Development of an Indirect Competitive ELISA Based on a Stable Epitope of β-Lactoglobulin for Its Detection in Hydrolyzed Formula Milk Powder DOI Creative Commons

Qinggang Xie,

Yuhao Huang, Xianli Zhang

et al.

Foods, Journal Year: 2024, Volume and Issue: 13(21), P. 3477 - 3477

Published: Oct. 30, 2024

The target of traditional immunological detection methods for milk allergens is usually the whole β-lactoglobulin molecule. However, thermal processes and hydrolysis can destroy epitope interfere with its accurate labeling in prepackaged foods, posing a health risk to milk-allergic patients. There currently remains need excavate locate recognition sites thermally processed hydrolyzed products. Therefore, stable (CAQKKIIAEKTKIPAVFKIDA) was selected as ideal site, an indirect competitive enzyme-linked immunosorbent assay (ELISA) developed using antibody against this order improve foods study. molecular dynamics simulation, binding ability anti-stable antibodies characterized ELISA ELISA. limit (LOD) quantitation (LOQ) established were 0.25 1.07 mg·kg

Language: Английский

Protein hydrolysates from Pleurotus spp. mushrooms as a source of antioxidant peptides and their stability after gastrointestinal digestion DOI

Daniela Fernanda Lima de Carvalho Cavenaghi,

Wander Miguel de Barros, Ruann Janser Soares de Castro

et al.

Food and Humanity, Journal Year: 2025, Volume and Issue: 4, P. 100519 - 100519

Published: Feb. 5, 2025

Language: Английский

Citations

0
Whey Protein Enzymatic Breakdown: Synthesis, Analysis, and Discovery of New Biologically Active Peptides in Papain-Derived Hydrolysates DOI Creative Commons
Michał Czelej, Katarzyna Garbacz, Tomasz Czernecki

et al.

Molecules, Journal Year: 2025, Volume and Issue: 30(7), P. 1451 - 1451

Published: March 25, 2025

Bioactive peptides derived from milk proteins offer promising potential that can be unlocked through hydrolysis. Enzymatic hydrolysis is particularly noteworthy because of its mild conditions and efficacy in producing with various biological activities. This study focused on creating whey protein hydrolysates using three enzymes: pepsin, trypsin, papain. The degree the antioxidant properties resulting were evaluated, papain demonstrated highest hydrolysis, leading to selection for further investigation. LC-MS was employed identify peptide sequences papain-derived hydrolysate, identification 107 distinct These predicted exhibit a range activities, including antihypertensive, antidiabetic, antioxidant, antimicrobial, immunomodulatory effects, as well roles regulating glucose homeostasis, maintaining cardiovascular health, supporting overall metabolic function. In vitro tests revealed significant antibacterial confirming use functional food pharmaceutical applications. novelty this lies novel Additional vivo studies are required fully elucidate health benefits these peptides.

Language: Английский

Citations

0
Biologically Active Dairy Protein Hydrolysates and Their Cyclodextrin Inclusion Complexes: Biotechnological Aspects of Production DOI Creative Commons
Tatsiana Halavach, З. В. Ловкис, В. П. Курченко

et al.

Food Processing Techniques and Technology, Journal Year: 2024, Volume and Issue: unknown, P. 461 - 482

Published: Oct. 2, 2024

Enzymatic hydrolysis of dairy proteins increases their nutritional and biological value while reducing allergenic potential. The subsequent complexation peptides with cyclodextrins (CDs) reduces the bitterness hydrolyzed proteins. research objective was to obtain hydrolysates whey cyclodextrin inclusion complexes peptides, as well describe peptide composition cleaved proteins, activity, sensory profile complexes. featured enzymatic protein an extensive degree β- γ-CDs. Dairy were alcalase, obtained subjected micro- ultrafiltration (cut-off limit – 10 kDa). determined by methods high-performance liquid chromatography chromatography-mass spectrometry. antimutagenic activity evaluated using Ames test whereas antibacterial effect studied impedimetric method. antioxidant detected fluorimetry spectrophotometry. method competitive enzyme immunoassay applied reveal antigenic properties. experimental sample s a evaluation. delivered optimal modes for cleavage alcalase that made it possible achieve efficient ultrafiltration. resulting hypoallergenic fractions γ-CDs possessed antioxidant, antibacterial, proteolysis filtration with/without tindalization demonstrated 265/589-fold decrease in residual antigenicity. fluorimetric showed 1.79/1.90-fold increase hydrolysate Binding β-CDs enhanced antimicrobial against Escherichia coli ATCC 8739 Staphylococcus aureus 6538. samples less bitterness. Whey under optimized conditions fractionation resulted product high consumer qualities. CD able substitute native components. Their bioactive properties, good taste, low potential mean prospects functional food industry.

Language: Английский

Citations

0
Development of an Indirect Competitive ELISA Based on a Stable Epitope of β-Lactoglobulin for Its Detection in Hydrolyzed Formula Milk Powder DOI Creative Commons

Qinggang Xie,

Yuhao Huang, Xianli Zhang

et al.

Foods, Journal Year: 2024, Volume and Issue: 13(21), P. 3477 - 3477

Published: Oct. 30, 2024

The target of traditional immunological detection methods for milk allergens is usually the whole β-lactoglobulin molecule. However, thermal processes and hydrolysis can destroy epitope interfere with its accurate labeling in prepackaged foods, posing a health risk to milk-allergic patients. There currently remains need excavate locate recognition sites thermally processed hydrolyzed products. Therefore, stable (CAQKKIIAEKTKIPAVFKIDA) was selected as ideal site, an indirect competitive enzyme-linked immunosorbent assay (ELISA) developed using antibody against this order improve foods study. molecular dynamics simulation, binding ability anti-stable antibodies characterized ELISA ELISA. limit (LOD) quantitation (LOQ) established were 0.25 1.07 mg·kg

Language: Английский

Citations

0