The development of three-dimensional (3D) printed meat analogs with fiber, texture, and sensory resembling meat remains challenging. This study investigated the effect of l-cysteine on functionality enhancement and fibrous structure formation in mixtures of mung bean protein isolate (MBPI) and wheat gluten (WG) for meat analog production. 3D printing was used to construct fibrous filaments. Raw MBPI-WG mixtures decreased rheological properties when increasing l-cysteine contents (0.0%-0.6%), promoting ink extrudability. The cys-0.4% ink exhibited the highest printing resolution and structural stability, correlated with its higher mechanical strength and increased disulfide cross-links. After cooking, the cys-0.4% sample showed a pronounced fibrousness in agreement with its microstructure image. This meat analog displayed a muscle-meat-like structure, improved texture, and reduced beany odor and bitter taste. Excessive cysteine contents (0.5%-0.6%) negatively affected the functionality of meat analogs. This study provides guidance for optimizing the amount of l-cysteine in meat analogs to improve product quality.

Effect of l-cysteine on functional properties and fibrous structure formation of 3D-printed meat analogs from plant-based proteins

Different Bacillus thuringiensis (Bt) strains produce a broad variety of pore-forming toxins (PFTs) that show toxicity against insects and other invertebrates. Some of these insecticidal PFT proteins have been used successfully worldwide to control diverse insect crop pests. There are several studies focused on describing the mechanism of action of these toxins that have helped to improve their performance and to cope with the resistance evolved by different insects against some of these proteins. However, crucial information that is still missing is the structure of pores formed by some of these PFTs, such as the three-domain crystal (Cry) proteins, which are the most commercially used Bt toxins in the biological control of insect pests. In recent years, progress has been made on the identification of the structural changes that certain Bt insecticidal PFT proteins undergo upon membrane insertion. In this review, we describe the models that have been proposed for the membrane insertion of Cry toxins. We also review the recently published structures of the vegetative insecticidal proteins (Vips; e.g. Vip3) and the insecticidal toxin complex (Tc) in the membrane-inserted state. Although different Bt PFTs show different primary sequences, there are some similarities in the three-dimensional structures of Vips and Cry proteins. In addition, all PFTs described here must undergo major structural rearrangements to pass from a soluble form to a membrane-inserted state. It is proposed that, despite their structural differences, all PFTs undergo major structural rearrangements producing an extended α-helix, which plays a fundamental role in perforating their target membrane, resulting in the formation of the membrane pore required for their insecticidal activity.

/pdf/structural-changes-upon-membrane-insertion-of-the-1dr5m8jg.pdf

Structural changes upon membrane insertion of the insecticidal pore-forming toxins produced by Bacillus thuringiensis

The dynamic changes in fluorescence intensity of the Maillard reactions of l-alanyl-l-glutamine (Ala-Gln)/Diglycine (Gly-Gly)/glycyl-l-glutamine (Gly-Gln) and glucose were investigated. It was found that the fluorescence intensity would increase with the reaction time; however, it would decrease after longer heating at higher temperatures, which was accompanied by rapid browning. The strongest intensity occurred at 45, 35, and 35 min at 130 °C for Ala-Gln, Gly-Gly, and Gly-Gln systems, respectively. The simple model reactions of Ala-Gln/Gly-Gly and dicarbonyl compounds were selected to reveal the formation and mechanism of fluorescent Maillard compounds. It was confirmed that both GO and MGO could react with peptides to form fluorescent compounds, especially GO, and this reaction was sensitive to temperature. The mechanism was also verified in the complex Maillard reaction of pea protein enzymatic hydrolysates.

Formation of Fluorescent Maillard Reaction Intermediates of Peptide and Glucose during Thermal Reaction and Its Mechanism.

Preservatives are added as antimicrobial agents to extend the shelf life of meat. Adding preservatives to meat products can affect their flavor and nutrition. This review clarifies the effects of preservatives on metabolic pathways and network molecular transformations in meat products based on lipidomics, metabolomics and proteomics analyses. Preservatives change the nutrient content of meat products via altering ionic strength and pH to influence enzyme activity. Ionic strength in salt triggers muscle triglyceride hydrolysis by causing phosphorylation and lipid droplet splitting in adipose tissue hormone-sensitive lipase and triglyceride lipase. DisoLipPred exploiting deep recurrent networks and transfer learning can predict the lipid binding trend of each amino acid in the disordered region of input protein sequences, which could provide omics analyses of biomarkers metabolic pathways in meat products. While conventional meat quality assessment tools are unable to elucidate the intrinsic mechanisms and pathways of variables in the influences of preservatives on the quality of meat products, the promising application of omics techniques in food analysis and discovery through multimodal learning prediction algorithms of neural networks (e.g., deep neural network, convolutional neural network, artificial neural network) will drive the meat industry to develop new strategies for food spoilage prevention and control.

Integrative deep learning framework predicts lipidomics-based investigation of preservatives on meat nutritional biomarkers and metabolic pathways.

This study investigates the potential use of peanut oil bodies as a fat replacer in ice cream. We explored the effects of different treatments, fresh (FOB), heated (HOB), and roasted (ROB) peanut oil bodies on ice cream preparation. Heat treatment altered the intrinsic protein profile on the oil bodies' surface, subsequently influencing the ice cream's properties. Notably, heat treatment increases the oil bodies' size and the absolute value of ζ-potential. The rheological analysis provided information about void volumes, indicating easier air incorporation during whipping for ROB (72 to 300 nm) than FOB (107 to 55 nm). ROB ice cream displays a high overrun and a lower melting rate compared to FOB ice cream. Moreover, thermal treatment reduces the beany flavors, n-hexanal, and 2-pentenylfuran. Overall, this study reveals peanut oil bodies as a promising platform for rational design of fat-substituted plant-based ice creams. 

Thermally treated peanut oil bodies as a fat replacer for ice cream: Physicochemical and rheological properties.

The potential application of vegetable oils in the D-xylose and L-cysteine Maillard reaction system for meaty aroma production.

Vip3Aa from Bacillus thuringiensis subsp. kurstaki HD1 is toxic to Aedes aegypti (Diptera: Culicidae).

Genome of Bacillus sp. strain QHF158 provides insights into its parasporal inclusions encoded by the S-layer gene

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The potential application of vegetable oils in the D-xylose and L-cysteine Maillard reaction system for meaty aroma production.

Vip3Aa from Bacillus thuringiensis subsp. kurstaki HD1 is toxic to Aedes aegypti (Diptera: Culicidae).

Genome of Bacillus sp. strain QHF158 provides insights into its parasporal inclusions encoded by the S-layer gene