Major Storage Protein Research Articles

Upcycling of Defatted Sesame Seed Meal via Protein Amyloid-Based Nanostructures: Preparation, Characterization, and Functional and Antioxidant Attributes.

Herein, the possibility of valorizing defatted sesame seed meal (DSSM) as a viable source for valuable plant proteins and amyloid-based nanostructure was investigated. Sesame seed protein isolate (SSPI) and the major storage protein globulin (SSG) were prepared by alkaline extraction-isoelectric point precipitation as well as fractionation in the case of SSG. The protein samples were characterized for their physicochemical attributes. SSPI and SSG were also evaluated for their ability to form amyloid structures under heating (90 °C) at low pH (2.0). Additionally, the functional attributes, antioxidant activity, and biocompatibility of the proteins and amyloid nanostructures were also examined. SSPI and SSG were both successfully prepared from DSSM. The data showed that the physicochemical attributes of both protein samples were quite similar, except for the fact that SSG was mostly composed of 11S globulin, as evinced by Tricine-SDS-PAGE analysis. TEM micrographs revealed that SSG was able to form curly-shaped fibrillar amyloid structures, whereas those derived from SSPI were mostly amorphous. Thioflavin-T assay and Tricine-SDS-PAGE analysis indicated that acidic heating promoted protein hydrolysis and self-aggregation of the hydrolyzed peptides into a β-sheet rich amyloid structure. Importantly, the amyloid preparations displayed commendable solubility, superior water and oil holding capacities, and antioxidant activity against DPPH and ABTS. The protein amyloid nanostructures were found to be non-toxic against RAW264.7 cells, HaCaT cells, and red blood cells. These findings indicate that DSSM could be upcycled into valuable protein amyloid structures with good potentialities as novel food ingredients.

A tandem activity-based sensing and labeling strategy reveals antioxidant response element regulation of labile iron pools

Iron is an essential element for life owing to its ability to participate in a diverse array of oxidation-reduction reactions. However, misregulation of iron-dependent redox cycling can also produce oxidative stress, contributing to cell growth, proliferation, and death pathways underlying aging, cancer, neurodegeneration, and metabolic diseases. Fluorescent probes that selectively monitor loosely bound Fe(II) ions, termed the labile iron pool, are potentially powerful tools for studies of this metal nutrient; however, the dynamic spatiotemporal nature and potent fluorescence quenching capacity of these bioavailable metal stores pose challenges for their detection. Here, we report a tandem activity-based sensing and labeling strategy that enables imaging of labile iron pools in live cells through enhancement in cellular retention. Iron green-1 fluoromethyl (IG1-FM) reacts selectively with Fe(II) using an endoperoxide trigger to release a quinone methide dye for subsequent attachment to proximal biological nucleophiles, providing a permanent fluorescent stain at sites of elevated labile iron. IG1-FM imaging reveals that degradation of the major iron storage protein ferritin through ferritinophagy expands the labile iron pool, while activation of nuclear factor-erythroid 2-related factor 2 (NRF2) antioxidant response elements (AREs) depletes it. We further show that lung cancer cells with heightened NRF2 activation, and thus lower basal labile iron, have reduced viability when treated with an iron chelator. By connecting labile iron pools and NRF2-ARE activity to a druggable metal-dependent vulnerability in cancer, this work provides a starting point for broader investigations into the roles of transition metal and antioxidant signaling pathways in health and disease.

Anti-SARS-CoV-2 Viral Activity of Sweet Potato Trypsin Inhibitor via Downregulation of TMPRSS2 Activity and ACE2 Expression In Vitro and In Vivo.

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has caused a global pandemic. Known as COVID-19, it has affected billions of people worldwide, claiming millions of lives and posing a continuing threat to humanity. This is considered one of the most extensive pandemics ever recorded in human history, causing significant losses to both life and economies globally. However, the available evidence is currently insufficient to establish the effectiveness and safety of antiviral drugs or vaccines. The entry of the virus into host cells involves binding to angiotensin-converting enzyme 2 (ACE2), a cell surface receptor, via its spike protein. Meanwhile, transmembrane protease serine 2 (TMPRSS2), a host surface protease, cleaves and activates the virus's S protein, thus promoting viral infection. Plant protease inhibitors play a crucial role in protecting plants against insects and/or microorganisms. The major storage proteins in sweet potato roots include sweet potato trypsin inhibitor (SWTI), which accounts for approximately 60% of the total water-soluble protein and has been found to possess a variety of health-promoting properties, including antioxidant, anti-inflammatory, ACE-inhibitory, and anticancer functions. Our study found that SWTI caused a significant reduction in the expression of the ACE2 and TMPRSS2 proteins, without any adverse effects on cells. Therefore, our findings suggest that the ACE2 and TMPRSS2 axis can be targeted via SWTI to potentially inhibit SARS-CoV-2 infection.

Developmental regulation of zinc homeostasis in differentiating oligodendrocytes

Oligodendrocytes develop through sequential stages and understanding pathways regulating their differentiation remains an important area of investigation. Zinc is required for the function of enzymes, proteins and transcription factors, including those important in myelination and mitosis. Our previous studies using the ratiometric zinc sensor chromis-1 demonstrated a reduction in intracellular free zinc concentrations in mature MBP+ oligodendrocytes compared with earlier stages (Bourassa et al., 2018). We performed a more detailed developmental study to better understand the temporal course of zinc homeostasis across the oligodendrocyte lineage. Using chromis-1, we found a transient increase in free zinc after O4+,O1− pre-oligodendrocytes were switched from proliferation medium into terminal differentiation medium. To gather other evidence for dynamic regulation of free zinc during oligodendrocyte development, qPCR was used to evaluate mRNA expression of major zinc storage proteins metallothioneins (MTs) and metal regulatory transcription factor 1 (MTF1), which controls expression of MTs. MT1, MT2 and MTF1 mRNAs were increased several fold in mature oligodendrocytes compared to oligodendrocytes in proliferation medium. To assess the depth of the zinc buffer, we assayed zinc release from intracellular stores using the oxidizing thiol reagent 2,2′-dithiodipyridine (DTDP). Exposure to DTDP resulted in ∼ 100% increase in free zinc in pre-oligodendrocytes but, paradoxically more modest ∼ 60% increase in mature oligodendrocytes despite increased expression of MTs. These results suggest that zinc homeostasis is regulated during oligodendrocyte development, that oligodendrocytes are a useful model for studying zinc homeostasis in the central nervous system, and that regulation of zinc homeostasis may be important in oligodendrocyte differentiation.

Integrated metabolome and transcriptome analyses reveal the molecular mechanism underlying dynamic metabolic processes during taproot development of Panax notoginseng

BackgroundPanax notoginseng (Burk) F. H. Chen is one of the most famous Chinese traditional medicinal plants. The taproot is the main organ producing triterpenoid saponins, and its development is directly linked to the quality and yield of the harvested P. notoginseng. However, the mechanisms underlying the dynamic metabolic changes occurring during taproot development of P. notoginseng are unknown.ResultsWe carried out metabolomic and transcriptomic analyses to investigate metabolites and gene expression during the development of P. notoginseng taproots. The differentially accumulated metabolites included amino acids and derivatives, nucleotides and derivatives, and lipids in 1-year-old taproots, flavonoids and terpenoids in 2- and 3-year-old taproots, and phenolic acids in 3-year-old taproots. The differentially expressed genes (DEGs) are related to phenylpropanoid biosynthesis, metabolic pathway and biosynthesis of secondary metabolites at all three developmental stages. Integrative analysis revealed that the phenylpropanoid biosynthesis pathway was involved in not only the development of but also metabolic changes in P. notoginseng taproots. Moreover, significant accumulation of triterpenoid saponins in 2- and 3-year-old taproots was highly correlated with the up-regulated expression of cytochrome P450s and uridine diphosphate-dependent glycosyltransferases genes. Additionally, a gene encoding RNase-like major storage protein was identified to play a dual role in the development of P. notoginseng taproots and their triterpenoid saponins synthesis.ConclusionsThese results elucidate the molecular mechanism underlying the accumulation of and change relationship between primary and secondary metabolites in P. notoginseng taproots, and provide a basis for the quality control and genetic improvement of P. notoginseng.

Dysfunction in atox-1 and ceruloplasmin alters labile Cu levels and consequently Cu homeostasis in C. elegans.

Copper (Cu) is an essential trace element, however an excess is toxic due to its redox properties. Cu homeostasis therefore needs to be tightly regulated via cellular transporters, storage proteins and exporters. An imbalance in Cu homeostasis has been associated with neurodegenerative disorders such as Wilson's disease, but also Alzheimer's or Parkinson's disease. In our current study, we explored the utility of using Caenorhabditis elegans (C. elegans) as a model of Cu dyshomeostasis. The application of excess Cu dosing and the use of mutants lacking the intracellular Cu chaperone atox-1 and major Cu storage protein ceruloplasmin facilitated the assessment of Cu status, functional markers including total Cu levels, labile Cu levels, Cu distribution and the gene expression of homeostasis-related genes. Our data revealed a decrease in total Cu uptake but an increase in labile Cu levels due to genetic dysfunction, as well as altered gene expression levels of Cu homeostasis-associated genes. In addition, the data uncovered the role ceruloplasmin and atox-1 play in the worm's Cu homeostasis. This study provides insights into suitable functional Cu markers and Cu homeostasis in C. elegans, with a focus on labile Cu levels, a promising marker of Cu dysregulation during disease progression.

Effects of pH and salt concentration on freeze-thaw fractionation of soymilk protein.

The two major storage proteins of soymilk are the globulins 7S and 11S. Freeze-thaw fractionation is a simple method for separating these proteins in raw soymilk. In this study, we assessed the freeze-thaw fractionation ability of raw soymilk under various pH (4.3-11.6) conditions and added salt (sodium chloride) concentrations (0.00-0.67 mol L-1). We successfully achieved fractionation within a pH range of 5.8-6.7 and when the salt concentration was 0.22 mol L-1 or lower. Analysis of particle size distribution and microscopic examination of soymilk revealed no direct correlation between particle size and freeze-thaw fractionation ability. Interestingly, it was confirmed that the ranges of zeta potential values associated with successful freeze-thaw fractionation in raw soymilk remained consistent across different pH and salt concentration conditions. These ranges were between -23 and -28 mV at pH levels ranging from 5.8 to 6.7 and between -18 and -29 mV at added salt concentrations ranging from 0 to 0.22 mol L-1. The pH and salt concentration in raw soymilk markedly influence the freeze-thaw fractionation process. We confirmed that the range of zeta potential values where fractionation was possible remained consistent under various pH and salt concentration conditions. These findings suggest that the zeta potential value might serve as an indicator for evaluating the freeze-thaw fractionation ability of raw soymilk. © 2024 Society of Chemical Industry.

Relationships between protein and other chemical composition and texture of tofu made from soybeans grown in different locations.

Understanding quantitative relationships between protein and other chemical components in diverse soybean genotypes (lines) grown in different locations and the firmness of tofu can provide scientific insight for selecting soybean suitable for tofu making. Locations showed significant effects on seed components, including total protein, major storage proteins, subunits and polypeptides of the major storage proteins, and calcium, but not magnesium or phytic acid. Results showed that 11S content, but not 11S/7S ratio, was only correlated with filled tofu firmness when analyzed over all locations. A strong and positive correlation between firmness and A3 polypeptide of the 11S protein content was found for both pressed tofu (r=0.80, p<0.001) and filled tofu (r=0.76, p<0.001) over three locations (overall pooled data) and within most individual locations. The correlation of filled tofu firmness and A3 polypeptide was significant for each of the three individual locations. However, the correlation of pressed tofu firmness and A3 polypeptide content was significant at two of three locations. Mean calcium content was positively correlated with mean pressed and filled tofu firmness over all locations, but calcium was not correlated with pressed tofu firmness at any individual location, and only one location showed a significant correlation of calcium and filled tofu firmness. In addition, pressed tofu firmness was found to be negatively correlated with tofu yield. The findings that A3 polypeptide's strong relationship with tofu firmness within certain locations may be used by the food industry to select proper soybean for manufacturing tofu and to facilitate tofu soybean breeding for tofu making.

Deep learning-based characterization and redesign of major potato tuber storage protein

Potato is one of the most important crops worldwide, to feed a fast-growing population. In addition to providing energy, fiber, vitamins, and minerals, potato storage proteins are considered as one of the most valuable sources of non-animal proteins due to their high essential amino acid (EAA) index. However, low tuber protein content and limited knowledge about potato storage proteins restrict their widespread utilization in the food industry. Here, we report a proof-of-concept study, using deep learning-based protein design tools, to characterize the biological and chemical characteristics of patatins, the major potato storage proteins. This knowledge was then employed to design multiple cysteines on the patatin surface to build polymers linked by disulfide bonds, which significantly improved viscidity and nutrient of potato flour dough. Our study shows that deep learning-based protein design strategies are efficient to characterize and to create novel proteins for future food sources.

Neltuma nigra cotyledon and seed flour: nutritional, phytochemical, and techno-functional characterization and nutraceutic potential of polyphenolic enriched extract.

Neltuma nigra seed and cotyledon flours were prepared and characterized. Both flours showed high protein and fiber content, and low carbohydrate and fat content. The major storage proteins in N. nigra flours were albumin and globulin. In addition, flours contained carotenoids and potassium as the main micronutrients. The free and bound phenolic compounds, tannins and flavonoids were the major phytochemical components. The phenolic enriched extracts (PEE) of both flours contained apigenin-derived C-glycosyl flavones, including schaftoside, and isoschaftoside as the main components. The PEE from seed flour contained higher antioxidant capacity on ABTS˙+, FRAP, H2O2, O2˙- and higher inhibitory effect on α-amylase and α-glucosidase than the cotyledon flour extract. Techno-functional property analyses showed better water retention capacity and emulsifying stability for cotyledon flour and better oil holding capacity and emulsifying activity for seed flour. The results suggest better biological properties and a low-cost accessibility of seed flour, and a better macronutrient balance for cotyledon flour. Therefore, both can be considered as ingredients or functional food for special foods related to the metabolic syndrome and diseases related to oxidative processes.

Iron derived from NCOA4-mediated ferritinophagy causes cellular senescence via the cGAS-STING pathway

Cellular senescence is a hallmark of aging and has been linked to age-related diseases. Age-related macular degeneration (AMD), the most common aging-related retinal disease, is prospectively associated with retinal pigment epithelial (RPE) senescence. However, the mechanism of RPE cell senescence remains unknown. In this study, tert-butyl hydroperoxide (TBH)-induced ARPE-19 cells and D-galactose-treated C57 mice were used to examine the cause of elevated iron in RPE cell senescence. Ferric ammonium citrate (FAC)-treated ARPE-19 cells and C57 mice were used to elucidated the mechanism of iron overload-induced RPE cell senescence. Molecular biology techniques for the assessment of iron metabolism, cellular senescence, autophagy, and mitochondrial function in vivo and in vitro. We found that iron level was increased during the senescence process. Ferritin, a major iron storage protein, is negatively correlated with intracellular iron levels and cell senescence. NCOA4, a cargo receptor for ferritinophagy, mediates degradation of ferritin and contributes to iron accumulation. Besides, we found that iron overload leads to mitochondrial dysfunction. As a result, mitochondrial DNA (mtDNA) is released from damaged mitochondria to cytoplasm. Cytoplasm mtDNA activates the cGAS-STING pathway and promotes inflammatory senescence-associated secretory phenotype (SASP) and cell senescence. Meanwhile, iron chelator Deferoxamine (DFO) significantly rescues RPE senescence and retinopathy induced by FAC or D-gal in mice. Taken together, these findings imply that iron derived from NCOA4-mediated ferritinophagy causes cellular senescence via the cGAS-STING pathway. Inhibiting iron accumulation may represent a promising therapeutic approach for age-related diseases such as AMD.

In vitro α-Amylase and α-Glucosidase Inhibitory Activity of Dioscorin from Dioscorea alata

Dioscorea alata is a species of yam found in many countries in Southeast Asia. It contains many bioactive compounds consisting of steroidal saponins, phenolic compounds flavonoids, polysaccharides, and proteins. Eighty to eighty-five of the soluble proteins in the tuber of D. alata are dioscorin. Dioscorin (31 kDa) is the major storage protein of yam tuber, exhibiting biochemical and immunomodulatory properties, such as antioxidant activity, reducing blood pressure and angiotensin I converting enzyme (ACE) inhibitors activity. The aims of this research focused on extraction of the total soluble protein from D. alata tuber, purification of dioscorin, and study of in vitro inhibitory activity of α-amylase and α-glucosidase of dioscorin extracts. The results showed that a maximum yield of total soluble protein was obtained from the buffers extraction using Tris-HCl buffer at pH 9.0 resulting in the protein concentration of 15.10 mg/g with a protein extraction yield of 31.56 ± 2.36%. The crude protein was further recovered using ammonium sulfate precipitation and dialysis. SDS-PAGE analysis showed that dioscorin from crude extracts was precipitated at the concentration of ammonium sulfate of 60% saturation. The purified dioscorin was obtained from anion exchange chromatography (DEAE-Sephacel) and its molecular weight of 31 kDa was estimated on SDS-PAGE. Furthermore, the α-amylase inhibitory activities of crude extract (1 mg/mL), purified dioscorin obtain from gastric digestion and purified dioscorin obtained from intestinal digestion were at 14.44% 2.21% and 78.13%, respectively. Moreover, the results showed that the α-glucosidase inhibitory activity of the crude extract, and purified dioscorin obtained from gastric digestion were at 10.56% and 2.61%, respectively.

Zein as a Basis of Recyclable Injection Moulded Materials: Effect of Formulation and Processing Conditions.

The growing concern about reducing carbon footprint has led to the progressive replacement of traditional polymeric materials by natural-based biodegradable materials. However, materials from natural sources (i.e., plants) typically possess poorer mechanical properties when compared to conventional plastics. To counterbalance this, they need to be adequately formulated and processed to eventually meet the standards for certain applications. Zein is the major storage protein from corn and can be obtained as a by-product from the corn-oil industry. It is an excellent candidate for producing green materials due to its stability, biodegradability, renewability, and suitable mechanical and technical-functional properties. In the present work, zein was blended with a plasticizer (i.e., glycerol) at three different zein/glycerol ratios (75/25, 70/30, and 65/25) and then injection moulded at three different processing temperatures (120, 150, and 190 °C). The properties of both blends and bioplastics were evaluated using dynamic mechanical analysis (DMA), tensile tests, and water absorption capacity (WUC). The properties-structure interrelation was assessed through a scanning electron microscope. Generally, a higher zein content and processing temperature led to a certain reinforcement of the samples. Moreover, all bioplastics displayed a thermoplastic behaviour finally melting at temperatures around 80 °C. The lack of massive crosslinking enabled this melting, which finally could be used to confirm the ability of zein based materials to be recycled, while maintaining their properties. The recyclability of thermoplastic zein materials widens the scope of their application, especially considering its biodegradability.

Proteome Changes Resulting from Malting in Hordein-Reduced Barley Lines.

Hordeum vulgare L., commonly known as barley, is primarily used for animal feed and malting. The major storage proteins in barley are hordeins, known triggers of celiac disease (CD). Here, sequential window acquisition of all theoretical mass spectra (SWATH)-MS proteomics was employed to investigate the proteome profile of grain and malt samples from the malting barley cultivar Sloop and single-, double-, and triple hordein-reduced lines bred in a Sloop background. Using a discovery proteomics approach, 2688 and 3034 proteins were detected from the grain and malt samples, respectively. By utilizing label-free relative quantitation through SWATH-MS, a total of 2654 proteins have been quantified from grain and malt. The comparative analyses between the barley grain and malt samples revealed that the C-hordein-reduced lines have a more significant impact on proteome level changes due to malting than B- and D-hordein-reduced lines. Upregulated proteins in C-hordein-reduced lines were primarily involved in the tricarboxylic acid cycle and fatty acid peroxidation processes to provide more energy for seed germination during malting. By applying proteomics approaches after malting in hordein-reduced barley lines, we uncovered additional changes in the proteome driven by the genetic background that were not apparent in the sound grain. Our findings offer valuable insights for barley breeders and maltsters seeking to understand and optimize the performance of gluten-free grains in malt products.

A sequential fractionation approach to understanding the physicochemical and functional properties of aqueous and enzyme-assisted aqueous extracted black bean proteins

Black bean proteins were sequentially extracted and characterized to determine the contribution of protein classes to the extractability, thermal behavior, and functionality of protein extracts produced by aqueous (AEP) and enzyme-assisted aqueous extraction processes (EAEP). Osborne fractionation showed that 56% of black bean proteins were water-soluble (albumin-rich), 22% salt-soluble (globulin-rich), 16% alkaline-soluble (glutelin-rich) and 0.65% alcohol-soluble (prolamin-rich). Protein extraction yields of 75 and 81% were achieved by AEP (pH 9.0, 50 °C, 1:10 solids-to-liquid ratio, 60 min) and EAEP (same conditions as AEP with 0.5% (w/w) alkaline protease), respectively. Gel electrophoresis demonstrated differences in the protein molecular weight profile in each fraction, as well as extensive proteolysis of major storage proteins in the EAEP. Proteomics revealed that similar proteins were present among the albumin-, globulin-, and glutelin-rich fractions, but in different proportions to yield distinct protein profiles. AEP and EAEP proteins had similar denaturation temperatures (Td = 92 °C) but were lower than the albumin- and globulin-rich fractions. There was not a clear association between solubility, emulsifying, and foaming properties for the protein classes, which highlighted the complex nature of the protein extracts, as well as potential impacts of the honogemization process on the surface properties of the proteins. Proteolysis significantly increased solubility at pH 4.5 (50 vs. 93%) and decreased foaming capacity at pH 4.5 and 7.0, while emulsifying capacity was not affected. Overall, the results demonstrate that enzyme-assisted extraction is a feasible method to increase black bean protein extractability while retaining thermal stability and modifying some functional properties.

From grain to malt: Tracking changes of ultra-low-gluten barley storage proteins after malting

Barley (Hordeum vulgare L.) is a major cereal crop produced globally. Hordeins, the major storage proteins in barley, can trigger immune responses leading to celiac disease or symptoms associated with food allergy. Here, proteomics approaches were employed to investigate the proteome level changes of grain and malt from the malting barley cultivar, Sloop, and single-, double- and triple hordein-reduced lines. The triple hordein-reduced line is an ultra-low gluten barley cultivar, Kebari®. Using discovery proteomics, 2,688 and 3,034 proteins in the barley and malt samples were detected respectively. Through the application of targeted proteomics, a significant reduction in the quantity of B-, D-, and γ-hordeins, as well as avenin-like proteins, was observed in the ultra-low gluten malt sample. A compensation mechanism was observed evidenced by increased biosynthesis of seed storage globulins, specifically vicilin-like globulins. Overall, this study has provided insights into protein compositional changes after malting in celiac-friendly barley varieties.

Unfolding the Dynamics of Mineral Nutrients and Major Storage Protein Fractions during Soybean Seed Development

Unfolding the Dynamics of Mineral Nutrients and Major Storage Protein Fractions during Soybean Seed Development

Extension Region Domain of Soybean 7S Globulin Contributes to Serum Triglyceride-Lowering Effect via Modulation of Bile Acids Homeostasis.

Soybean 7S globulin (β-conglycinin), a major soybean storage protein, has been demonstrated to exert remarkable triglyceride (TG) and cholesterol-lowering effects, yet the underlying mechanism remains controversial. A comparative investigation is performed to assess the contribution of different structural domains of soybean 7S globulin, including core region (CR) and extension region (ER) domains, to biological effects of soybean 7S globulin using a high-fat diet rat model. The results show that ER domain mainly contributes to the serum TG-lowering effect of soybean 7S globulin, but not for CR domain. Metabolomics analysis reveals that oral administration of ER peptides obviously influences the metabolic profiling of serum bile acids (BAs), as well as significantly increased the fecal excretion of total BAs. Meanwhile, ER peptides supplementation reshapes the composition of gut microbiota and impacts the gut microbiota-dependent biotransformation of BAs which indicate by a significantly increased secondary BAs concentration in fecal samples. These results highlight that TG-lowering effects of ER peptides mainly stem from their modulation of BAs homeostasis. Oral administration of ER peptides can effectively lower serum TG level by regulating BAs metabolism. ER peptides have potential to be used as a candidate pharmaceutical for the intervention of dyslipidemia.

The Distribution of Ferritins in Marine Copepods

Iron is an essential element for the functioning of cellular processes. Ferritins, the major intracellular iron storage proteins, convert the free Fe2+ into the nontoxic Fe3+ which can be stored and transported where needed. To date, little is known about the iron metabolism in copepods; however, in these crustaceans, ferritins have been used as biomarkers of stress and diapause. A limiting factor of these studies has been the use of a single ferritin transcript as a biomarker. In this paper, we in silico mined the publicly available copepod transcriptomes to characterize the multiplicity of the ferritin transcripts in different orders and families. We also examined the expression of ferritin in three ecologically important copepods—Calanus finmarchicus, C. helgolandicus and Temora stylifera—during development and under stress conditions. A full-length transcript encoding ferritin heavy chain has been identified in all 27 mined transcriptomes, with 50% of the species possessing multiple transcripts. Ferritin expression increased in C. finmarchicus during the early–late development transition, and in T. stylifera females exposed to oxylipins at sea. Overall, our results suggest that copepod ferritins can be involved in iron storage, larval development and stress response, thus representing potential biomarker genes for ocean health status monitoring.

Revealing the mechanism underlying the effects of γ-aminobutyric acid-dioscorin interactions on dioscorin structure and emulsifying properties by molecular dynamic simulations

Many studies have shown that γ-aminobutyric acid (GABA) exhibits various beneficial biological activities, including gut-modulating, neuro-stimulating, and cardio-protecting activities. Naturally, GABA exists in small amounts in yam, which is primarily synthesized by the decarboxylation of L-glutamic acid in the presence of glutamate decarboxylase. Dioscorin, the major tuber storage protein of yam, has been shown to have good solubility and emulsifying activity. However, how GABA interacts with dioscorin and affects their properties has yet to be clarified. In this research, the physicochemical and emulsifying properties of GABA-fortified dioscorin, which was dried by spray drying and freeze drying, were studied. As results, the freeze-dried (FD) dioscorin produced more stable emulsions, while the spray-dried (SD) dioscorin adsorbed more rapidly to oil/water (O/W) interface. The fluorescence spectroscopy, ultraviolet spectroscopy and circular dichroism spectroscopy showed that GABA changed the structure of dioscorin, by exposing its hydrophobic groups. The addition of GABA significantly promoted the adsorption of dioscorin to the O/W interface and prevented droplets coalescence. The results of molecular dynamics simulation (MD) showed that GABA destroyed the H-bond network between dioscorin and water, increased surface hydrophobicity and finally improved the emulsifying properties of dioscorin.