) were purchased from Changsheng Biotechnology Co., Ltd. (Dalian, China).…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

“…The loading amount of each strip was 7.5 μL and first run at 30 V for 60 min and then at 100 V for 240 min. Finally, the color was stained in the dyeing solution for 1 h, and the color was decolorized in the decolorizing solution for 24 h …”

Section: Methodsmentioning

confidence: 99%

See 3 more Smart Citations

Mechanism of Targeted Regulation of Ovalbumin Epitopes by Pulsed Electric Field-Assisted Alcalase Treatment

Ding

Dong

et al. 2023

J. Agric. Food Chem.

View full text Add to dashboard Cite

Egg is one of the eight major food allergens, and ovalbumin (OVA) is the most abundant allergenic protein in eggs. In this study, the effects of pulsed electric field (PEF)-assisted Alcalase hydrolysis on the spatial conformation and potential allergenicity of OVA were studied, and the mechanism of its inhibiting allergic reactions effect was revealed. PEF-assisted Alcalase hydrolysis increased the degree of hydrolysis, surface hydrophobicity, and free sulfhydryl group content. Moreover, the reduction in the α-helix content, fluorescence intensity, and disulfide bond content suggested that PEF promoted the OVA hydrolysis by Alcalase. Additionally, enzyme-linked immunosorbent assay data indicated that PEF-assisted Alcalase hydrolysis hindered OVA binding to immunoglobulins E and G1. Finally, based on bioinformatics combined with mass spectrometry, PEF-assisted Alcalase reduced OVA-induced allergic reactions by destroying epitopes in OVA. Overall, PEF technology further destroyed the epitopes of allergens by targeting the binding sites of substrates and enzymes to improve the affinity of enzymes and substrates, reducing allergic reactions.

show abstract

Section: Resultsmentioning

confidence: 94%

Section: ■ Materials and Methodsmentioning

confidence: 99%

Section: ■ Materials and Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 2 more Smart Citations

Mechanism of Targeted Regulation of Ovalbumin Epitopes by Pulsed Electric Field-Assisted Alcalase Treatment

Ding

Dong

et al. 2023

J. Agric. Food Chem.

View full text Add to dashboard Cite

show abstract

“…Compared with microbial fermentation, the bioactive peptides obtained by enzymatic hydrolysis were more effective, shorter in reaction time, easy to expand ( 4 ), high in economic value, and high in safety ( 5 , 6 ). In the process of the enzymatic reaction, some short protein sequences that may perform biological functions and physiological activities can be released from proteins ( 7 ), and the hydrolysis processing could reduce the interference of starch and other components ( 8 ) and achieve a higher conversion rate ( 9 , 10 ). Thus, it was important to investigate the specific condition of enzymatic hydrolysis to obtain bioactive peptides.…”

Section: Introductionmentioning

confidence: 99%

Preparation and activity evaluation of angiotensin-I converting enzyme inhibitory peptides from protein hydrolysate of mulberry leaf

Chen

et al. 2023

Front. Nutr.

View full text Add to dashboard Cite

Angiotensin-I converting enzyme (ACE) inhibitory peptides drew wide attention in the food industry because of their natural reliability, non-toxicity, and safety. However, the characteristics of ACE inhibitory peptides obtained from protein hydrolysate of mulberry leaf prepared by Flavourzyme were still unclear. Based on the single-factor test, the Plackett–Burman test and response surface test were used to determine the key factors affecting the ACE inhibition rate in mulberry leaf protein hydrolysate and the optimum conditions of enzymatic hydrolysis. The results showed that the optimum technical parameters were as follows: the ratio of material to liquid is 1: 25 (w / v, g/mL), the Flavourzyme to substrate ratio was 3,000 U/g, the temperature of enzymatic hydrolysis was 50°C, pH was 6.3, and the time of enzymatic hydrolysis was 2.9 h. The ACE inhibitory peptides in the mulberry leaf protein hydrolysates were purified by ultrafiltration and gel filtration, aiming to obtain the highest active component. The 12 peptide sequences were identified by reverse liquid chromatography-mass spectrometry, and then, they were docked to the crystal structure of human angiotensin-I converting enzyme (1O8A), and the interaction mechanisms of 12 peptide sequences and 1O8A were analyzed. The docking results showed that among the 12 peptide sequences, ERFNVE (792.37 Da), TELVLK (351.72 Da), MELVLK (366.72 Da), and FDDKLD (376.67 Da), all had the lowest docking energy, and inhibition constant. The chemosynthetic ERFNVE (IC50: 2.65 mg/mL), TELVLK (IC50: 0.98 mg/mL), MELVLK (IC50:1.90 mg/mL) and FDDKLD (IC50:0.70 mg/mL) demonstrated high ACE-inhibitory activity with competitive inhibition mode. These results indicated that the ACE-inhibiting peptides from mulberry leaf protein hydrolyzed (FHMP) had the potential activities to inhibit ACE and could be used as functional food or drugs to inhibit ACE. This work provides positive support for mining the biological activity of mulberry leaves in the treatment of hypertension.

show abstract

Effect of Oat β-Glucan on the Structure and Properties of Soybean Protein Isolate During Maillard Reaction

Chu,

Zhang,

et al. 2023

Plant Foods Hum Nutr

View full text Add to dashboard Cite

Structural changes and cholesterol-lowering in denatured whey protein isolate: Malic acid combined enzymolysis

Cited by 16 publications

References 95 publications

Mechanism of Targeted Regulation of Ovalbumin Epitopes by Pulsed Electric Field-Assisted Alcalase Treatment

Mechanism of Targeted Regulation of Ovalbumin Epitopes by Pulsed Electric Field-Assisted Alcalase Treatment

Preparation and activity evaluation of angiotensin-I converting enzyme inhibitory peptides from protein hydrolysate of mulberry leaf

Effect of Oat β-Glucan on the Structure and Properties of Soybean Protein Isolate During Maillard Reaction

Contact Info

Product

Resources

About