Alterations In Secondary Structure Research Articles

Effect of α-tocopherol, soybean oil, and glyceryl monostearate oleogel on gel properties and the in-vitro digestion of low-salt silver carp (Hypophthalmichthys molitrix) surimi

To improve nutritional health, a low-salt (0.5 %) silver carp (Hypophthalmichthys molitrix) surimi gel with α-tocopherol, soybean oil, and glyceryl monostearate oleogel was fabricated and evaluated for textural qualities, lipid oxidation, and in-vitro digestion analysis. Based on the texture profile analysis, gel strength, water holding capacity (WHC), rheological, protein secondary structure, and microstructural examination, 5 % oleogel addition to low-salt surimi exhibited similar physicochemical properties to regular-salt surimi gels. By crosslinking myosin and filling protein network voids, the oleogel increased surimi gel density. Increasing oleogel content improved the physicochemical qualities of heat-induced surimi, causing protein aggregation during digestion and reducing digestibility. The presence of oleogel altered protein secondary structure, reducing α-helix content and increasing β-sheet and other structures, enhancing WHC and gel strength of low salt surimi. Adding oleogel improved the antioxidant activity of digestive solutions. This study will help understand myosin-oleogel interaction and the development of sustainable and nutritious surimi-based foods.

Radio frequency drying on functional diversity of tiger nut flour: Effects on physicochemical, structural, and rheological properties

Tiger nut (TN) is a valuable nutrient and gluten-free tuber. To achieve high-quality TN flour as functional ingredients in food, it is essential to develop effective drying technologies for TN. Five drying methods including natural drying (Control), hot-air drying (HD), radio frequency single drying (RFSD), RF assisted hot-air drying (RFHD), and RF- vacuum drying (RFVD) were selected and compared to determine their effects on physiochemical, structural, and rheological properties of TN flour. Results showed that RF drying (RFD) significantly improved the hydration, oil-absorbing, and antioxidant activity capacity, especially for RFVD. RFHD exhibited greater color (BI = 13.80 ± 0.05 and C = 10.26 ± 0.05) and reducing sugar content (253.50 ± 2.27 mg d.b.) than RFSD and RFVD. The gelatinization temperature, enthalpy value, and particle size (57.30–269.33 μm) of TN flour were reduced. The structural property results indicated that RFD reduced the relative crystallinity and short-range ordering of the flour, altered protein secondary structure, and caused the damaged microstructure in comparison with Control and HD groups. All sample gels exhibited a weak strain overshoot behavior (type III) under large amplitude oscillations, and RFD resulted in a reduced viscoelastic behavior. RFD could be an effective method to produce functional TN flour.

Kappa-carrageenan and xylooligosaccharide effect on water mobility and structural changes in silver carp proteins during frozen storage.

The cryoprotective effect of xylooligosaccharide (XO) and kappa-carrageenan (KC) mixture on silver carp proteins in fluctuated frozen storage from 4 to -18 °C was analyzed. Positive control as a conventional cryoprotectant mixture of sucrose (4%) and sorbitol (4%), KC (3%) and XO/KC (3%) treatments were incorporated in silver carp surimi and myofibrillar proteins to analyze the water mobility and its influence on structural attributes. The temperature fluctuation significantly increased the structural alteration in samples with no treatments due to oxidative changes, protein denaturation and recrystallization. Meanwhile, the mixture of XO and KC (XO/KC 3%) significantly reduced the tertiary and secondary structural alterations by preventing the oxidative changes in α-helix and tryptophan (Trp) residues. Moreover, XO/KC (3%) inhibited water mobility, hindering the T22 relaxation time, as compared to the samples added with KC (3%) and the positive control. Interestingly, the XO/KC (3%) mixture significantly reduced the formation of extracellular spaces and recrystallization by restricting the partial dehydration of muscles and extracellular solution concentration. From the current results, it can be concluded that the XO/KC mixture could be efficient in protecting aquatic food proteins during fluctuating frozen storage by preventing the exposure of Trp residues and α-helix contents. Moreover, XO/KC restricted the water mobility by establishing a bond and making water unavailable for crystallization and recrystallization. Therefore, XO/KC could be used as an effective mixture to prevent fluctuated and frozen storage changes in aquatic foods. © 2024 Society of Chemical Industry.

Insights into the Binding Interactions between Microplastics and Human α-Synuclein Protein by Multispectroscopic Investigations and Amyloidogenic Oligomer Formation.

Aggregation of human α-synuclein protein is regarded to be a key stage in the etiology of Parkinson's disease and numerous other neurodegenerative illnesses. Microplastics pollution can be a potential agent to promote various neurodegenerative disorders. In this study, we have employed various multispectroscopic analytical methods to investigate the binding interactions between polyethylene (PE-MPs), polyvinyl chloride (PVC-MPs), polystyrene (PS-MPs) microplastics, and human α-synuclein protein. Spectroscopic investigations using UV-vis absorption, circular dichroism, and Fourier transform infrared have indicated different alterations in α-synuclein protein's secondary structures induced by the formation of the α-synuclein protein-MP binding complex. This study suggests that PS-MPs are found to be the most effective microplastic that promote amyloidogenic oligomer emergence because of their tiny size (100 nm).

Investigating the impact of common migration substances found in milk packaging on proteases: A multispectral and molecular docking approach

The effects of common migration substances in milk packaging on digestive protease were studied. We choose the common migrants found in eight types of multi-layer composite milk packaging. Enzyme activity experiments revealed that pepsin activity decreased by approximately 18 % at 500 μg/mL of stearic acid and stearamide treatment, while trypsin activity decreased by approximately 18 % only by stearic acid treatment (500 μg/mL). Subsequently, fluorescence spectroscopy, circular dichroism spectroscopy, and molecular docking technology were employed to investigate the inhibition mechanism of protease activity by migrating substances in three systems: stearic acid-trypsin, stearic acid-pepsin, and stearamide-pepsin. Results showed that the inhibitory effect of stearic acid on trypsin is a reversible mixed inhibition, whereas the inhibitory effects of stearic acid and stearamide on pepsin are non-competitive. In all three systems, ΔH < 0, ΔS < 0, and ΔG < 0, indicating the binding process between the migrant and the protease is a spontaneous exothermic process primarily driven by hydrogen bonding and van der Waals forces. In addition, their binding constants are all around 104 L/moL, indicating that there are moderate binding affinities exist between migrants and proteases. The binding process results in the quenching of the protease's endogenous fluorescence and induces alterations in the enzyme's secondary structure. Synchronized fluorescence spectroscopy showed that stearic acid enhanced the hydrophobicity near the Tyr residue of trypsin. The molecular docking results indicated that the binding affinity of stearic acid-trypsin, stearic acid-pepsin, and stearamide-pepsin was –22.51 kJ/mol, −12.35 kJ/mol, −19.28 kJ/mol respectively, which consistent with the trend in the enzyme activity results. This study can provide references for the selection of milk packaging materials and the use of processing additives, ensuring food health and safety.

Biomimetic protein structural transitions regulate activation and inhibition of the broad-spectrum bactericidal activity of cationic nanoparticles

The development of cationic polymers as alternative materials to antibiotics necessitates addressing the challenge of balancing their antimicrobial activity and toxicity. Here we propose a precise switching strategy inspired by biomimetic voltage-gated ion channels, enabling controlled activation and inhibition of cationic antimicrobial functions through protein conformational transitions in diverse physiological environments. Following thermodynamic studies on the specific recognition between mannose end groups on polycations and concanavalin A (ConA), we synthesized a type of ConA-polycation nanoparticle. The nanoparticle was inhibited under neutral conditions, with cationic moieties shielded by ConA's β-sheet. This shielding suppresses their antimicrobial activity, thereby ensuring satisfactory biocompatibility. In mildly acidic environments, however, the transition of a portion of ConA to an α-helix conformation exposed cations at the particle periphery, activating antibacterial functionality. Compared to inhibited nanoparticles, those in the activated state exhibited a 32–256 times reduction in the minimum bactericidal concentration against bacteria and fungi (2–16 µg/mL). In a murine acute pulmonary infection model, intravenous administration of inhibited nanoparticles effectively reduced bacterial counts by 4-log within 12 h. The biomimetic design, regulating cationic antimicrobial functionality through the alteration in protein secondary structure, significantly retards bacterial resistance development, holding great promise for intelligent antimicrobial materials. Statement of significanceCationic antimicrobial polymers exhibit advantages distinct from antibiotics due to their lower propensity for resistance development. However, the presence of cationic moieties also poses a threat to healthy cells and tissues, significantly constraining their potential for clinical applications. To address this challenge, we propose a biomimetic strategy that mimics voltage-gated ion channels to activate the antimicrobial functionality of cations selectively in bacterial environments through the conformational transitions of proteins between β–sheets and α–helices. In healthy tissues, the antimicrobial functionality is inhibited, ensuring satisfactory biocompatibility. Antimicrobial cationic materials capable of intelligent switching between an activated state and an inhibited state in response to environmental changes offer an effective strategy to prevent the development of resistance and mitigate potential side effects.

Revealing the Improved Binding Interaction of Plant Alkaloid Harmaline with Human Hemoglobin in Molecular Crowding Condition.

Harmaline and harmine are two structurally similar β-carboline alkaloids with several therapeutic activities, such as anti-inflammatory, antioxidant, neuroprotective, nephroprotective, antidiabetic, and antitumor activities. It has been previously reported that the interaction between harmaline and hemoglobin (Hb) is weak in buffer media compared to harmine. Crowding agents induce a molecular crowding environment in the ex vivo condition, which is almost similar to the intracellular environment. In this present study, we have investigated the nature of the interactions of harmaline and harmine with Hb by increasing the percentage of the crowding agent in buffer solution. The results of the UV-vis and fluorescence spectroscopy analysis have showed that with an increasing proportion of crowding agents, the interaction between harmaline and Hb is steadily improving in comparison to harmine. It has been found that the binding constant of Hb-harmaline reaches 6.82 × 105 M-1 in the 40% polyethylene glycol 200-mediated crowding condition, indicating high affinity compared to very low interaction in buffer media. Steady-state fluorescence anisotropy along with fluorescence lifetime measurements further revealed that the rotational movement of harmaline is maximally restricted by Hb in high crowding environments. Stoichiometry results represent that Hb and harmaline interacts in a 1:1 ratio in different percentages of the crowding agent. The circular dichroism spectroscopic results predict stronger interaction of harmaline with Hb (secondary structure alterations) in a higher crowding environment. From the melting study, it was found that the reactions between Hb and harmaline in crowding environments are endothermic (ΔH > 0) and disordering (ΔS > 0) in nature, indicating that hydrogen bonding and van der Waals interactions are the main interacting forces between Hb and harmaline. Harmaline molecules are more reactive in molecular crowding conditions than in normal buffer condition. This study represents that the interaction between harmaline and Hb is stronger compared to the structurally similar harmine in a molecular crowding environment, which may enlighten the drug discovery process in cell-mimicking conditions.

The effect of chrysin binding on the conformational dynamics and unfolding pathway of human serum albumin

Studies on the interactions between ligands and proteins provide insights into how a possible medication alters the structures and activities of the target or carrier proteins. The natural flavonoid aglycone Chrysin (CHR) has demonstrated anti-inflammatory, antioxidant, antiapoptotic, neuroprotective, and antineoplastic effects, both in vitro and in vivo. In this work, we investigated the impact of CHR binding on the as-yet-unexplored conformation, dynamics, and unfolding mechanism of human serum albumin (HSA). We determined CHR binding to HSA domain-II with the association constant (Ka) of 2.70 ± 0.21 × 105 M−1. The urea-induced sequential unfolding mechanism of HSA was used to elucidate the debatable binding location of CHR. CHR binding induced both secondary and tertiary structural alterations in the protein as studied by far-UV circular dichroism and intrinsic fluorescence spectroscopy. Red edge excitation shift (REES) indicated a decrease in conformational dynamics of the protein on the complex formation. This suggested an ordered compact and spatial arrangement of the CHR-boundmolecule. The binding of CHR was found to significantly modulate the urea-induced unfolding pathway of HSA. Urea-induced unfolding pathway of HSA became a two-state process (N-U) from a three-state process (N-I-U). The interaction of CHR is found to increase the thermal stability of the protein by ∼4 °C. This study focuses on the fundamental sciences and demonstrates how prospective medication compounds can alter the dynamics and stability of protein structure.

Mechanisms of inhibition of advanced glycation end-products (AGEs) and α-glucosidase by Heliotropium bacciferum: Spectroscopic and molecular docking analysis

Diabetes mellitus is characterized by hyperglycemia that makes insulin more prone to glycation and form advanced glycation end products (AGEs). Here, we report the effect of glyoxal (GO) on the formation of AGEs using human insulin as model protein and their structural modifications. The present investigation also reports the anti-AGE potential of Heliotropium bacciferum (Leaf) extracts. The phytochemical analysis of H. bacciferum revealed that free phenolic extract contains higher amount of total phenolic (3901.58 ± 17.06 mg GAE/100 g) and total flavonoid content (30.41 ± 0.32 mg QE/100 g) when compared to bound phenolic extract. Naringin and caffeic acid were identified as the major phenolic ingredients by UPLC-PAD method. Furthermore, bound phenolics extract showed significantly higher DPPH and superoxide radicals scavenging activity (IC50 17.53 ± 0.36 μg/mL and 0.306 ± 0.038 mg/ mL, respectively) (p ≤ 0.05). Besides, the bound phenolics extract also showed significant (p ≤ 0.05) chelating power (IC50 0.063) compared to free phenolic extract. In addition, bound phenolic extract could efficiently trap GO under physiological conditions. Spectroscopic investigation of GO-modified insulin illustrated changes in the tertiary structure of insulin and formation of AGEs. On the other hand, no significant alteration in secondary structure was observed by far UV-CD measurement. Furthermore, H. bacciferum extract inhibited α-glucosidase activity and AGEs formation implicated in diabetes. Molecular docking analysis depicted that GO bind with human insulin in both chains and forms a stable complex with TYR A: 14, LEU A:13, ASN B:3, SER A:12 amino acid residues with binding energy of – 2.53 kcal/mol. However, caffeic acid binds to ASN A:18 and GLU A:17 residues of insulin with lower binding energy of −4.67 kcal/mol, suggesting its higher affinity towards human insulin compared to GO. Our finding showed promising activity of H. bacciferum against AGEs and its complications. The major phenolics like caffeic acid, naringin and their derivatives could be exploited for the drug development for management of AGEs in diabetes.

Unraveling the binding mechanism between soybean protein isolate and selected bioactive compounds

The present study was aimed to investigate the interactions between soybean protein isolate (SPI) with resveratrol (RESV) and lutein (LUT). The binding forces, molecular interactions and functional properties were explored by multi-spectroscopic analysis, molecular docking and functional property indexes between SPI and RESV/LUT. The RESV/LUT quenched SPI chromophore residues with static mechanism and the endothermic reaction. The SPI- RESV/LUT complexes were formed through hydrogen bond, electrostatic and hydrophobic interactions. Molecular docking confirmed van-der-Waals force as one of the important forces. The interaction of RESV/LUT led to SPI's secondary structure alterations with a decrease in α-helix and random coil and an increase in β-sheet and β-turns. RESV/LUT developed foaming and emulsifying properties of SPI and showed a significant decrease of the surface hydrophobicity with RESV/LUT concentrations increase attributed to SPI's partial unfolding. Our study exposed molecular mechanisms and confirmations to understand the interactions in protein- RESV/LUT complexes for protein industrial base promotion.

The Effect of Microwaves on Protein Structure: Molecular Dynamics Approach.

The impact of microwave (MW) irradiation on protein folding, potentially inciting misfolding, was investigated by employing molecular dynamics (MD) simulations. Twenty-nine proteins were subjected to MD simulations under equilibrium (300 K) and MW conditions, where the rotational temperature was elevated to 700 K. The utilized replacement model captures the microwave effects of δ- and γ-relaxation processes (frequency range of ∼300 MHz to ∼20 GHz). The results disclosed that MW heating incited a shift toward more compact protein conformations, as indicated by decreased root-mean-square deviations, root-mean-square fluctuations, head-to-tail distances, and radii of gyration. This compaction was attributed to the intensification of intramolecular electrostatic interactions and hydrogen bonds within the protein caused by MW-destabilized hydrogen bonds between the protein and solvent. The solvent-accessible surface area (SASA), particularly that of polar amino-acid residues, shrank under MW conditions, corresponding to a reduced polarity of the water solvent. However, MW irradiation produced no significant alterations in protein secondary structures; hence, MW heating was observed to primarily affect the protein tertiary structures.

Effect of benzoic acid-based and cinnamic acid-based polyphenols on foaming properties of ovalbumin at acidic, neutral and alkaline pH conditions

To broaden the application of ovalbumin (OVA) in food formulations, it is meaningful to improve its foaming characteristics. This study aimed to investigate the effect of benzoic acid-based (3,4-dihydroxybenzoic acid, DA) and cinnamic acid-based polyphenols (trans-2-hydroxycinnamic acid, T2A) on the foaming properties of OVA at acidic (pH 3.0), neutral (pH 7.4) and alkaline (pH 9.0) pH conditions. Both the addition of polyphenols and acid treatment enhanced the foaming properties of OVA. Surface hydrophobicity, circular dichroism, free sulfhydryl groups, and Fourier transform infrared spectroscopy results indicated that after acidic workup, the presence of stronger hydrophobic interactions in OVA-polyphenol aggregates induced more disordered protein conformation and conversion or breakage of disulfide bonds. Particle size and zeta potential indicated that acidic treatment neutralized protein surface charges, further inducing self-aggregation and swelling of OVA, ultimately enhancing foaming properties. Comparatively, T2A exhibited better foam-inducing capacity due to its stronger interaction with OVA, leading to the unfolding of the OVA structure and the exposure of more hydrophobic groups. The intrinsic and 3-D fluorescence spectra experiments also confirmed that OVA-T2A aggregates at pH 3.0 had greater altered non-covalent interaction forces and protein secondary and tertiary structures compared to other complexes. This study provides a theoretical basis for designing protein formulations with excellent foaming properties.

Inhibitory mechanism of arabinoxylan and β-glucan from hull-less barley on α-amylase activity: A comparison study

The inhibitory mechanisms of arabinoxylan (HBAX) and β-glucan (HBBG) from hull-less barley against pancreatic α-amylase were investigated using enzymatic inhibitory kinetics, multi-spectroscopy and thermodynamic analysis. Results indicated that both HBAX and HBBG effectively inhibited α-amylase activity, with HBAX exhibiting superior potency (IC50 of 3.26 mg/mL) compared to HBBG (IC50 of 13.23 mg/mL). Kinetic analysis revealed that HBAX displayed competitive and noncompetitive mixed inhibition, while HBBG predominantly exhibited noncompetitive inhibition. Interaction studies demonstrated that both HBAX and HBBG could spontaneously interact with α-amylase through hydrogen bonding and van der Waals forces, leading to structural adjustments of α-amylase, albeit without notable secondary structure alterations. However, HBAX showed stronger fluorescence quenching ability and microenvironmental modifications of α-amylase compared to HBBG. Bio-layer interferometry confirmed the stronger binding ability of HBAX to α-amylase, characterized by higher association binding constant (Ka) and lower dissociation constant (Kd) and affinity constant (KD). The lower equilibrium dissociation constant (K) and greater enthalpy change (ΔH) of HBAX to α-amylase further proved its stronger interaction with α-amylase. These differences were ascribed that HBAX inhibited α-amylase activity potentially through starch competition or physical interference, while HBBG might primarily act as physical barriers. This study enhances understanding of HBAX and HBBG in lowering starch digestion from an enzyme-inhibitory perspective.

Identification of a Novel Peptide with Alcohol Dehydrogenase Activating Ability from Ethanol-Induced Lactococcus lactis: A Combined In Silico Prediction and In Vivo Validation.

Alcohol dehydrogenase (ADH) is a crucial rate-limiting enzyme in alcohol metabolism. Our previous research found that ethanol-induced intracellular extracts of Lactococcus lactis (L. lactis) could enhance alcohol metabolism in mice, but the responsible compounds remain unidentified. The study aimed to screen potential ADH-activating peptides from ethanol-induced L. lactis using virtual screening and molecular docking calculation. Among them, the pentapeptide FAPEG might bind to ADH through hydrophobic interaction and hydrogen bonds, then enhancing ADH activity. Spectroscopy analysis further investigated the peptide-enzyme interaction between FAPEG and ADH, including changes in the amino acid residue microenvironment and secondary structural alterations. Furthermore, FAPEG could protect against alcoholic liver injury (ALI) in mice by reducing blood alcohol concentration, enhancing the activity of antioxidant and alcohol metabolism enzymes, and attenuating alcohol-induced hepatotoxicity, which was related to the activation of the Nrf2/keap1/HO-1 signaling pathway. The study provided preliminary evidence that the generation of ADH-activating peptides in ethanol-induced L. lactis has the potential in preventing ALI in mice using in silico prediction and in vivo validation approaches.

Thermodynamic and functional changes of alpha-chymotrypsin after interaction with gallic acid

In the present study, the interaction mechanism between gallic acid (GA) and α-Chymotrypsin (α-CT) was investigated by employing a series ofspectroscopic methods, computational docking and molecular dynamic (MD) simulation. Fluorescence spectra analysis indicated the formation of a stable complex between GA and α-CT, where the quenching of the fluorescence emission was predominantly characterized by a static mechanism. TheCA obtained binding constants for the α-CT-GA complex were in the order of 103 M−1, indicating the moderate binding affinity of GA for α-CT. The corresponding CD findings showed that the interaction between GA and α-CT resulted in an alteration of the protein's secondary structure. The findings of the enzyme activity investigation clearly showed that the presence of GA led to a notable decline in the enzymatic activity of α-CT, highlighting GA's function as an effective inhibitor for α-CT. The molecular docking simulations revealed the optimal binding site for the GA molecule within the α-CT structure and MD simulations confirmed the stability of the α-CT-GA complex. This research expands our comprehension regarding the behavior of enzymes in the presence of small-molecule ligands and opens avenues for food safety.

Methotrexate for Drug Repurposing as an Anti-Aggregatory Agent to Mercuric Treated α-Chymotrypsinogen-A.

Protein aggregation is related to numerous pathological conditions like Alzheimer's and Parkinson's disease. In our study, we have shown that an already existing FDA-approved drug; methotrexate (MTX) can be reprofiled on preformed α-chymotrypsinogen A (α-Cgn A) aggregates. The zymogen showed formation of aggregates upon interaction with mercuric ions, with increasing concentration of Hg2Cl2 (0-150 µM). The hike in ThT and ANS fluorescence concomitant with blue shift, bathochromic shift and the hyperchromic effect in the CR absorbance, RLS and turbidity measurements, substantiate the zymogen β-rich aggregate formation. The secondary structural alterations of α- Cgn A as analyzed by CD measurements, FTIR and Raman spectra showed the transformation of native β-barrel conformation to β-inter-molecular rich aggregates. The native α- Cgn A have about 30% α-helical content which was found to be about 3% in presence of mercuric ions suggesting the formation of aggregates. The amorphous aggregates were visualized by SEM. On incubation of Hg2Cl2 treated α- Cgn A with increasing concentration of the MTX resulted in reversing aggregates to the native-like structure. These results were supported by remarkable decrease in ThT and ANS fluorescence intensities and CR absorbance and also consistent with CD, FTIR, and Raman spectroscopy data. MTX was found to increase the α-helical content of the zymogen from 3 to 15% proposing that drug is efficient in disrupting the β-inter-molecular rich aggregates and reverting it to native like structure. The SEM images are in accordance with CD data showing the disintegration of aggregates. The most effective concentration of the drug was found to be 120 µM. Molecular docking analysis showed that MTX molecule was surrounded by the hydrophobic residues including Phe39, His40, Arg145, Tyr146, Thr151, Gly193, Ser195, and Gly216 and conventional hydrogen bonds, including Gln73 (bond length: 2.67Å), Gly142 (2.59Å), Thr144 (2.81Å), Asn150 (2.73Å), Asp153 (2.71Å), and Cys191 (2.53Å). This investigation will help to find the use of already existing drugs to cure protein misfolding-related abnormalities.

Advances in Nanoparticle-Enhanced Thermoelectric Materials from Synthesis to Energy Harvesting: A Review.

This comprehensive review analysis examines the domain of composite thermoelectric materials that integrate nanoparticles, providing a critical assessment of their methods for improving thermoelectric properties and the procedures used for their fabrication. This study examines several approaches to enhance power factor and lattice thermal conductivity, emphasizing the influence of secondary phases and structural alterations. This study investigates the impact of synthesis methods on the electrical characteristics of materials, with a particular focus on novel techniques such as electrodeposition onto carbon nanotubes. The acquired insights provide useful guidance for the creation of new thermoelectric materials. The review also compares and contrasts organic and inorganic thermoelectric materials, with a particular focus on the potential of inorganic materials in the context of waste heat recovery and power production within industries. This analysis highlights the role of inorganic materials in improving energy efficiency and promoting environmental sustainability.

Effect of carbonyl-amino condensation, non-covalent cross-linking and conformational changes induced by ultrasound-assisted Maillard reaction on lysinoalanine formation in silkworm pupa protein

The inhibition of cross-linked lysinoalanine (LAL) formation in silkworm pupa protein isolates (SPPI) by Maillard reaction (using varying xylose concentration) and ultrasound treatment was studied. Results showed that sonicated SPPI was effectively grafted with high concentration of xylose (5 %), resulting in the lowest LAL content, which was 48.75 % and 30.64 % lower than the control and ultrasound-treated samples, respectively. Chemical bond analysis showed that the combined treatment destroyed the ionic bonds, intrachain (g-g-t), and interchain (g-g-g) disulfide bonds, but stimulated the polymerization of hydrogen and hydrophobic bonds between SPPI and xylose, and as well enhanced the net negative charge between SPPI/Xylose complexes. The particles of the complexes were more loose, dispersed and rough, and had a stronger hydrophilic microenvironment, accompanied by alterations in microscopic, secondary and tertiary structures. Ultrasound treatment induced the breakdown of the oxidative cross-linking in SPPI, and promoted the sulfhydryl group-dehydroalanine binding and the carbonyl-amino condensation of the protein and xylose, and thus inhibited the formation of cross-linked LAL. Furthermore, the physicochemical and structural parameters were highly interrelated with cross-linked LAL content (|r| > 0.9). The outcomes provided a novel avenue and theoretical basis for minimizing LAL formation in SPPI and improving the nutrition and safety of SPPI.

Tracking protein aggregation behaviour and emulsifying properties induced by structural alterations in common carp (Cyprinus carpio) myofibrillar protein during long-term frozen storage

The effect of ultrasound-assisted immersion freezing (UIF), air freezing (AF), and immersion freezing (IF) on the protein structure, aggregation, and emulsifying properties of common carp (Cyprinus carpio) myofibrillar protein during frozen storage were evaluated in the present study. The result showed that, compared with AF and IF samples, UIF sample had higher reactive/total sulfhydryl, protein solubility, and lower protein turbidity (P < 0.05), indicating that UIF was beneficial to inhibit protein oxidation and aggregation induced by frozen storage. UIF inhibited the alteration of secondary structure and tertiary structure during frozen storage. Meanwhile, UIF sample had higher emulsifying activity index, and smaller emulsion droplet diameter than AF and IF samples (P < 0.05), suggesting that UIF was beneficial for maintaining the emulsifying properties of protein during storage. In general, UIF is a potential and effective method to suppress the decrease in protein emulsifying properties during long-term frozen storage.

Evaluation of structure, quality, physicochemical properties, and phenolics content of pea proteins: A novel strategy through the incorporation of fermentation.

The utilization of pea proteins (PPs) is limited due to their relatively low protein digestibility (∼81%) compared to animal-based proteins, such as whey. The present investigation involved the fermentation of PPs at a concentration of 1% (w/v) using 5% (w/v) water kefir for 60h at 25°C to improve the functional properties of PPs. The results showed a significant (p<0.05) increase in lactic acid and acetic acid production during fermentation. These findings suggest that PPs can be effectively fermented using water kefir as a starter culture for the increased protein digestibility of PPs. The PP conformation underwent modifications, including secondary and tertiary protein structure alterations. The total phenolic compounds increased throughout the fermentation, reaching around 695.32±15mg gallic acid equivalent/100g after 24h of fermentation. Furthermore, the fermentation process has culminated in significant (p<0.05) changes in the surface charge and hydrophobic properties of the fermented PPs, from -38.1 to -45.73 and 362.7 to 550.2, respectively. Fermentation using water kefir is a promising technique for improving the digestibility, protein structure, and nutritional values of PPs.