AI Article Synopsis
- The study investigated the impact of ohmic heating (OH) on collagen from eel skin, focusing on thermal denaturation and allergenicity.
- Allergenicity decreased by around 70% at 50 °C, while molecular weight remained stable but showed reduced band strength in SDS-PAGE.
- OH was more efficient than water bath heating, needing less time and energy, and effectively reduced fish skin collagen allergenicity through changes in protein structure.
Article Abstract
This study aimed to evaluate the effect of ohmic heating (OH) on the thermal denaturation, structure, and allergenicity of collagen in fresh eel skin. The allergenicity of collagen decreased by approximately 70% at 50 °C as measured by simulated gastric fluid (SGF), simulated intestinal fluid (SIF) and ELISA in vitro. SDS-PAGE analysis showed that the molecular weight of collagen did not decrease, but the band strength decreased with an increase in the processing temperature. FTIR and SEM analyses showed that the secondary structure and microstructure of collagen also changed. The water retention, dielectric properties and amino acid content of collagen also decreased with increasing temperature. Compared to water bath heating (WH), OH required significantly less time and energy and reduced the allergenicity of fish skin collagen through protein unfolding and secondary structure changes, thus potentially reducing the allergenicity of eel.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.foodchem.2022.133272 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Characterization and film-forming properties of collagen from three species of sea cucumber from the South China Sea: Emphasizing the effect of transglutaminase.
Int J Biol Macromol
January 2025
College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, China; Shenzhen Institute of Guangdong Ocean University, Shenzhen 518108, China; National Research and Development Branch Center for Shellfish Processing (Zhanjiang), Zhanjiang 524088, China; Guangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, Guangdong Provincial Engineering Technology Research Center of Seafood, Zhanjiang 524088, China. Electronic address:
This study aimed to investigate the structural characteristics of Stichopus horrens collagen (SHC), Holothuria scabra collagen (HSC), and Holothuria leucospilota collagen (HLC) and to assess the effect of transglutaminase (TGase) on their film-forming properties. The results indicated that the collagens from three species of sea cucumbers were type I collagen with a complete triple helical structure. The thermal denaturation temperature of HLC (34.
View Article and Find Full Text PDFExploring the Effect of Hydrocarbon Cross-Linkers on the Structure and Binding of Stapled p53 Peptides.
Proteins
January 2025
Department of Chemistry, Indian Institute of Technology Bombay, Mumbai, India.
Short-length peptides are used as therapeutics due to their high target specificity and low toxicity; for example, peptides are designed for targeting the interaction between oncogenic protein p53 and E3 ubiquitin ligase MDM2. These peptide therapeutics form a class of successful inhibitors. To design such peptide-based inhibitors, stapling is one of the methods in which amino acid side chains are stitched together to get conformationally rigid peptides, ensuring effective binding to their partners.
View Article and Find Full Text PDFCounterintuitive DNA destabilization by monovalent salt at high concentrations due to overcharging.
Nat Commun
January 2025
Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Renmin Hospital of Wuhan University, Wuhan University, Wuhan, China.
Monovalent salts are generally believed to stabilize DNA duplex by weakening inter-strand electrostatic repulsion. Unexpectedly, our force-induced hairpin unzipping experiments and thermal melting experiments show that LiCl, NaCl, KCl, RbCl, and CsCl at concentrations beyond ~1 M destabilize DNA, RNA, and RNA-DNA duplexes. The two types of experiments yield different changes in free energy during melting, while the results that high concentration monovalent salts destabilize duplexes are common.
View Article and Find Full Text PDFEnhancement of soy protein functionality by conjugation or complexation with polysaccharides or polyphenols: A review.
Compr Rev Food Sci Food Saf
January 2025
State Key Laboratory of Food Science and Resources, Jiangnan University, School of Food Science and Technology, Collaborative innovation center of food safety and quality control in Jiangsu Province, Jiangnan University, Wuxi, China.
Soy proteins have good nutritional quality and exhibit a range of useful functional attributes, making them a viable option for replacing animal proteins in the development of more sustainable and eco-friendly plant-based food products. Nevertheless, soy proteins are prone to denaturation and/or aggregation under conditions they encounter in some food and beverage products (including certain pH, ionic, and thermal conditions), which adversely impact their functional performance. This problem can often be overcome by covalently (conjugation) or noncovalently (complexation) linking the soy proteins to polysaccharides or polyphenols, thereby expanding their application scope.
View Article and Find Full Text PDFDeciphering Saquinavir-Bovine Serum Albumin Interactions: Spectroscopic and Computational Insights.
J Mol Recognit
January 2025
Biopolymer Modeling and Protein Chemistry Laboratory, Centre for Advanced Studies in Crystallography and Biophysics, University of Madras, Chennai, India.
Bovine serum albumin (BSA) plays a crucial role as a carrier protein in plasma, binding various ligands, including drugs. Understanding the interaction between BSA and saquinavir, an antiretroviral drug, is essential for predicting its pharmacokinetics and pharmacodynamics. We employed spectroscopic approaches, including circular dichroism spectrometry and fluorescence spectroscopy, to investigate the binding of saquinavir to BSA.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!