Low Molecular Peptides Research Articles

Protective Effect of Tuna Bioactive Peptide on Dextran Sulfate Sodium-Induced Colitis in Mice.

Bioactive peptides isolated from marine organisms have shown to have potential anti-inflammatory effects. This study aimed to investigate the intestinal protection effect of low molecular peptides (Mw < 1 kDa) produced through enzymatic hydrolysis of tuna processing waste (tuna bioactive peptides (TBP)) on dextran sulfate sodium (DSS)-induced ulcerative colitis (UC) in BALB/c mice. Here, we randomly divided twenty-four male BALB/c mice into four groups: (i) normal (untreated), (ii) DSS-induced model colitis, (iii) low dose TBP+DSS-treated (200 mg/kg/d), and (iv) high dose TBP+DSS-treated groups (500 mg/kg/d). The results showed that TBP significantly reduced mice weight loss and improved morphological and pathological characteristics of colon tissues. In addition, it increased the activities of antioxidant enzymes (SOD and GSH-Px) and decreased inflammatory factors (LPS, IL-6, and TNF-α) expression. TBP increased the gene expression levels of some tight junction (TJ) proteins. Moreover, TBP increased the short-chain fatty acids (SCFAs) levels and the diversity and imbalance of intestinal flora. Therefore, TBP plays some protective roles in the intestinal tract by enhancing antioxidant and anti-inflammatory abilities of the body, improving the intestinal barrier and metabolic abnormalities, and adjusting intestinal flora imbalance.

Amylase enhances production of low molecular weight collagen peptides from the skin of spent hen, bovine, porcine, and tilapia

Low molecular weight (LMW) collagen peptides show skin and bone health benefits for human. However, the production of LMW collagen peptides from land vertebrate sources remains challenging due to the presence of advanced glycation end products (AGEs) cross-links. In this study, the effect of α-amylase pre-treatment on proteolytic production of LMW collagen peptides by papain was investigated; spent hen, bovine, porcine, and tilapia skin collagens (HSC, BSC, PSC, and TSC, respectively) were chosen. Results showed that pre-treatment with α-amylase considerably improved the production of LMW peptides (<2 kDa) from HSC (33.79–67.66%), PSC (86.03–90.85%), BSC (6.60–28.78%), and TSC (89.92–90.27%). The HSC presented the highest carbohydrate content and was increased the most in LMW peptides after amylase pretreatment. These results suggested that α-amylase could cleave glycosidic bonds of AGEs between collagen and thus enhance the production of LMW collagen peptides.

Peptidomic analysis of low molecular weight antioxidative peptides prepared by lotus (Nelumbo nucifera Gaertn.) seed protein hydrolysates

Lotus (Nelumbo nucifera Gaertn.) seeds are rich in proteins and are considered to be a beneficial source of plant proteins. In this study, lotus seed protein hydrolysate (LSPH) was prepared using Flavourzyme and antioxidant activities were evaluated. The LSPH possessed the highest DPPH-scavenging (EC50 2.9 mg/mL), H2O2-scavenging (EC50 16.1 mg/mL), and reducing power activity (8.0 mg/mL) at 180 min of hydrolysis. After gel filtration and reverse phase HPLC purification, the low molecular weight fraction was then analyzed by Nano-LC-MS/MS. Sixteen peptides with corresponding mass from 1 to 2 kDa were identified. Peptides with hydrophobic features and acidic amino acids, Asp and Glu, are considered to contribute to overall antioxidant activities. These results show Flavourzyme hydrolysis of lotus seed protein successfully generates low molecular fragments that make them a potential nutraceutical or health promoting supplement.

Metabolomics approach based on LC-HRMS for the fast screening of iron(II)-chelating peptides in protein hydrolysates.

Production of iron-chelating peptides from protein hydrolysates requires robust and adequate screening methods to optimize their purification and subsequently valorize their potential antioxidant properties. An original methodology was developed for direct and sensitive screening of iron(II)-chelating peptides based on ion-pair reverse phase liquid chromatography (IP-RPLC) coupled to high-resolution mass spectrometry (HRMS). Peptide mixture was first added to iron(II) solution to form iron(II)-peptide complexes. Then IP-RPLC-HRMS analysis was conducted on this iron-peptide mixture and on the iron-free peptide solution for comparative mass spectra analysis. This protocol, initially applied to a range of low molecular weight standard peptides, allowed detection of [(Peptide-H)+56FeII]+ complex ion for iron(II)-chelating peptides (GGH, EAH, DAH, βAH, DMH, DTH, DSH). GGH was added in complex peptide mixtures and targeted analysis of [(GGH-H)+56FeII]+ complex showed a limit of detection (LOD) below 0.77mgL-1 of GGH. This protocol was finally tested in combination with metabolomics software and additional digital processing for non-targeted search for iron(II)-chelating peptides. Applicability of this new screening methodology has been validated by detection of GGH as iron(II)-chelating peptide when added at 0.77mgL-1 in casein hydrolysate. Graphical abstract.

Purification and identification of novel antioxidant peptides from silver carp muscle hydrolysate after simulated gastrointestinal digestion and transepithelial transport

Unregulated oxidative reactions occur in human body or food system can cause harmful effects both on food quality and human health. This study aimed to develop novel antioxidant peptides from silver carp muscle hydrolysate after simulated gastrointestinal digestion and transepithelial transport. Results showed that alcalase- and papain-induced hydrolysates had higher antioxidant activities before and after in vitro gastrointestinal digestion. Fractions with molecular weight <1 kDa from these two digestive products (named A-GID-1 and P-GID-1) exhibited the greatest antioxidant capacity, which was ascribed to the large proportion of low-molecular peptides and hydrophobic amino acids. After transepithelial transport analysis, a total of ten peptides were identified from the RP-HPLC fractions with the highest antioxidant activity from both P-GID-1 and A-GID-1 permeates. Among them, LVPVAVF exhibited the highest DPPH radical scavenging and reactive oxygen species (ROS) inhibitory activity. Our findings will provide new knowledge for the development of novel natural antioxidants and the high-value utilization of silver carp protein.

Naturally occurring low molecular peptides identified in egg white show antioxidant activity

Egg white is a rich source of bioactive proteins that are essential to provide protection to the embryo in yolk. There is an ongoing interest in identifying novel egg white proteins; it is not known however if peptides are also present in egg white. The objectives of the study were to identify low molecular peptides occurring naturally in egg white using a peptidomics approach and to determine their potential antioxidant activity. A total of 45 peptides were identified but surprisingly all are originated from egg white minor proteins (except ovotransferrin); three most abundant peptides, STDVPRDPWVWGSAHPQAQHTR, GDPSAWSWGAEAHS, and ALGEDIVDLDSFSEQH are derived from ovocleidin, zona pellucida glycoprotein C (ZPC), and sulfhydryl oxidase 1, respectively. Neuropeptide Y was identified for the first time in egg whites. The concentrations of eight most abundant peptides in egg white ranged from 0.004 to 0.292 mg/g, determined by triple quadrupole mass spectrometer in multiple-reaction monitoring (MRM) mode. Six peptides were found to have antioxidant activities based on reduced formation of superoxide and increased levels of superoxide dismutase (SOD) and catalase (CAT) in cells. Our study provided evidence on the presence of naturally occurring antioxidant peptides in egg white.

Биокаталитическая конверсия белка молочной сыворотки микроорганизмами рода Aspergillus oryx season для снижения аллергенности

Introduction. More than 170 foods can cause allergic reactions in humans. The list of potential allergens includes a lot of dairy products. To reduce the antigenic properties, dairy raw materials can be subjected to thermal treatment. However, prolonged heating reduces the nutritional value, solubility, and digestibility of the final product. Biocatalytic conversion is considered a more effective way to reduce the allergenicity of milk proteins and dairy products.&#x0D; Study objects and methods. The research featured the bioconversion process of milk whey using an enzyme complex of fungal protease and exo-peptidase produced by Aspergillus oryx season. The research provided an optimal concentration of the enzyme preparation, as well as temperature parameters, reaction time, and the effect of pH on the intensity of the process. The experiment involved standard research methods. The mass fraction of free amino acids was determined by distribution chromatography after protein hydrolysis.&#x0D; Results and discussion. The research helped to define the effect of enzymatic treatment time and the pH on the hydrolysis of serum proteins after bioconversion. The indicator of the degree of hydrolysis and its time was affected by the concentration of the introduced enzyme preparation. The maximum degree of hydrolysis was observed at pH = 4.0 ± 0.1 with an enzyme-substrate ratio of 1:700. The degree of hydrolysis in samples with an enzyme-substrate ratio of 1:1,000 and 1:700 was almost the same. Therefore, the enzymesubstrate ratio of 1:1,000 proved more effective. The concentration of many important amino acids increased, which indicated the hydrolytic cleavage of the protein. The research made it possible to determine the most effective parameters of the process of biocatalytic conversion of whey enzyme by the protease complex Aspergillus oryx season: the ratio of enzyme-substrate – 1:1,000, time – 60–90 min, pH – 4.0 ± 0.1, temperature – 35–45°C.&#x0D; Conclusion. The whey samples subjected to biocatalytic conversion by an enzyme complex of the genus Aspergillus oryx season showed the presence of low-molecular peptides in its composition, which indicated the effectiveness of the process and reducing the allergenicity of the whey protein.

Structure and stability of low molecular weight collagen peptide (prepared from white carp skin) -calcium complex

The low molecular weight (≤3 kDa) collagen peptide (CPLW) was prepared from white carp skin by intestinal simulation digested and ultrafiltration membranes. CPLW and calcium ions were combined to form a peptide-calcium complex (CPLW-Ca), and the structure and stability of the complex were characterized. The single factor optimization results indicated that the highest protein conversion rate and the maximum calcium binding ability were 60%, and 22.16 ± 0.55 mg/g, respectively. Structural analysis demonstrated that calcium ions bound to CPLW mainly via the formation of ionic bonds with carboxyl oxygen, hydroxyl oxygen and amino nitrogen atom of CPLW. The CD and particle size analyses showed that after CPLW was combined with calcium ions, the spatial structure was folded, which reduced the particle size with the formation of irregular nanoparticles. Stability analysis revealed that the calcium retention rate of the prepared CPLW-Ca remained substantially at 90% below 90 °C, and the calcium content of CPLW-Ca was significantly decreased under high acidic conditions. CPLW-Ca has the potential to be applied as an alternative for dietary calcium supplements.

Asymmetric Catalysis Mediated by Synthetic Peptides, Version 2.0: Expansion of Scope and Mechanisms.

Low molecular weight synthetic peptides have been demonstrated to be effective catalysts for an increasingly wide array of asymmetric transformations. In many cases, these peptide-based catalysts have enabled novel multifunctional substrate activation modes and unprecedented selectivity manifolds. These features, along with their ease of preparation, modular and tunable structures, and often biomimetic attributes make peptides well-suited as chiral catalysts and of broad interest. Many examples of peptide-catalyzed asymmetric reactions have appeared in the literature since the last survey of this broad field in Chemical Reviews (Chem. Rev. 2007, 107, 5759-5812). The overarching goal of this new Review is to provide a comprehensive account of the numerous advances in the field. As a corollary to this goal, we survey the many different types of catalytic reactions, ranging from acylation to C-C bond formation, in which peptides have been successfully employed. In so doing, we devote significant discussion to the structural and mechanistic aspects of these reactions that are perhaps specific to peptide-based catalysts and their interactions with substrates and/or reagents.

Canned Products Based on Animal Hearts as Collagen and Ferrum Sources

To activate the elastic tissues regeneration, a man needs to receive at least 5 g of such amino acids as proline and oxyproline, which are involved in the process of the body’s own collagen production, with food every day. The source of collagen can be products made from the hearts of farm animals. High temperature influence destroys collagen, and there is an accumulation of low-molecular peptides that are available to the human body. The article presents the results on the development of new types of canned food based on the farm animal hearts and plant raw materials. The animal hearts are high-protein raw materials in terms of protein content. The fat content does not exceed 3.7 ± 0.5 %, which results in a lower energy value compared to muscle tissue. Proteins in animal hearts are balanced in terms of amino acid composition; the content of collagen in them is 4.8–4.5 %, which is significantly higher than its amount in muscle tissue proteins. The researchers developed technology and recipes of canned food based on animal hearts and vegetable raw materials. The mass fraction of hearts in canned food recipes is 60.0–65.0 %. The additional components were beans and vegetables. Developed canned food made on the basis of animal hearts and vegetable raw materials had high organoleptic characteristics: protein content was 10.7–12.6 %; fat – 7.6–9.1 %. 100 g of canned food contains 0.85 ± ± 0.5 g of collagen-forming amino acids, which allows the human body to provide 16.5 ± ± 0.5 % of the daily need for them. Canned food is an additional source of iron (the content of which is 2.9 ± 0.3 g/100 g). A man recommends canned foods based on animal hearts and vegetable raw materials as specialized products for dietary and preventive nutrition of people of older age groups and persons with reduced processes of elastic tissue regeneration.

Multidimensional separation schemes enhance the identification and molecular characterization of low molecular weight proteomes and short open reading frame-encoded peptides in top-down proteomics

Short open reading frame-encoded peptides (SEP) represent a widely undiscovered part of the proteome. The detailed analysis of SEP has, despite inherent limitations such as incomplete sequence coverage, challenges encountered with protein inference, the identification of posttranslational modifications and the assignment of potential N- and C-terminal truncations, predominantly been assessed using bottom-up proteomic workflows. The use of top-down based proteomic workflows is capable of providing an unparalleled level of characterization information, which is of increased importance in the case of alternatively encoded protein products. However, top-down based analysis is not without its own limitations, for which efficient separation prior to MS analysis is a major issue.We established a sample preparation approach for the combined bottom-up and top-down proteomic analysis of SEP. Key improvements were made by the application of solid phase extraction (SPE), which supported enrichment of proteins below ca. 20 kDa, followed by 2D-LC-MS top-down analysis encompassing both HCD and EThcD ion activation. Bottom-up experiments were used to support and confirm top-down data interpretation. This strategy allowed for the top-down characterization of 36 proteoforms mapping to 12 SEP from the archaeon Methanosarcina mazei strain Gö1, with the concurrent detection and identification of several posttranslational modifications in SEP. Biological significanceSmall or short open reading frames (sORF) have been widely neglected in genome research in the past. With their increasing discovery, the question about the presence and molecular function of their translation products, the short open reading frame-encoded peptides (SEP), arises. As these small proteins are usually below the 10 kDa range, the number of peptides identifiable by bottom-up proteomics is limited which hampers both the identification and the recognition of potential posttranslational modifications. The presented top-down approach allowed for the detection of full length SEP, as well as of terminally truncated proteoforms, and further enabled the identification of disulfide bonds in these small proteins. This demonstrates, that this yet widely undiscovered part of the proteome undergoes the same modifications as classical proteins which is an essential step for future understanding of the biological functions of these molecules.

Identification and analysis of small proteins and short open reading frame encoded peptides in Hep3B cell

The small proteins and short open reading frames encoded peptides (SEPs) are of fundamental importance because of their essential roles in biological processes. However, the annotation or identification of them is challenging, in part owing to the limitation of the traditional genome annotation pipeline and their inherent characteristics of low abundance and low molecular weight. To discover and characterize SEPs in Hep3B cell line, we developed an optimized peptidomic assay by combining different peptide extraction and separation methods. The organic solvent precipitation method in peptidomic showed promotion in the enrichment of low molecular proteins or peptides, and the data clearly showed a beneficial effect from the reduction of sample complexity, resulting in high-quality MS/MS spectra. Furthermore, different strategies exhibited good complementarity in improving the total amount of small proteins and their sequence coverage. In total, 1192 proteins within less than 100 amino acids were identified, including 271 newly discovered SEPs that been annotated in the OpenProt database and 147 SEPs of them encoded from ncRNA or lincRNA. Results in this work provide robust evidence to date that the human proteome is more complicated than previously appreciated, and this will be a benefit to discoveries of proteins without function annotation. SignificanceIn this work, methods were optimized to identify SEPs in Hep3B. The organic solvent precipitation presents promotion in enrichment of low molecular proteins or peptides, and the data clearly showed a beneficial effect from the reduction of sample complexity, resulting in high quality MS/MS spectra. Different strategies exhibited good complementarity in improving total amount of small proteins and their sequence coverage. In total, 1192 proteins within less than 100 amino acids were identified, including 271 newly discovered SEPs that been annotated in the OpenProt database and 147 SEPs of them encoded from ncRNA or lincRNA. Furthermore, 22 SEPs generated from the uORF may has potential effect in translation control, and 149 newly identified SEPs have known functional domains or cross-species conservation. Results in this work present robust evidence for the coding potential of the ignored region of human genomes and may provide additional insights into tumor biology.

The First Human Clinical Trial on the Skin Depigmentation Efficacy of Glycinamide Hydrochloride

A previous study identified certain low molecular anti-melanogenic peptides that share a common sequence with α-melanocyte stimulating hormone (MSH) and end with a glycinamide moiety. Glycinamide itself also showed anti-melanogenic activity in cell-based assays, but neither glycine nor acetyl glycinamide were active, which indicated a special structure and activity relationship. The aim of this study was to examine the skin depigmentation efficacy of glycinamide hydrochloride in human subjects. The primary skin irritation potential of glycinamide hydrochloride was evaluated by patch testing in 30 human subjects. The skin depigmentation efficacy of glycinamide hydrochloride was evaluated in a double-blinded clinical test in 21 human subjects. The test product and a control product were applied to designated sites on the right or left side of the face twice daily for eight weeks. Skin color parameters, i.e., the melanin index, the L* value (representing skin lightness), a* value (redness), and b* value (yellowness) were measured using instruments. The individual topology angle (ITAo, representing skin color) was calculated from L* and b values. The degree of skin pigmentation was visually assessed by two testers. The primary skin irritation test showed that a solution containing glycinamide hydrochloride up to 10% did not induce any adverse skin responses. In the efficacy test, the test product significantly reduced the melanin index, and increased L* value and ITAo after two weeks of application relative to the baseline value at the start of the test. It also significantly lowered the degree of pigmentation after 6 weeks of application, relative to the baseline value. Differences in the melanin index, L* value, ITAo and the degree of pigmentation between the test and control groups became statistically significant after six weeks or eight weeks of application. No signs of skin irritation were observed during the efficacy test. The present study suggests that glycinamide hydrochloride has great potential to be used in the control of skin hyperpigmentation.

The use of enzymatic modification in recycling of meat and bone collagen-containing byproducts

The objective of this research was to study the process of extraction of valuable protein watersoluble substances from highly mineralized meat and bone raw materials during hydrolysis by proteolytic enzymes. The experiments were carried out on beef tubular and costal bones using enzymes Alcalase 2.5 L, Protamex, Protosubtilin G3x. The efficiency of protein hydrolysis was evaluated by the accumulation of nonprotein amino nitrogen in the aqueous protein extract, the amount of which was determined by formol titration. The chemical composition of raw materials and hydrolysis products was evaluated by standard physicochemical methods. The drying of hydrolyzed protein fractions was carried out on a lyophilic freeze dryer at a condenser temperature of -55 ° C. Drying of the sedimentary protein-mineral fraction was carried out by convection method at 60 about C. The general chemical composition of raw materials and protein hydrolysates is established. It was shown that fermentolysis in an aqueous medium with preliminary separation of fat and subsequent separation of fractions makes it possible to obtain low molecular weight water-soluble peptides and protein-mineral insoluble compositions, as well as fat products in the amount of 13.3–14.4 % of raw materials by weight. The yield of proteins by the content of solid products in water-soluble freeze-dried products was 6.1–7.9 %, depending on the type of enzyme and hydrolysis conditions. The bulk of the raw material's protein mass is precipitated together with mineral substances during fermentolysis. The solids content in dense sediments was 66.5–73.8 %. It is recommended to use the fermentolysis of meat and bone raw materials for pre-treatment in subsequent high-temperature hydrolysis. Protein products obtained by enzymatic modification of meat and bone raw materials are recommended for use as part of feed supplements, microbiological media and fertilizers, as well as feed for aquaculture. To accomplish that, it is necessary to study their amino acid composition and conduct biological tests. The extracted fat may also serve as a raw material for a number of fat products (margarine, spreads, soap).

Effect of Thermal Treatment on the Physicochemical Properties of Emulsion Stabilized by Gelatin from Black Tilapia (Oreochromis mossambicus) Skin

This study investigated the influence of thermal treatment (30 °C to 110 °C, 30 min) on the physicochemical and rheological properties of an emulsion stabilized by black tilapia (Oreochromis mossambicus) skin at pH 4. The protein pattern of tilapia gelatin did not have any significant difference after the gelatin was heated within a temperature range of 30 °C to 70 °C. However, at 90 °C and 110 °C, denaturation occurred where α-, β- and γ-chains of the gelatin were degraded, leading to a concomitant increase in low molecular peptides. The emulsion stability was investigated through a particle size analyzer, zeta potential, microscopic observation and creaming index. The gelatin emulsion was physically stable at 30 °C to 70 °C with a mean droplet size of less than 13 μm. When the heating temperature was increased to 90 °C and 110 °C, the emulsion showed a pronounced increase in droplet size due to coalescence. The gelatin emulsion heated at 90 °C and 110 °C also displayed instability against creaming after storage at room temperature for 7 days. As the heating temperature increased, the gelatin emulsion exhibited a decrease in apparent viscosity and the flow behavior changed from shear thinning to Newtonian. The rheological data also showed that the storage modulus (G′) of emulsion became more frequency dependent as the heating temperature increased, indicating weak droplet interactions. The tilapia gelatin emulsion was physically unstable when subjected to thermal treatment above 70 °C. The data reported in this study provides useful insight into the formulation of acidic food emulsions that require thermal treatment.

Effect on Myogenesis and Anti-Inflammation of Mealworm (Tenebrio Molitor) Larvae Protein Hydrolysate

Abstract Objectives Sarcopenia, a loss of skeletal muscle mass and functions, becomes prevalent in older populations. Adequate dietary protein intake is one of the most effective ways to improve sarcopenia. The mealworm is an edible insect that comprises high levels of proteins and micro-nutrients. It could be used a potential protein source for enhancing muscle growth. Also, protein hydrolysate is easily digested and absorbed by the human body with greater functional properties. In investigating the prevention of sarcopenia with mealworm larvae, we optimize the hydrolysis condition of mealworm larvae protein isolate (MPI) and the effect of myogenesis and anti-inflammation of mealworm larvae protein hydrolysate (MPH). Methods The optimization of MPH by alcalase and flavorzyme was investigated based on the amount of available α-amino acids (L-Leucine) by TNBS assay and the distribution patterns of molecular weight by SDS-PAGE. ABTS radical scavenging capacity, expression of myostatin (MSTN), MSTN promoter activity, and anti-inflammatory induced by palmitate and LPS were examined. Results The hydrolysate prepared for 12 hours by adding flavourzyme after hydrolysis of the MPI with alcalase for 12 hrs under 1% substrate and 1% enzyme/substrate at 55˚C, pH 8 showed the highest available α-amino acid (22.09 mg/g) and had the largest amount of low-molecular peptides at 10 kDa or less. Antioxidant capacity was also the highest (97.8%) among the hydrolysates prepared under different conditions. In the MSTN level which negatively regulate muscle growth, MPH (0.28 MSTN/GAPDH) was lower than MPI (0.38 MSTN/GAPDH). Also, in the MSTN promoter activity, MPI (16.94 Luc/β-gal) was higher than the control while MPH (9.99 Luc/β-gal) was lower activity than the control (12.47 Luc/β-gal). MPI and MPH induced lower expression levels of IL-6, TNF-a, and IL-1b cytokines. Conclusions MPH had better capacity in myogenesis compared to MPI, particularly hydrolyzed by flavourzyme after hydrolysis of the MPI with alcalase. Also, the MPH decreased proinflammatory cytokines which increase proteolysis and muscle atrophy. These results demonstrate that MPH could be used as a source for preventing sarcopenia. Funding Sources This study was supported in part by the National Research Foundation of Korea.

Analysis of the serum peptidome associated with Toxoplasma gondii infection

Toxoplasma gondii is an obligate intracellular parasite that can cause severe disease in immunocompromised individuals and congenitally infected neonates. In order to determine whether serum peptide profile could reveal disease markers or allow determination of toxoplasmosis aggressiveness, mouse sera were collected from acutely infected, chronically infected and control subjects, and analyzed by a quantitative label-free pepdomics approach (LC-MS/MS). Six hundred and seven endogenous peptides were identified among all samples, with peptide profiling of difference that readily distinguished between acutely infected samples and other samples. Among these peptides detected in this study, 81 and 68 differentially expressed peptides (DEPs) were found in the acute and chronic infection stages, respectively. Through Gene Ontology analysis, most of the precursor proteins of these DEPs were associated with biological regulation and binding activity. These findings in this study will help in the search of peptide targets with a key role in disease diagnosis and create new opportunities for the development of better means for the prevention and control of toxoplasmosis. SignificanceToxoplasma gondii is an unicellular parasite which infects humans and a wide range of warm-blooded animals. The serum peptidome contains a large set of low molecular weight endogenous peptides derived from secretion, protease activity and PTMs. In the present study we quantified the effects of T. gondii infection on the serum peptidome to identify novel disease regulated secretory factors. We developed an optimized label-free LC-MS/MS method to analyze endogenous peptides during toxoplasmosis progression. This resulted in quantification of 607 unique peptides at both acute and chronic infection stages. Collectively, our deep peptidomic analysis of serum revealed that peptide variations were affected by disease development, and peptidomics is an ideal method for quantifying changes in circulating factors on a global scale in response to pathophysiological perturbations such as T. gondii infection.

SUBSTANTIATION OF RATIONAL PARAMETERS FOR COMPLEX PROCESSING OF SECONDARY RAW MATERIALS OF SPRAT PRODUCTION USING THE METHOD OF HIGH-TEMPERATURE HYDROLYSIS

Processing of secondary raw materials from production of canned food «Sprats in oil» is considered. Comprehensive technology is developed for producing of protein, fat, and protein-mineral food additives from the sprat waste, as smoked sprat heads, using the method of high temperature hydrolysis. Rational method of the hydrolysis is substantiated, including preliminary separation of fat in fatty raw materials and its enzymatic-thermal treatment. The optimal values of temperature and duration of hydrolysis in autoclave are determined. Balances of organic substances are calculated for the main operations. This new technology was tested for fatty (24 %) and medium fat (13 %) raw materials under the temperature of 130–160оС. The hydrolyzed organic mass was divided into fat, protein, and mineralized fractions and proteinfat emulsion. Food additives containing low molecular weight water-soluble peptides and high molecular weight insoluble proteins were extracted from the protein fraction by freeze-drying and mineral compounds were extracted from the mineral fraction by convective drying. The proteins were extracted more thoroughly, so the content of low molecular weight peptides in the freeze-dried hydrolysate of protein fraction was &gt; 80 %. The produced additives have pleasant organoleptic properties and are sanitary safe. They are tested with some seafood, with positive result. The developed technology for processing of smoked waste is economically valuable and allows to solve the problem of pollution in the fish smoking industry.

Биотехнологические аспекты получения функциональных ингредиентов на основе конверсии биомассы Saccharomyces cerevisiae 985-Т

An algorithm for the biocatalytic conversion of polymers of subcellular structures of Saccharomyces cerevisiae 985-T has been developed. It was shown that the action of enzymes on cell wall mannoproteins and (3-glucans led to deformation of their structure and the transfer of more than 50% of polysaccharides to a soluble state with the formation of 13.4% reducing carbohydrates, 1.8% amine nitrogen and 7.7% free amino acids (biological-1). Biological-2 had an increased content of total carbohydrates (32.2%) and fiber (10.5%). It was found that the combined action of the complex of proteinases and peptidases contributed to an increase in the degree of hydrolysis of subcellular structures, which was accompanied by a growth of the content of amino nitrogen by 2.7 times, free amino acids by 3.1 times, and low-molecular peptides (up to 500 Da) by 3.5 times (biological-3). The obtained biologicals were characterized by a high content of phosphorus and potassium. It was shown that the use of enzyme systems that catalyze the hydrolysis of intracellular polymers in yeast biomass allows us to obtain products with different biochemical and structural-fractional composition, which determines their properties. Saccharomyces cerevisiae, enzymes, structural-fractional composition, functional ingredients The work was carried out at the expense of the subsidy for the implementation of the State Task.

Low molecular weight self-assembling peptide-based materials for cell culture, antimicrobial, anti-inflammatory, wound healing, anticancer, drug delivery, bioimaging and 3D bioprinting applications.

In this review, we have focused on the design and development of low molecular weight self-assembling peptide-based materials for various applications including cell proliferation, tissue engineering, antibacterial, antifungal, anti-inflammatory, anticancer, wound healing, drug delivery, bioimaging and 3D bioprinting. The first part of the review describes about stimuli and various noncovalent interactions, which are the key components of various self-assembly processes for the construction of organized structures. Subsequently, the chemical functionalization of the peptides has been discussed, which is required for the designing of self-assembling peptide-based soft materials. Various low molecular weight self-assembling peptides have been discussed to explain the important structural features for the construction of defined functional nanostructures. Finally, we have discussed various examples of low molecular weight self-assembling peptide-based materials for cell culture, antimicrobial, anti-inflammatory, anticancer, wound healing, drug delivery, bioimaging and 3D bioprinting applications.