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An egg yolk protein by-product following ethanol extraction of phospholipids (YP) was hydrolyzed with pepsin to produce and identify novel peptides that revealed antioxidant, ACE inhibitory and antidiabetic (α-glucosidase and DPP-IV inhibitory) activities. The peptic hydrolysate of YP was fractionated by ion-exchange chromatography and reversed-phase high-pressure liquid chromatography. Isolated peptides were identified using mass spectrometry (MALDI-ToF) and the Mascot Search Results database. Four peptides of MW ranging from 1,210.62 to 1,677.88 Da corresponded to the fragments of Apolipoprotein B (YINQMPQKSRE; YINQMPQKSREA), Vitellogenin-2 (VTGRFAGHPAAQ) and Apovitellenin-1 (YIEAVNKVSPRAGQF). These peptides were chemically synthesized and showed antioxidant, ACE inhibitory or/and antidiabetic activities. Peptide YIEAVNKVSPRAGQF exerted the strongest ACE inhibitory activity, with IC₅₀ = 9.4 µg/mL. The peptide YINQMPQKSRE showed the strongest DPPH free radical scavenging and DPP-IV inhibitory activities and its ACE inhibitory activity (IC₅₀) reached 10.1 µg/mL. The peptide VTGRFAGHPAAQ revealed the highest α-glucosidase inhibitory activity (IC₅₀ = 365.4 µg/mL). A novel nutraceutical effect for peptides from an egg yolk hydrolysate was shown.

Female to male sex reversal was achieved in an emerging agricultural insect pest, Drosophila suzukii , by creating a temperature-sensitive point mutation in the sex-determination gene, transformer-2 ( tra-2 ), using CRISPR/Cas9 (clustered regularly interspaced palindromic repeats/CRISPR-associated) homology-directed repair gene-editing. Ds-tra-2 ts2 mutants developed as normal fertile XX and XY adults at permissive temperatures below 20 °C, but at higher restrictive temperatures (26 to 29 °C) chromosomal XX females developed as sterile intersexuals with a predominant male phenotype, while XY males developed with normal morphology, but were sterile. The temperature-dependent function of the Ds-TRA-2 ts2 protein was also evident by the up- and down-regulation of female-specific Ds-Yolk protein 1 ( Ds-Yp1 ) gene expression by temperature shifts during adulthood. This study confirmed the temperature-dependent function of a gene-edited mutation and provides a new method for the more general creation of conditional mutations for functional genomic analysis in insects, and other organisms. Furthermore, it provides a temperature-dependent system for creating sterile male populations useful for enhancing the efficacy of biologically-based programs, such as the sterile insect technique (SIT), to control D. suzukii and other insect pest species of agricultural and medical importance.

Biologically active peptides derived from food proteins have been increasingly popular due to their therapeutic properties. This paper attempts to utilize a by-product of phospholipid extraction from egg yolk as a source of peptides with antioxidant [radical scavenging capacity, Fe2+ chelating effect, reducing power (FRAP)] and ACE-inhibitory activity. In addition, in this research we analysed the ability to release bio-peptides of a non-commercial proteases obtained from Yarrowia lipolytica yeast. Yeast serine protease exert greater ability to evaluate antioxidant and ACE inhibitory activity than yeast aspartyl protease during degradation of protein by-product. Purification procedures including membrane filtration, gel filtration chromatography and reversed-phase high-performance liquid chromatography led to obtain a decapeptide QSLVSVPGMS with strong DPPH free radical scavenging and ACE inhibitory activities. A new application of the serine protease from Y. lipolytica yeast in the production of bioactive peptides from egg yolk protein by-product was demonstrated.

Accumulation of yolk precursor protein in the oviparous egg is essential for embryo growth. Transferrin-like protein, also known as major yolk protein, is a major precursor protein in sea urchins and sea cucumbers. In sea urchins, a new yolk protein was recently detected in Strongylocentrotus intermedius and Mesocentrotus nudus eggs. This protein, tentatively named yolk-related protein (YRP), was thought to have important physiological functions for sea urchin gonadal growth and gametogenesis. To understand the relationship between YRP and vitellogenesis, we investigated the molecular structure of sea urchin YRP, quantified the transcript levels during oogenesis, and identified the presence of YRP in coelomic fluid. Using molecular cloning, we characterized one cDNA that encoded YRP (mn-yrp). Structural analysis revealed that mn-YRP is an apolipoprotein B (ApoB)-like protein that belongs to the large lipid transfer protein superfamily. Quantification of mn-yrp (mn-apob) transcripts showed that mn-apob is mainly expressed in the stomach during gonadal growth. Immunobiochemical methods using antiserum revealed that mn-ApoB was present in the coelomic fluid. These results indicate that ApoB has a role in the transport of nutrients, such as sugar, lipids, and carotenoids, from the digestive tract to eggs via coelomic fluid in sea urchin.

The objective of this study was to determine the immunomodulatory effects of egg yolk protein–water extract (EYW) on splenocyte proliferation, cytokine secretion, immunoglobulin production, and NK cell cytotoxic activity in BALB/c mice. The forced swimming test (FST) was used to provide a model for suppressing immune regulation. The proliferation of B cells in the EYW supplementation group was significantly increased from the level to which it was reduced by the FST (from 40.9% to 81.8%, p < 0.05). EYW supplementation affected cytokine secretion of splenocytes. Levels of interleukin (IL)-2 and IL-10—as Th1 and Th2 cytokines, respectively—were decreased after the FST. However, EYW supplementation showed that secretion levels of these cytokines were significantly increased to pre-FST levels (p < 0.05). The production of immunoglobulins (IgA and IgG) was increased abnormally after the FST, whereas EYW supplementation significantly decreased it to pre-FST levels (p < 0.05). EYW supplementation also improved NK cell cytotoxic activity against YAC-1 tumor cells compared to the PC group (p < 0.05). These data suggest that EYW has potential as an immunomodulatory agent in the food and/or pharmaceutical industries.

In the present study, we examined the localization of the major yolk protein (MYP) in the intestine of the sea urchin Strongylocentrotus intermedius . First, partial MYP complementary DNA was isolated from the sea urchin intestine. The expression level of MYP messenger RNA (mRNA) along the sea urchin digestive tract is highest in the intestine, so we performed in situ hybridization and immunohistochemical analysis using this tissue. No MYP mRNA was detected in the luminal epithelium, connective tissue, muscle tissue, or coelomic epithelium by in situ hybridization analysis. Positive immunohistochemical staining was observed in the luminal epithelium, inner epithelium and connective tissue, the signal being strongest in the latter. We conclude that MYP synthesized in the inner epithelial cells is moved to and stored in connective tissue and the luminal epithelium, before being secreted into the body cavity and the inner digestive cavity of the sea urchin.

A 3 x 3 treatment arrangement varying in dietary protein and TSAA:Lys was used to evaluate the effect of low-protein diets fed to Hy-Line W-98 laying hens. Phase I was 20 to 43 wk of age with 18.9, 17.0, and 14.4 g of protein/hen per day and 0.97, 0.85, and 0.82 TSAA:Lys, whereas phase II was 44 to 63 wk of age with 16.3, 14.6, and 13.8 g of protein/hen per day and 0.92, 0.82, and 0.72 TSAA:Lys. Egg production and feed consumption decreased from 83.7 to 82.2% and 98.8 to 95.6 g, respectively. Feed efficiency improved from 1.680 to 1.645 g of feed/g of egg mass with decreasing dietary protein. Body weight gain was similar for hens fed high or medium protein diets. In phase II, hens consuming 13.8 g of protein/day had significantly reduced egg weight compared with hens consuming 14.6 or 16.3 g of protein/day. Wet and dry albumen percentage, albumen solids, and albumen and yolk protein percentages were significantly decreased with feeding low-protein diets. Yolk protein percentage was increased from 14.85 to 15.11% when decreasing the ratio from 0.97 to 0.82. Hens consuming a low-protein diet produced eggs with the lowest specific gravity. An interaction was observed for protein retention during phase I, feeding 14.4 g of protein/day or a ratio of 0.97 improved protein retention by 9 and 16%, respectively. Overall, hens consuming 16.3 or 14.6 g of protein/hen per day performed similar to hens consuming 18.9 and 17.0 g of protein/hen per day during P1 and P2, respectively. Also, hens consuming diets containing 0.97 and 0.92 TSAA:Lys produced eggs with improved shell quality as compared with other ratios during P1 and P2, respectively.

Vitellogenin (Vtg), a yolk nutrient protein that is synthesized in the livers of female animals, and subsequently carried into the ovary, contributes to vitellogenesis in oviparous animals. Thus, Vtg levels are elevated during oogenesis. In contrast, Vtg proteins have been genetically lost in viviparous mammals, thus the yolk protein is not involved in their oogenesis and embryonic development. In this study, we identified Vtg protein in the livers of females during the gestation of the viviparous teleost, Xenotoca eiseni. Although vitellogenesis is arrested during gestation, biochemical assays revealed that Vtg protein was present in ovarian tissues and lumen fluid. The Vtg protein was also detected in the trophotaeniae of the intraovarian embryo. Immunoelectron microscopy revealed that Vtg protein is absorbed into intracellular vesicles in the epithelial cells of the trophotaeniae. Furthermore, extraneous Vtg protein injected into the abdominal cavity of a pregnant female was subsequently detected in the trophotaeniae of the intraovarian embryo. Our data suggest that the yolk protein is one of the matrotrophic factors supplied fromthe mother to the intraovarian embryo during gestation in X. eiseni.

Vitellogenesis is pre-requisite to insect egg production and embryonic development after oviposition. During insect vitellogenesis, the yolk protein precursor vitellogenin (Vg) is mainly synthesized in the fat body, transported by the hemolymph through the intercellular spaces (known as patency) in the follicular epithelium to reach the membrane of maturing oocytes, and sequestered into the maturing oocytes via receptor-mediated endocytosis. Insect vitellogenesis is governed by two critical hormones, the sesquiterpenoid juvenile hormone (JH) and the ecdysteriod 20-hydroxyecdysone (20E). JH acts as the principal gonadotropic hormone to stimulate vitellogenesis in basal hemimetabolous and most holometabolous insects. 20E is critical for vitellogenesis in some hymenopterans, lepidopterans and dipterans. Furthermore, microRNA (miRNA) and nutritional (amino acid/Target of Rapamycin and insulin) pathways interplay with JH and 20E signaling cascades to control insect vitellogenesis. Revealing the regulatory mechanisms underlying insect vitellogenesis is critical for understanding insect reproduction and helpful for developing new strategies of insect pest control. Here, we outline the recent research progress in the molecular action of gonadotropic JH and 20E along with the role of miRNA and nutritional sensor in regulating insect vitellogenesis. We highlight the advancements in the regulatory mechanisms of insect vitellogenesis by the coordination of hormone, miRNA and nutritional signaling pathways.

The biodiversity of useful organisms, e.g., insects, decreases due to many environmental factors and increasing anthropopressure. Multifunctional tissues, such as the fat body, are key elements in the proper functioning of invertebrate organisms and resistance factors. The fat body is the center of metabolism, integrating signals, controlling molting and metamorphosis, and synthesizing hormones that control the functioning of the whole body and the synthesis of immune system proteins. In fat body cells, lipids, carbohydrates and proteins are the substrates and products of many pathways that can be used for energy production, accumulate as reserves, and mobilize at the appropriate stage of life (diapause, metamorphosis, flight), determining the survival of an individual. The fat body is the main tissue responsible for innate and acquired humoral immunity. The tissue produces bactericidal proteins and polypeptides, i.e., lysozyme. The fat body is also important in the early stages of an insect’s life due to the production of vitellogenin, the yolk protein needed for the development of oocytes. Although a lot of information is available on its structure and biochemistry, the fat body is an interesting research topic on which much is still to be discovered.