Total Sulfhydryl Content Research Articles

Physiological tolerance of black locust (Robinia pseudoacacia L.) and changes of rhizospheric bacterial communities in response to Cd and Pb in the contaminated soil.

Woody plants possess great potential for phytoremediation of heavy metal-contaminated soil. A pot trial was conducted to study growth, physiological response, and Cd and Pb uptake and distribution in black locust (Robinia pseudoacacia L.), as well as the rhizosphere bacterial communities in Cd and Pb co-contaminated soil. The results showed that R. pseudoacacia L. had strong physiological regulation ability in response to Cd and Pb stress in contaminated soil. The total chlorophyll, malondialdehyde (MDA), soluble protein, and sulfhydryl contents, as well as antioxidant enzymes (superoxide dismutase, peroxidase, catalase) activities in R. pseudoacacia L. leaves under the 40mg·kg-1 Cd and 1000mg·kg-1 Pb co-contaminated soil were slightly altered. Cd uptake in R. pseudoacacia L. roots and stems increased, while the Pb content in the shoots of R. pseudoacacia L. under the combined Cd and Pb treatments decreased in relative to that in the single Pb treatments. The bacterial α-diversity indices (e.g., Sobs, Shannon, Simpson, Ace, and Chao) of R. pseudoacacia L. rhizosphere soil under Cd and Pb stress were changed slightly relative to the CK treatment. However, Cd and Pb stress could significantly (p < 0.05) alter the rhizosphere soil microbial communities. According to heat map and LEfSe(Linear discriminant analysis Effect Size) analysis, Bacillus, Sphingomonas, Terrabacter, Roseiflexaceae, Paenibacillus, and Myxococcaceae at the genus level were notably (p < 0.05) accumulated in the Cd- and/or Pb-contaminated soil. Furthermore, the MDA content was notably (p < 0.05) negatively correlated with the relative abundances of Isosphaeraceae, Gaiellales, and Gemmatimonas. The total biomass of R. pseudoacacia L. was positively (p < 0.05) correlated with the relative abundances of Xanthobacteraceae and Vicinamibacreraceae. Network analysis showed that Cd and Pb combined stress might enhance the modularization of bacterial networks in the R. pseudoacacia L. rhizosphere soil. Thus, the assembly of the soil bacterial communities in R. pseudoacacia L. rhizosphere may improve the tolerance of plants in response to Cd and/or Pb stress.

Effect of protein structure changes during different power ultrasound thawing on emulsification properties of common carp (Cyprinus carpio) myofibrillar protein

The impact of ultrasound thawing (UT) at different power (0 W, 100 W/0.132 W·cm−2, 300 W/1.077 W·cm−2, and 500 W/1.997 W·cm−2, namely WT, UT-100, UT-300, and UT-500) on protein structure, aggregation, and emulsifying properties of common carp (Cyprinus carpio) myofibrillar protein were investigated in the present study. The result showed that the reactive sulfhydryl content, total sulfhydryl content, protein solubility, and absolute potential of UT-300 samples were obviously higher than those of other thawed samples, while the turbidity of UT-300 samples was lower (P < 0.05), which indicated that proper UT power was beneficial to inhibit protein aggregation caused by thawing, while too low (100 W) or too high (500 W) ultrasonic power had poor effect. The Ca2+-ATPase activity and thermal stability of UT-300 samples were much higher than those of other thawed samples (P < 0.05), indicating that UT-300 inhibited myosin denaturation and thermal stability reduction of thawed products. The α-helix content of UT-300 samples was higher than that of other thawed samples, while the β-sheet content was significantly lower than that of other thawed samples (P < 0.05). The fluorescence intensity of UT-300 samples was higher than that of other thawed samples, and the λmax of UT-300 samples and UT-100 samples were lower than that of other thawed samples, which indicated that UT-300 could effectively inhibit the alteration of protein secondary structure and tertiary structure during thawing. The emulsifying activity of UT-300 samples was significantly higher than that of WT samples, and the droplet diameter of UT-300 samples was also lower than that of WT samples (P < 0.05), which indicated that UT-300 inhibited the decrease of emulsifying property during thawing. Overall, moderate ultrasonic power (300 W) could effectively inhibit the protein aggregation and structural changes during thawing, led to the decrease of emulsifying activity.

Effects of electron beam irradiation on protein oxidation and textural properties of shrimp (Litopenaeus vannamei) during refrigerated storage

Protein oxidation leads to changes in shrimp texture, which affects sensory profile and consumer acceptability. This study aimed to evaluate the impact of electron beam irradiation (EBI) on protein oxidation and textural properties of Litopenaeus vannamei during refrigerated storage. Results revealed that EBI treatment and storage increased the protein oxidation level of shrimps. Shrimps irradiated with ≥ 7 kGy exhibited remarkably higher (P < 0.05) reactive oxygen species, turbidity, and carbonyl contents, and remarkably lower (P < 0.05) Ca2+-ATPase activity, surface hydrophobicity, solubility, and total sulfhydryl contents compared to the control group (0 kGy) on the 7th day of storage. Shrimps irradiated with 3 and 5 kGy exhibited remarkably higher (P < 0.05) hardness, springiness, and chewiness compared to the control group (14.99 N, 1.26 mm, and 3.19 mJ). Collectively, suitable EBI doses of 3–5 kGy were recommended in shrimp preservation to inhibit texture softening by inducing moderate protein oxidation.

The impact of ice slurry as a medium on oxidation status and flesh quality of shrimp (Litopenaeus vannamei) during refrigeration storage.

Oxidation of lipid and protein is a major reason of flesh quality deterioration during storage. In this work, cold storage (CS) and flake ice (FI) storage, as traditional strategies for live shrimp (Litopenaeus vannamei) sedation and refrigerated storage, showed remarkable oxidation damage of lipid and protein in shrimp flesh during storage. In contrast, ice slurry (IS), with good heat exchange capacity and contactability, stunned shrimp in a sudden and thus relieved antemortem stress, which resulted in reducing the reactive oxygen species and reactive nitrogen species accumulation, and the oxidation damage risk in flesh. Additionally, IS, as a storage medium acted an oxygen barrier, further inhibited the oxidation of lipid and myofibrillar protein (MP), as revealed by the lower thiobarbituric acid reactive substances level, carbonyl (CO) derives content, total disulfide bond (S-S) content, and the higher total sulfhydryl (SH) content in shrimp flesh during storage, compared with CS and FI. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis electrophoretogram pattern of MP also suggested better preservation of myosin heavy chain, myosin light chain, actin, and tropomyosin in IS, whereas these proteins degraded in CS and FI. Consequently, IS prevented the formation of cross-linking caused by oxidation in MP, leading to improved shrimp flesh quality during refrigerated storage, as demonstrated by the better maintained hardness, springiness, and water-holding capacity compared to CS and FI.

Binding of Selected Aroma Compounds to Myofibrillar Protein, Sarcoplasmic Protein, and Collagen during Thermal Treatment: Role of Conformational Changes and Degradation of Proteins.

To investigate the effects of conformational changes and thermal degradation of myofibrillar protein (MP), sarcoplasmic protein (SP), and collagen (CO) on the binding ability for aroma compounds during heating. Using SDS-PAGE, HPLC, and LC-MS/MS, a consistent rise in the total concentration of peptides and free amino acids formed by the thermal degradation of proteins was observed. The surface hydrophobicity, total sulfhydryl content, particle size, and secondary structure content of proteins changed significantly over time. Furthermore, the aroma binding ability of proteins was determined by gas chromatography-mass spectrometry. The results revealed an increase in binding ability during 5 or 10 min of heating due to protein unfolding and the accumulation of degradation products. However, the binding ability decreased due to protein aggregation with prolonged heating. Notably, all proteins exhibited strong affinity toward (E)-2-octenal, (E,E)-2,4-decadienal, 2-methyl-3-furanthiol, and dimethyl trisulfide. The binding ability of MP and SP was similar but differed significantly from that of CO, which had lower binding ability for hexanal, (E)-2-octenal, (E,E)-2,4-decadienal, and dimethyl trisulfide compared to MP and SP.

Differentiation of protein types extracted from tilapia byproducts by FTIR spectroscopy combined with chemometric analysis and their antioxidant protein hydrolysates

This research aimed to characterize protein types including sarcoplasmic protein (SP), myofibrillar protein (MP), and alkali-aided protein extract (AP) prepared from tilapia byproducts using water, 0.6 M NaCl, and alkaline solution (pH 11), respectively compared to freeze-dried minced tilapia muscle (CONTROL). Principal component analysis was performed from second derivative FTIR spectra to differentiate protein type. The AP mostly contained β-sheet structure and had low total sulfhydryl content and surface hydrophobicity. SP can be distinguished from MP by the loading plots of the FTIR bands representing the α-helical structure. While the bands for lipids and β-sheet of protein were noted for differentiating AP from CONTROL. After being hydrolyzed by Protease G6, the AP hydrolysate disclosed the highest ABTS radical scavenging activity, while the SP hydrolysate revealed the strongest metal chelating ability. Thus, an understanding of how fish processing waste can be utilized in the production of antioxidant protein hydrolysates has been achieved.

Physico-chemical, functional, and structural properties of un-defatted, cold and hot defatted yellow lupin protein isolates

This study investigates the structure, physico-chemical and functional properties of yellow lupin isolate protein (YLPI) obtained by different processes (conventional wet and purely aqueous fractionation) from un-defatted (YLPIU), and hot (YLPIHD) and cold (YLPICD) defatted flour. The defatting process modified the physical, structural and functional characteristics of lupin protein isolates. Indeed, a decrease of α-helix, free sulfhydryl groups amount and an increase of disulfide bond levels were observed for defatted samples, improving their emulsifying stability. The defatting process exposes the hydrophobic groups present within the YLPI, which increases total sulfhydryl content and protein surface hydrophobicity. Hot and cold defatting induced a decrease in turbidity, water-holding capacity, oil adsorption capacity, tapped and poured bulk densities. In addition, the defatting process changed the particle size of protein isolates that induced changes in their viscosity. Tryptophan spectra and protein surface hydrophobicity indicated that YLPICD and YLPIHD underwent structural conformational change during the defatting process.

Effects of dietary Periplaneta americana water extract on growth, chemical composition, muscle antioxidant status, and meat quality of Nile tilapia

Abstract This study investigated the effects of dietary Periplaneta americana water extract (PAWE) supplementation (0, 1, 2, and 4 g/kg) on the chemical composition, antioxidant capacity, and meat quality in Nile tilapia. The results showed that the extract improved weight gaining rated of Nile tilapia (Oreochromis niloticus). Meanwhile, dietary PAWE decreased lactate content, glycolytic potential, centrifugal water loss, and cooking loss, and enhanced muscle pH, protein content, total sulfhydryl content and meat color in Nile tilapia muscle. Dietary PAWE also improved the total antioxidant capability with enhanced superoxide dismutase, catalase, and glutathione peroxidase activities and lowered contents of reactive oxygen species, and lipid and protein oxidation products (i.e. thiobarbituric acid reactive species and protein carbonylation). Moreover, dietary PAWE enhanced the contents of flavor amino acids, total amino acids, adenosine monophosphate, and 5′-inosine monophosphate with enhanced the taste indicators (umami, richness and sweetness). In addition, PAWE supplementation improved myofiber growth and muscle protein deposition likely by activating of the IGFs/PI3K/Akt/TOR/S6K1/4E-BP1 pathway, contributing to the enhanced growth performance of Nile tilapia. The optimal dietary PAWE requirement for maximum growth and muscle protein was approximately 3 g/kg. Together, PAWE is a promising natural food additive that enhances muscle quality and nutritional value of Nile tilapia.

Effect of static magnetic field-assisted thawing on the quality, water status, and myofibrillar protein characteristics of frozen beef steaks

This study investigated the effect of static magnetic field-assisted thawing (SMAT) at varying intensities (0, 1, 2, and 3 mT) on the quality, water status, and myofibrillar protein (MP) characteristics of frozen beef steaks. The thawing times of SMAT-1, 2, and 3 treatments could be shortened by approximately 10.9 %, 20.0 %, and 8.5 %, respectively, compared to the control. The results indicated that SMAT treatment significantly decreased thawing loss, maintained color stability, and reduced the degree of lipid oxidation in beef steaks compared to the control group (P < 0.05). Low-field nuclear magnetic resonance results confirmed that SMAT treatment enhanced the water-holding capacity of muscle. Furthermore, SMAT-2 treatment protected the muscle microstructure, decreased carbonyl content, and increased total sulfhydryl content (P < 0.05) compared to the control group. In conclusion, SMAT treatment effectively improved the beef quality and the characteristics of MP after thawing, especially in 2 mT.

Chitooligosaccharide–gallic acid complexes suppress the denaturation of myofibrillar proteins in peeled shrimp (Litopenaeus vannamei) during frozen storage

SummaryThe cryoprotective effects of chitooligosaccharide–gallic acid (COS–GA) complexes on peeled Pacific white shrimp were investigated and compared with single treatments of COS, GA and polyphosphate (PP) during 49 days of frozen storage at −5 °C. The data revealed a significant improvement in the antioxidant activity of COS through the conjugation of COS and GA. The soaking treatments of COS–GA and PP effectively maintained the water‐holding capacity and sensory properties of shrimp muscle compared with the water‐soaked shrimp (control). Furthermore, the COS–GA‐soaked shrimp samples exhibited significant inhibitory effects on the textural and chrominance deterioration of muscle tissues compared with the control samples. Chemical analyses demonstrated that the COS–GA treatment also preserved higher levels of myofibrillar protein content, total sulfhydryl content and Ca2+‐ATPase activity in the frozen shrimp samples. Histological observations indicated that the COS–GA soaking treatment effectively protected the integrity and stability of muscle tissues. Overall, COS–GA exhibited superior antioxidation and water‐retaining properties, stabilising the shrimp muscle during long‐term frozen storage.

Natural Deep Eutectic Solvent based Ultrasound-assisted extraction: A green approach for extraction of sulfhydryl and mimosine from Leucaena leucocephala (Lam) de Wit seeds

Leucaena leucocephala (Lam.) de Wit seeds, also known as river tamarind, contain sulfhydryl compounds that exhibit antioxidant effects. However, these seeds also possess a toxic effect from mimosine. In this study, the river tamarind seeds were extracted using a natural deep eutectic solvent (NADES) based UAE. Among six NADES compositions screened, choline chloride-glycerol (ChCl-Gly) and choline chloride-sucrose (ChCl-Suc) were selected to be further optimized using a Box-Behnken Design in the RSM. The optimization of total sulfhydryl content was performed in 17 runs using three variables, namely water content in NADES (39%, 41%, and 43%), extraction time (5, 10, and 15 min), and the liquid-solid ratio (3, 5, and 7 mL/g). The highest concentration of sulfhydryls was obtained from ChCl-Gly-UAE (0.89 mg/g sample) under the conditions of a water content in NADES of 41% (v/v) and a liquid-solid ratio of 3 mL/g for 15 min, followed by that of from ChCl-Suc-UAE extract under the conditions of water content in NADES of 43% (v/v) and the liquid-solid ratio of 3 mL/g for 10 min with total sulfhydryl level was 0.67 mg/g sample. The maceration method using 30% ethanol resulted in the lowest level of sulfhydryls with a value of 0.52 mg/g. The mimosine compounds obtained in the NADES-based UAE (ChCl-Suc and ChCl-Gly) extracts were 4.95 and 7.67 mg/g, respectively, while 12.56 mg/g in the 30% ethanol-maceration extract. The surface morphology of L. leucocephala seed before and after extraction was analyzed using scanning electron microscopy. Therefore, it can be concluded that the use of ChCl-Suc and ChCl-Gly in NADES-based UAE is more selective in attracting sulfhydryl compounds than that of 30% ethanol-maceration extraction.

Effect of Flammulina velutipes polysaccharides on the physicochemical properties of catfish surimi and myofibrillar protein oxidation during frozen storage.

This study investigated the effect of Flammulina velutipes polysaccharides (FVPs) on the myofibrillar protein (MP) oxidation protein and physicochemical properties of catfish surimi during 75 days of frozen storage at -18°C. FVP was added to surimi at 1%, 1.5%, and 2%, respectively; the degree of MP oxidation and the physicochemical properties of the surimi were investigated, and the microstructure of the surimi was observed by scanning electron microscopy (SEM). The results showed that the carbonyl content and the thiobarbituric acid reactive substances (TBARS) in the FVP groups were lower than those in the CK group (the blank surimi). In comparison, the total sulfhydryl content, solubility, and Ca2+-ATPase activity were higher than those in the CK group after 75 days of storage. The addition of FVP significantly increased the water-holding capacity (WHC), gel strength, elastic modulus (G'), and loss modulus (G") of surimi, and made the gel of surimi have stronger continuity and a denser structure. Therefore, FVP has a better cryoprotective effect on surimi. It improves the quality of surimi, decreases MP oxidation, and reduces lipid and water loss during frozen storage. The anti-freezing effect of FVP added at 2% was similar to that of commercial protectants (4% sucrose and 4% sorbitol).

Zingerone neuroprotective effects in a rat model of manic-like behavior induced by ketamine

Bipolar disorder (BD), before known as manic depression, is a chronic illness and a mood disorder characterized by manic and depressive periods. Drugs used to treat bipolar disorder can cause side effects if used chronically. Therefore, new therapeutic approaches are needed for treatment of BD. Given that inflammatory parameters and oxidative markers increase in BD and on the other hand there are a lot of evidences that zingerone (ZGR) has antioxidant and anti-inflammatory effects, the aim of this study was to investigate the neuroprotective effects of ZGR as one of the active phytochemicals existing in ginger in a model of manic-like behavior (MLB) induced by ketamine (KET) in rats. Thirty-six rats were randomly divided into six groups, including three groups of healthy rats: control, lithium chloride (LiCl) (45 mg/kg, p.o.) and ZGR (50 mg/kg, p.o.), and three groups of MLB rats (received 25 mg/kg KET, i.p. from day 8 to day 15): control, lithium (45 mg/kg, p.o.) and ZGR (50 mg/kg, p.o.). Pre-treatment with ZGR (50 mg/kg) once daily or LiCl (45 mg/kg) twice a day for 14 days prevented all KET-induced changes except total sulfhydryl content (total SH), which was not significant. The data of this study showed that 25 mg/kg KET increased the number of crossings in the open-field test and induced oxidative and inflammatory damage in the rat hippocampus (HPC) and prefrontal cortex (PFC). KET increased thiobarbituric acid reactive substances (TBARS), nitric oxide (NO), and tumor necrosis factor-alpha (TNF-α) levels; and decreased the activity of catalase (CAT) and superoxide dismutase (SOD) enzymes as well as the amount total SH in the HPC and PFC. These findings suggest that oxidative stress (OS) and inflammation may play an important role in BD, and ZGR as an anti-inflammatory and antioxidant agent might be able to reduce the oxidative and inflammatory damage related to the manic phase of this disorder.

Ionic strength-mediated protein and flavor studies on thermally processed hairtail pieces.

This study aimed to investigate the impact of different ionic strengths on the texture, protein, and flavor of thermally processed hairtail pieces. Incorporating salt ions into the heat treatment process had a positive impact on the quality of the cooked hairtail pieces. The pieces treated with 2M NaCl showed superior texture and sensory scores. The ionic strength had a significant positive correlation with the chewiness and cohesion of cooked hairtail (p<0.01). Furthermore, the myofibrillar protein content and total sulfhydryl content increased significantly. Circular dichroism spectra analysis revealed a transition in the protein structure from a β-sheet structure to an α-helical structure as the ionic strength decreased. The ionic strength had a significant impact on the interaction between protein and flavor compounds. Specifically, it impacted the expression of certain volatile components (p<0.05). Our study suggests that selecting the appropriate cooking method is crucial for both healthiness and sensory quality of processed hairtail products, and ionic strength mediation is superior in both aspects.

Catechins affect the oil-holding capacity of meat batters by changing the structure and emulsifying properties of surface proteins at the fat globules

The effects of different concentrations of catechins on the oil-holding capacity, myofibrillar proteins (MPs) structure and adsorbed properties of interfacial proteins in meat batters were investigated. The addition of 100 mg/kg catechin had no negative effects on the physicochemical properties of meat batter. However, 500 and 1500 mg/kg catechin caused an increase in drip loss and deterioration of dynamic rheological properties; the total sulfhydryl content, surface hydrophobicity and α-helix ratio of MPs decreased significantly (p < 0.05); in meat emulsions, the emulsifying property was reduced, the particle size increased, and less interfacial protein was absorbed on the fat globules. All concentrations of catechins significantly (p < 0.05) inhibited lipid oxidation in meat batters. Medium and high concentrations of catechins induced aggregation of MPs via covalent and noncovalent interactions between MPs and MPs or MPs and catechins, which destroyed the gel and emulsifying property of protein and eventually decrease the oil-holding capacity of meat batters.

Whey Protein Hydrolysate Improved the Structure and Function of Myofibrillar Protein in Ground Pork during Repeated Freeze-Thaw Cycles.

Whey protein hydrolysate (WPH) has made a breakthrough in inhibiting oxidative deterioration and improving the quality of meat products during storage. Based on our previous study of extracting the most antioxidant active fraction I (FI, the molecular weight < 1 kDa) from whey protein hydrolysates of different molecular weights, the present study continued to delve into the effects of WPH with fraction I on the structure and function of myofibrillar proteins (MP) in ground pork during the freeze-thaw (F-T) cycles. With the number of F-T cycles raised, the total sulfhydryl content, the relative contents of α-helix, Ca2+-ATPase activity, K+-ATPase activity, solubility, emulsion activity index (EAI), and emulsion stability index (ESI) of MP gradually decreased. Conversely, the carbonyl content and the relative content of random curl showed an increasing trend. In particular, the damage to the structure and the function of MP became more pronounced after three F-T cycles. But, during F-T cycles, FI stabilized the structure of MP. Compared to the control group, the 10% FI group showed a remarkable improvement (p < 0.05) in the total sulfhydryl content, Ca2+-ATPase activity, K+-ATPase activity, solubility, EAI and ESI after multiple F-T cycles, suggesting that 10% FI could effectively inhibit protein oxidation and had the influence of preserving MP function properties. In conclusion, WPH with fraction I can be used as a potential natural antioxidant peptide for maintaining the quality of frozen processed meat products.

Effect of pulsed light on myofibrillar protein of large yellow croaker (Pseudosciaena crocea) during refrigerated storage.

This study mainly evaluated the effect of different energies of pulsed light (PL) treatment (100, 200, 300, 400, and 500J/pulse) on myofibrillar protein (MP) of large yellow croaker during refrigerated storage. The results showed that PL treatment would cause a certain degree of oxidation to the MP of large yellow croaker at the initial stage, which showed that the total sulfhydryl content of the protein decreased, the carbonyl content and the average particle size increased, and the β-sheet to β-turn transformation, the tertiary structure of the protein unfolds, and the hydrophobic groups were exposed, causing the reduction of intrinsic fluorescence intensity. However, subsequent storage studies found that PL treatment could slow down the oxidation rate of MP. The decrease rate of total sulfhydryl content and the increase rate of carbonyl content in the 300J/pulse group were both reduced by about 1.7 times compared with the control group. At the same time, the PL treatment with this intensity could also better protect the secondary structure, tertiary structure, and microstructure of MP. This study provided theoretical basis and reference for analyzing the quality change rule and mechanism of large yellow croaker during refrigerated storage after PL treatment. Studies have shown that PL treatment can reduce the adverse changes of MP in large yellow croaker during cold storage.

Sub‑chronic administration of lead alters markers of oxidative stress, acetylcholinesterase and Na+K+‑ATPase activities in rat brain.

This study investigated the effects of sub‑chronic administration of lead (Pb) acetate on thiobarbituric acid reactive substances (TBA‑RS), total sulfhydryl content, protein carbonyl content, antioxidant enzymes (superoxide dismutase [SOD], catalase [CAT], glutathione peroxidase [GSH‑Px]), acetylcholinesterase (AChE), and Na+K+‑ATPase in the cerebral structures of rats. Male Wistar rats aged 60 days were treated with saline (control group) or Pb (treatment group), at various doses, by gavage, once a day for 35 days. The animals were sacrificed twelve hours after the last administration, and the cerebellum, hippocampus and cerebral cortex were removed. The results showed that Pb did not alter the evaluated oxidative stress parameters. Furthermore, Pb (64 and/or 128 mg/kg) altered SOD in the cerebellum, cerebral cortex and hippocampus. Pb (128 mg/kg) altered CAT in the cerebellum and cerebral cortex and GSH‑Px in the cerebral cortex. Also, Pb (64 mg/kg and 128 mg/kg) altered GSH‑Px in the cerebellum. Moreover, Pb (128 mg/kg) increased AChE in the hippocampus and decreased Na+K+‑ATPase in the cerebellum and hippocampus. In conclusion, sub‑chronic exposure to Pb (occupational and environmental intoxication) altered antioxidant enzymes, AChE, and Na+K+‑ATPase, contributing to cerebral dysfunction.

Effect of Freezing on Soybean Protein Solution.

To investigate the impact of frozen storage conditions on the physicochemical properties of soybean protein and explore the underlying mechanisms, this study focused on soybean isolate (SPI), ß-soybean companion globulin (7S), and soybean globulin (11S). The protein solutions were prepared at a concentration of 2% and subjected to freezing for 1 and 5 days. Subsequently, the protein content, physicochemical properties, secondary structure, sulfhydryl content, and chemical interaction forces were assessed and analyzed using UV spectrophotometry, Zeta potential measurements, SDS-PAGE, Fourier infrared spectroscopy, and endogenous fluorescence photoemission spectroscopy. The obtained results revealed that the solubility and total sulfhydryl content of SPI, 7S, and 11S exhibited a decreasing trend with prolonged freezing time. Among them, 11S demonstrated the largest decrease in solubility and total sulfhydryl content, followed by SPI, and 7S the least. During freezing, the aromatic amino acids of SPI, 7S, and 11S molecules were exposed, leading to increased hydrophobicity, protein aggregation, and particle size enlargement, and the structure of the protein changed from disordered structure to ordered structure. After freezing, the polarity of the microenvironment of SPI, 7S, and 11S increased, and their maximum fluorescence emission wavelengths were red-shifted. Notably, the largest red shift of SPI was from 332 nm to 335 nm. As freezing time increased, the contribution of hydrogen bonding increased, while the contribution of hydrophobic interactions decreased. This indicates that freezing affects the hydrophobic interactions, hydrogen bonding, and other chemical forces of the protein. The growth of ice crystals leads to the unfolding of protein molecular chains, exposure of internal hydrophobic groups, enhancement of hydrophobicity, and alters the secondary structure of the protein.

Characterization and techno-functional properties of Tenebrio molitor larvae protein concentrate

Global population growth and an alarming rate of global warming conditions have driven the need for protein from alternative non-conventional sources, namely, insect proteins, through a sustainable approach. The protein concentrate of Tenebrio molitor larvae was examined for its suitability and applicability as a food ingredient. Protein was extracted through the acid-alkali method with ∼79% of extraction efficiency. The protein-bound polyphenols were extracted and quantified, and the anti-oxidant potential of protein-bound polyphenols and protein concentrate was assessed. The colour parameters of protein concentrate showed brighter colour (L*, 57.3) than the whole insect powder (L*, 39.0). The surface hydrophobicity of protein concentrate increased to 650, and an increase in the total and free sulfhydryl content (15.39 and 9.158 μmol/g, respectively) was also observed compared to the whole insect powder. Significantly higher protein solubility was observed at pH 2 (72.3%) and pH 11 (66.4%), as compared to near the pI (6.9% at pH 5 and 30.15% at pH 4). Several prominent proteins, including 86 and 56 kDa early-staged encapsulation-inducing proteins, cuticle proteins, and structural proteins were identified in protein concentrate. The techno-functional properties revealed that mealworm protein concentrate was superior to whole insect powder and comparable to whey protein isolate. These findings confirmed the excellent functional properties of mealworm protein concentrate, which can be further explored as a novel food ingredient.