Potential use of yeast protein in terms of biorefinery, functionality, and sustainability in food industry.

A growing demand for sustainable, alternative protein sources that are nutrient-dense, such as microorganisms, and insects, has gradually evolved. When paired with effective processing techniques, yeast cells contain substantial substances that could supply the population's needs for food, medicine, and fuel. This review article explores the potential of yeast proteins as a sustainable and viable alternative to animal and plant-based protein sources. It highlights the various yeast protein extraction methods including both mechanical and non-mechanical methods. The application of nanoparticles is one example of the fast-evolving technology used to damage microbial cells. SiO2 or Al2O3 nanoparticles break yeast cell walls and disrupt membranes, releasing intracellular bioactive compounds. Succinylation of yeast protein during extraction can increase yeast protein extraction rate, lower RNA concentration, raise yeast protein solubility, increase amino acid content, and improve yeast protein emulsification and foaming capabilities. Combining physical and enzymatic extraction methods generates the most representative pool of mannose proteins from yeast cell walls. Ethanol or isoelectric precipitation purifies mannose proteins. Mannoproteins can be used as foamy replacement for animal-derived components like egg whites due to their emulsification, stability, and foaming capabilities. Yeast bioactive peptide was separated by ultrafiltration after enzymatic hydrolysis of yeast protein and has shown hypoglycemic, hypotensive, and oxidative action in vitro studies. Additionally, the review delves into the physicochemical properties and stability of yeast-derived peptides as well as their applications in the food industry. The article infers that yeast proteins are among the promising sources of sustainable protein, with a wide range of potential applications in the food industry.

Crustacean shellfish allergens: influence of food processing and their detection strategies.

Despite the increasing popularity of crustacean shellfish among consumers due to their rich nutrients, they can induce a serious allergic response, sometimes even life-threatening. In the past decades, a variety of crustacean allergens have been identified to facilitate the diagnosis and management of crustacean allergies. Although food processing techniques can ease the risk of crustacean shellfish allergy, no available processing methods to tackle crustacean allergies thoroughly. Strict dietary avoidance of crustacean shellfish and its component is the best option for the protection of sensitized individuals, which should rely on the compliance of food labeling and, as such, on their verification by sensitive, reliable, and accurate detection techniques. In this present review, the physiochemical properties, structure aspects, and immunological characteristics of the major crustacean allergens have been described and discussed. Subsequently, the current research progresses on how various processing techniques cause the alterations and modifications in crustacean allergens to produce hypoallergenic crustacean food products were summarized and discussed. Particularly, various analytical methodologies employed in crustacean shellfish allergen detection, and the effect of food processing and matrix on these techniques, are also herein emphasized for the appropriate selection of analytical detection tools to safeguard consumers safety.

Insight into the Characterization of Volatile Compounds in Smoke-Flavored Sea Bass (Lateolabrax maculatus) during Processing via HS-SPME-GC-MS and HS-GC-IMS.

The present study aimed to ascertain how the volatile compounds changed throughout various processing steps when producing a smoke-flavored sea bass (Lateolabrax maculatus). The volatile compounds in different production steps were characterized by headspace-solid phase microextraction-gas chromatography-mass spectrometry (HS-SPME-GC-MS) and headspace-gas chromatography-ion mobility spectrometry (HS-GC-IMS). A total of 85 compounds were identified, and 25 compounds that may be considered as potential key compounds were screened by principal component analysis (PCA) and partial least squares discriminant analysis (PLS-DA). Results indicated that aldehydes were the major volatile compounds throughout the processing. The characteristic volatile compound in fresh samples was hexanol, and curing was an effective method to remove the fishy flavor. The concentration of volatile compounds was significantly higher in dried, smoked, and heated samples than in fresh and salted samples. Aldehydes accumulated because of the drying process, especially heptanal and hexanal. Smoke flavoring was an important stage in imparting smoked flavor, where phenols, furans and ketones were enriched, and heating leads to the breakdown of aldehydes and alcohols. This study will provide a theoretical basis for improving the quality of smoke-flavored sea bass products in the future.

A systematic review on the recent advances of wheat allergen detection by mass spectrometry: future prospects.

Wheat is one of the three major staple foods in the world. Although wheat is highly nutritional, it has a variety of allergenic components that are potentially fatal to humans and pose a significant hazard to the growth and consumption of wheat. Wheat allergy is a serious health problem, which is becoming more and more prevalent all over the world. To address and prevent related health risks, it is crucial to establish precise and sensitive detection and analytical methods as well as an understanding of the structure and sensitization mechanism of wheat allergens. Among various analytical tools, mass spectrometry (MS) is known to have high specificity and sensitivity. It is a promising non immune method to evaluate and quantify wheat allergens. In this article, the current research on the detection of wheat allergens based on mass spectrometry is reviewed. This review provides guidance for the further research on wheat allergen detection using mass spectrometry, and speeds up the development of wheat allergen research in China.

Thermal induced the structural alterations, increased IgG/IgE binding capacity and reduced immunodetection recovery of tropomyosin from shrimp (Litopenaeus vannamei).

Shrimps were first subjected to various thermal processing, then tropomyosin (TM) was purified and their structure, IgG/IgE-binding ability and detectability were evaluated for elucidating the mechanisms responsible for thermal-induced TM immunodetection recovery alterations. According to CD and FT-IR analysis, heat-treated shrimp TM had significantly reduced α-helix and ß-sheet contents with elevated random coil contents, contributing to an increase of 24.42%-62.22% in IgG/IgE reactivity as compared with raw shrimp TM. The exposure of hydrophobic residues and glycosylation occurred in various heated shrimps TM were confirmed by UV, intrinsic/extrinsic fluorescence spectrum and free amino group analysis, which caused some epitopes masking or modification, thereby inducing considerable TM recovery reduction (48.48%-90.44%). These results demonstrated that thermal-treated TMs with higher structural flexibility facilitated IgG/IgE recognition, however the lower number of epitopes within the thermal-treated TMs might cause considerable underestimation of recovery. The number of antigen binding sites might play a critical role in sandwich immunodetection.

A sensitive sandwich enzyme-linked immunosorbent assay (sELISA) targeted multiple wheat protein fractions for the detection of several cereal grains in processed foods.

Wheat allergy has become a global public health and food safety concern; however, there is no accessible cure for wheat allergy. The complete exclusion of wheat-containing foods and environmental exposure is the most efficient allergy management to avoid the adverse reactions, which can be severe and occasionally life threatening. Therefore, the assay for accurate detection of wheat residues is demanded urgently for appropriate labeling guidelines and consumer safety. Thus, a sandwich enzyme-linked immunosorbent assay (sELISA) targeting multiple wheat protein fractions was fabricated in the present study. The results showed that the limit of detection (LOD) and limit of quantitation (LOQ) of the constructed sELISA were 0.25 and 0.5 µg/g with high specificity for wheat. No cross-reactivity was observed in 32 foods or food ingredients tested, except barley and rye. The developed sELISA can also discriminate against many commercial foods containing declared or undeclared wheat residues except for Chinese yellow wine. Furthermore, high heat also can obtain a higher level of proteins extracted with corresponding enhanced detectability up to 100°C from heated samples and 160 °C in baked samples. PRACTICAL APPLICATION: Wheat is the most common food ingredient and wildly applied in various processed foods. However, wheat can cause severe and life-threatening symptoms in some allergic patients and must be labeled and tested accurately to protect those with a wheat allergy. Developing a new test assay can serve as a powerful tool for food manufacturers and regulatory agencies to accurately quantify wheat residues in processed foods and ensure their absence due to unintended contamination.

Insight into IgG/IgE binding ability, in vitro digestibility and structural changes of shrimp (Litopenaeus vannamei) soluble extracts with thermal processing.

The effects of six kinds of thermal processing on soluble protein recovery, potential allergenicity, in vitro digestibility and structural characteristics of shrimp soluble proteins were evaluated. Obtained results confirmed soluble protein recovery and IgG/IgE reactivity of shrimp soluble extracts were markedly suppressed by various thermal treatments with enhanced digestibility depended on the extent and type of heating applied, which correlated well with the structural alterations and modification. The maximum reduction of IgG/IgE-binding capacity and digestive stability were observed in the autoclaved shrimps because of unfolding of protein and hydrophobic residues exposed. Notably, tropomyosin (TM) and sarcoplasmic calcium-binding protein (SCP) were still IgG/IgE-reactive in various heat-processed shrimps, even higher IgG reactivity were found in heat-treated shrimps TM according to TM antiserum western-blotting and indirect ELISA results. Shrimp TM and SCP maintains its IgE/IgG-binding capacity after various cooking methods, thus most probably initiating allergic sensitization to both raw and cooked shrimps.

A comprehensive review on the application of novel disruption techniques for proteins release from microalgae.

There is an emergent demand for sustainable and alternative protein sources such as insects and microorganisms that meet the nutritional requirements. Microalgae possess valuable substances that could satisfy the population's dietary requirement, medicinal purpose, and energy, aligned with effective processing techniques. Several disruption techniques were applied to microalgae species for protein recovery and other compounds. The thick microalgae cell wall makes it difficult to recover all the valuable biomolecules through several downstream processes. Thus, forethought key factors need to be considered when choosing a cell lysis method. The most challenging and crucial issue is selecting a technique that requires consideration of their ability to disrupt all cell types, easy to use, purity degree, reproducible, scalable, and energy efficient. This review aims to provide useful information specifically on mechanical and non-mechanical disruption methods, the status and potential in protein extraction capacities, and constraints. Therefore, further attention in the future on potential technologies, namely explosive decompression, microfluidization, pulsed arc technology, is required to supplement the discussed techniques. This article summarizes recent advances in cell disruption methods and demonstrates insights on new directions of the techniques and future developments.