Enzymatic Protein Hydrolysates Research Articles

Gelatinization and fermentation synergy: investigating the protein digestibility, mineral bioaccessibility and microstructural transformations of black mash beans through Saccharomyces cerevisiae and Lactobacillus spp

ABSTRACT This study explored the nutritional qualities of black mash bean flour impacted by fermentation, gelatinization and their combination. Protease activity, in vitro protein digestibility (IVPD), and protein solubility were evaluated for both fermented and unfermented black mash bean flour samples. Interestingly, when compared to fermented samples and gelatinized mash bean flour (GMBF), raw mash bean flour (RMBF) showed the highest protein solubility. Due to enzymatic activity and protein hydrolysis, fermentation with Lactobacillus E14 and Saccharomyces cerevisiae MK-157 enhanced protein solubility. Prolonged fermentation timeframes were positively correlated with protease activity and IVPD, suggesting the degradation of complex proteins. The highest levels of IVPD (90.12%) and protease activity (5546.78 U/g) were detected in GMBF fermented by S. cerevisiae MK-157, indicating the impact of fermentation on protein breakdown. The Lactobacillus E14-fermented RMBF exhibited 5521.45 U/g of protease activity and 87.54% IVPD. The mineral content of the fermented samples was substantially greater than that of the unfermented GMBF. The increased calcium, magnesium, potassium, sodium, iron, zinc, and copper levels for the GMBF fermented by S. cerevisiae MK-157 indicated that fermentation facilitated the release of minerals from chelated compounds. Microscopic examination revealed higher protein quantities in the fermented flour as well as hydrolyzed and broken starch granules embedded in the protein matrix. Large mash bean proteins were shown to be proteolyzed during fermentation into smaller peptides by SDS PAGE. Storage proteins were extensively broken down during fermentation with S. cerevisiae MK-157, whereas Lactobacillus E14 displayed a more focused pattern of hydrolysis. The nutritional profile of black mash bean flour was improved by fermentation with Lactobacillus E14 and S. cerevisiae MK-157.

The Effect of Whey Protein Isolate Hydrolysate on Digestive Properties of Phytosterol.

Phytosterol (PS) is a steroid, and its bioavailability can be enhanced by interacting with protein in the C-24 hydroxyl group. The interaction between sterols and amino acid residues in proteins can be enhanced by enzymatic hydrolysis. Phytosterol and whey insulation hydrolysates (WPH1-4) fabricated by the Alcalase enzyme at different enzymatic hydrolysis times were selected as delivery systems to simulate sterol C-24 hydroxyl group interaction with protein. Increasing hydrolysis time can promote the production of β-Lg, which raises the ratio of β-turn in the secondary structure and promotes the formation of interaction between WPH and PS. The correlation coefficient between hydrogen bonds and encapsulation efficiency (EE) and bioaccessibility is 0.91 and 0.88 (P < 0.05), respectively, indicating that hydrogen bonds of two components significantly influenced the combination by concealing the hydrophobic amino acids and some residues, which improved PS EE and bioavailability by 3.03 and 2.84 times after PS was combined with the WPI hydrolysate. These findings are expected to enhance the absorption of PS and other macromolecules by protein enzymatic hydrolysis to broaden their applications for food.

Antioxidant and Anti-Inflammatory Properties of Hydrolyzed Royal Jelly Peptide in Human Dermal Fibroblasts: Implications for Skin Health and Care Applications.

Hydrolyzed royal jelly peptide (RJP) has garnered attention for its health-promoting functions. However, the potential applications of RJP in skincare have not been fully explored. In this study, we prepared RJP through the enzymatic hydrolysis of royal jelly protein with trypsin and investigated its antioxidant and anti-inflammatory properties on primary human dermal fibroblasts (HDFs). Our results demonstrate that RJP effectively inhibits oxidative damage induced by H2O2 and lipid peroxidation triggered by AAPH and t-BuOOH in HDFs. This effect may be attributed to the ability of RJP to enhance the level of glutathione and the activities of catalase and glutathione peroxidase 4, as well as its excellent iron chelating capacity. Furthermore, RJP modulates the NLRP3 inflammasome-mediated inflammatory response in HDFs, suppressing the mRNA expressions of NLRP3 and IL-1β in the primer stage induced by LPS and the release of mature IL-1β induced by ATP, monosodium urate, or nigericin in the activation stage. RJP also represses the expressions of COX2 and iNOS induced by LPS. Finally, we reveal that RJP exhibits superior antioxidant and anti-inflammatory properties over unhydrolyzed royal jelly protein. These findings suggest that RJP exerts protective effects on skin cells through antioxidative and anti-inflammatory mechanisms, indicating its promise for potential therapeutic avenues for managing oxidative stress and inflammation-related skin disorders.

From laboratory to industrial use: Understanding process variation during enzymatic protein hydrolysis with dry film fourier-transform infrared spectroscopy

Industries are continuously looking for dedicated sensor solutions for evaluating the chemical composition of products that can provide valuable insights into process control, process optimization, and product quality. A rapid and robust analytical method, Fourier-Transform Infrared (FTIR) spectroscopy, holds significant potential in this regard as it provides detailed compositional values of food nutrients. The main aim of the present study was to use dry film FTIR spectroscopy as an analytical tool to characterize products from an industrial enzymatic protein hydrolysis process and link this to understand industrial process variations. For this purpose, 463 protein hydrolysate samples were obtained from an industrial enzymatic protein hydrolysis plant. In the same period, systematic variations in process parameters such as raw material composition, enzyme type, and water addition, were performed. All samples were analyzed using dry film FTIR spectroscopy. Two subsets containing 200 and 68 hydrolysate samples were chosen for measuring average molecular weight (AMW) and collagen content respectively, providing reference data for constructing calibration models based on partial least squares regression (PLSR). The percentage of low molecular weight constituents was derived from the molecular weight distribution of size exclusion chromatograms of protein hydrolysates and also used in the modeling. Calibration models for the prediction of AMW, low molecular weight constituents, and collagen content were obtained with a good fit and lower estimation errors. Principal component analysis (PCA) of protein hydrolysates' FTIR spectra effectively differentiated process variations (enzyme types and raw materials) without extensive reference analysis. One-factor analysis of variance (ANOVA) tests was used to observe the impact of process variation on product quality. FTIR proved to be a sensitive method for liquid protein analysis and process control with a significant potential in process optimization approaches. To the authors’ knowledge, this is the first time dry film FTIR spectroscopy has been used to evaluate an industrial bioprocess with designed process variations.

Ultrasonic monitoring of enzymatic hydrolysis of proteins. 2. Relaxation effects

The paper investigates the occurrence of relaxation processes in enzymatic hydrolysis of whey proteins in phosphate buffer using high-resolution ultrasonic spectroscopy. The hydrolysis produces a frequency-dependent evolution of ultrasonic velocity and attenuation originated by the proton transfer between the terminal group of protein hydrolysates and the phosphate ions. Such frequency dependence is absent in other systems, e.g., Tris buffer. Real-time profiles of ultrasonic velocity and attenuation measured during the hydrolysis of β–lactoglobulin, α–lactalbumin and bovine serum albumin by α–chymotrypsin were employed in quantitative analysis of the relaxation mechanisms, relaxation times, determination of the proton transfer rate constants and the reaction volume. The proton transfer is characterised by the rate constant 9.4 x 107 L mol-1 s-1 and the adiabatic reaction volume 24 x 10-6 m3 mol-1. The obtained reaction volume agrees well with thermodynamic data for ionisation volumes and enthalpies of the terminal amino group and phosphate. The described methodology for estimating the relaxation contribution to ultrasonic characteristics allows for precision real-time ultrasonic measurements of the concentration of peptide bonds cleaved during protein hydrolysis in a broad range of environmental conditions.

Emulsifying property, antioxidant activity, and bitterness of soybean protein isolate hydrolysate obtained by Corolase PP under high hydrostatic pressure

Enzymatic hydrolysis of proteins can enhance their emulsifying properties and antioxidant activities. However, the problem related to the hydrolysis of proteins was the generation of the bitter taste. Recently, high hydrostatic pressure (HHP) treatment has attracted much interest and has been used in several studies on protein modification. Hence, the study aimed to investigate the effects of enzymatic hydrolysis by Corolase PP under different pressure treatments (0.1, 100, 200, and 300 MPa for 1–5 h at 50 °C) on the emulsifying property, antioxidant activity, and bitterness of soybean protein isolate hydrolysate (SPIH). As observed, the hydrolysate obtained at 200 MPa for 4 h had the highest emulsifying activity index (47.49 m2/g) and emulsifying stability index (92.98 %), and it had higher antioxidant activities (44.77 % DPPH free radical scavenging activity, 31.12 % superoxide anion radical scavenging activity, and 61.50 % copper ion chelating activity). At the same time, the enhancement of emulsion stability was related to the increase of zeta potential and the decrease of mean particle size. In addition, the hydrolysate obtained at 200 MPa for 4 h had a lower bitterness value and showed better palatability. This study has a broad application prospect in developing food ingredients and healthy foods.

Enzymatic Hydrolysis of Salmon Frame Proteins Using a Sequential Batch Operational Strategy: An Improvement in Water-Holding Capacity.

The meat industry uses phosphates to improve the water-holding capacity (WHC) of meat products, although excess phosphates can be harmful to human health. In this sense, protein hydrolysates offer an alternative with scientific evidence of improved WHCs. Salmon frames, a byproduct rich in protein, must be processed for recovery. Enzymatic technology allows these proteins to be extracted from muscle, and the sequential batch strategy significantly increases protein nitrogen extraction. This study focused on evaluating the WHC of protein hydrolysates from salmon frames obtained through double- and triple-sequential batches compared to conventional hydrolysis. Hydrolysis was carried out for 3 h at 55 °C with 13 mAU of subtilisin per gram of salmon frames. The WHC of each hydrolysate was measured as the cooking loss using concentrations that varied from 0 to 5% (w/w) in the meat matrix. Compared with those obtained through conventional hydrolysis, the hydrolysates obtained through the strategy of double- and triple-sequence batches demonstrated a 55% and 51% reduction in cooking loss, respectively, when they were applied from 1% by weight in the meat matrix. It is essential to highlight that all hydrolysates had a significantly lower cooking loss (p ≤ 0.05) than that of the positive control (sodium tripolyphosphate [STPP]) at its maximum allowable limit when applied at a concentration of 5% in the meat matrix. These results suggest that the sequential batch strategy represents a promising alternative for further improving the WHC of hydrolysates compared to conventional hydrolysis. It may serve as a viable substitute for polyphosphates.

GEN1 as a risk factor for human congenital anomalies of the kidney and urinary tract

BackgroundCongenital anomalies of the kidney and urinary tract (CAKUT) are prevalent birth defects. Although pathogenic CAKUT genes are known, they are insufficient to reveal the causes for all patients. Our previous studies indicated GEN1 as a pathogenic gene of CAKUT in mice, and this study further investigated the correlation between GEN1 and human CAKUT.MethodsIn this study, DNA from 910 individuals with CAKUT was collected; 26 GEN1 rare variants were identified, and two GEN1 (missense) variants in a non-CAKUT group were found. Mainly due to the stability results of the predicted mutant on the website, in vitro, 10 variants (eight CAKUT, two non-CAKUT) were selected to verify mutant protein stability. In addition, mainly based on the division of the mutation site located in the functional region of the GEN1 protein, 8 variants (six CAKUT, two non-CAKUT) were selected to verify enzymatic hydrolysis, and the splice variant GEN1 (c.1071 + 3(IVS10) A > G) was selected to verify shear ability. Based on the results of in vitro experiments and higher frequency, three sites with the most significant functional change were selected to build mouse models.ResultsProtein stability changed in six variants in the CAKUT group. Based on electrophoretic mobility shift assay of eight variants (six CAKUT, two non-CAKUT), the enzymatic hydrolysis and DNA-binding abilities of mutant proteins were impaired in the CAKUT group. The most serious functional damage was observed in the Gen1 variant that produced a truncated protein. A mini-gene splicing assay showed that the variant GEN1 (c.1071 + 3(IVS10) A > G) in the CAKUT group significantly affected splicing function. An abnormal exon10 was detected in the mini-gene splicing assay. Point-mutant mouse strains were constructed (Gen1: c.1068 + 3 A > G, p.R400X, and p.T105R) based on the variant frequency in the CAKUT group and functional impairment in vitro study and CAKUT phenotypes were replicated in each.ConclusionOverall, our findings indicated GEN1 as a risk factor for human CAKUT.

Characterization of Yeast Protein Hydrolysate for Potential Application as a Feed Additive.

Yeast protein can be a nutritionally suitable auxiliary protein source in livestock food. The breakdown of proteins and thereby generating high-quality peptide, typically provides nutritional benefits. Enzyme hydrolysis has been effectively uesed to generate peptides; however, studies on the potential applications of different types of enzymes to produce yeast protein hydrolysates remain limited. This study investigated the effects of endo- (alcalase and neutrase) and exotype (flavourzyme and prozyme 2000P) enzyme treatments on yeast protein. Endotype enzymes facilitate a higher hydrolysis efficiency in yeast proteins than exotype enzymes. The highest degree of hydrolysis was observed for the protein treated with neutrase, which was followed by alcalase, prozyme 2000P, and flavourzyme. Furthermore, endotype enzyme treated proteins exhibited higher solubility than their exotype counterparts. Notably, the more uniform particle size distribution was observed in endotype treated yeast protein. Moreover, compared with the original yeast protein, the enzymatic protein hydrolysates possessed a higher content of β-sheets structures, indicating their higher structural stability. Regardless of enzyme type, enzyme treated protein possessed a higher total free amino acid content including essential amino acids. Therefore, this study provides significant insights into the production of protein hydrolysates as an alternative protein material.

Potential use of yeast protein in terms of biorefinery, functionality, and sustainability in food industry.

A growing demand for sustainable, alternative protein sources that are nutrient-dense, such as microorganisms, and insects, has gradually evolved. When paired with effective processing techniques, yeast cells contain substantial substances that could supply the population's needs for food, medicine, and fuel. This review article explores the potential of yeast proteins as a sustainable and viable alternative to animal and plant-based protein sources. It highlights the various yeast protein extraction methods including both mechanical and non-mechanical methods. The application of nanoparticles is one example of the fast-evolving technology used to damage microbial cells. SiO2 or Al2O3 nanoparticles break yeast cell walls and disrupt membranes, releasing intracellular bioactive compounds. Succinylation of yeast protein during extraction can increase yeast protein extraction rate, lower RNA concentration, raise yeast protein solubility, increase amino acid content, and improve yeast protein emulsification and foaming capabilities. Combining physical and enzymatic extraction methods generates the most representative pool of mannose proteins from yeast cell walls. Ethanol or isoelectric precipitation purifies mannose proteins. Mannoproteins can be used as foamy replacement for animal-derived components like egg whites due to their emulsification, stability, and foaming capabilities. Yeast bioactive peptide was separated by ultrafiltration after enzymatic hydrolysis of yeast protein and has shown hypoglycemic, hypotensive, and oxidative action in vitro studies. Additionally, the review delves into the physicochemical properties and stability of yeast-derived peptides as well as their applications in the food industry. The article infers that yeast proteins are among the promising sources of sustainable protein, with a wide range of potential applications in the food industry.

Black Soldier Fly Larvae Grown on Hemp Fiber: Nutritional Composition and Production of Potential Bioactive Peptides

Black soldier fly larvae (BSFL) represent a way of converting organic substrates into valuable biomolecules, and are potentially exploitable as feed and food. In the present work, BSFL grown on retted hemp fiber were chemically analyzed to evaluate their nutritional profile. Chemical analysis revealed BSFL biomass to be an interesting source of proteins (40% on dry matter) rich in essential amino acids. In addition, larval biomass contained 12% fat, mainly composed of saturated fatty acids, and β-sitosterol and campesterol were found to be the most abundant among sterols. A total of 9% of the larval biomass was composed of chitin. The investigation extended to the enzymatic hydrolysis of proteins, leading to the identification of potential bioactive peptides. Peptidomics analysis coupled with in silico tools unveiled promising antioxidant, ACE-inhibitory, and DPP-IV-inhibitory properties within the protein hydrolysates. These findings revealed the potential of BSFL grown on retted hemp fiber as a source of dietary compounds as well as bioactive molecules which can be exploited as functional ingredients in the feed and food sectors.

Protein hydrolysates enhance recovery from drought stress in tomato plants: phenomic and metabolomic insights.

High-throughput phenotyping technologies together with metabolomics analysis can speed up the development of highly efficient and effective biostimulants for enhancing crop tolerance to drought stress. The aim of this study was to examine the morphophysiological and metabolic changes in tomato plants foliarly treated with two protein hydrolysates obtained by enzymatic hydrolysis of vegetal proteins from Malvaceae (PH1) or Fabaceae (PH2) in comparison with a control treatment, as well as to investigate the mechanisms involved in the enhancement of plant resistance to repeated drought stress cycles. A phenotyping device was used for daily monitoring morphophysiological traits while untargeted metabolomics analysis was carried out in leaves of the best performing treatment based on phenotypic results.Results: PH1 treatment was the most effective in enhancing plant resistance to water stress due to the better recovery of digital biomass and 3D leaf area after each water stress event while PH2 was effective in mitigating water stress only during the recovery period after the first drought stress event. Metabolomics data indicated that PH1 modified primary metabolism by increasing the concentration of dipeptides and fatty acids in comparison with untreated control, as well as secondary metabolism by regulating several compounds like phenols. In contrast, hormones and compounds involved in detoxification or signal molecules against reactive oxygen species were downregulated in comparison with untreated control. The above findings demonstrated the advantages of a combined phenomics-metabolomics approach for elucidating the relationship between metabolic and morphophysiological changes associated with a biostimulant-mediated increase of crop resistance to repeated water stress events.

Enzymatic protein hydrolysates of a residue from grape by-products industry for winemaking application: influence of the starting material and hydrolysis time

Enzymatic protein hydrolysates of a residue from grape by-products industry for winemaking application: influence of the starting material and hydrolysis time

Proteolytic Activity of Silkworm Thorn (Cudrania tricuspidata) Fruit for Enzymatic Hydrolysis of Food Proteins.

This study aimed to isolate the proteolytic fraction from the silkworm thorn fruit (Cudrania tricuspidata) through ethanol precipitation at different ratios, and to determine its proteolytic activity and optimal activity conditions. Furthermore, the hydrolysis characteristics and antioxidant activity of soy protein isolate (SPI) and whey protein concentrate (WPC) hydrolyzates obtained through the enzymatic hydrolysis of freeze-dried silkworm thorn fruit powder (SF) were evaluated. For isolation and partial purification of proteolytic fraction, the water-solubilized fraction of the silkworm thorn fruit was purified through ethanol precipitation at four different ratios of 1:1, 1:2, 1:4, and 1:6 (v/v). The protein recovery rate, caseinolytic activity, protein pattern, and optimal activity (pH, temperature, and inhibitors) of fractional ethanol precipitate obtained from the silkworm thorn fruit (ESF) were evaluated. The proteolytic fraction obtained from silkworm thorn fruit exhibited a major protein band around 65-70 kDa and showed the highest proteolytic activity at a 1:4 ratio of ethanol precipitation (p < 0.05). The optimal activity of the measured enzyme fraction was determined to be at pH 9.0 and 50 °C, and the proteolytic activity of ESF was almost inhibited by phenyl methyl sulphonyl fluoride (PMSF, 2 mM), a serine protease inhibitor. Compared to Alcalase and papain, extensively used as commercial enzymes, the silkworm thorn fruit powder was less effective in hydrolyzing SPI and WPC. Nevertheless, SPI and WPC hydrolyzates mediated with silkworm thorn fruit powder showed even better antioxidant activities than those mediated with Alcalase and papain. Thus, our results show the potential application of silkworm thorn fruit as a novel source of plant protease for producing human-grade protein hydrolyzates.

In vitro evaluation of the anti-hypertensive potential of albumin and globulin hydrolysates from cocoa bean (Theobroma cacao L. var. Forastero)

According to reports from the World Health Organization (WHO), hypertension is considered the most common cardiovascular risk factor, affecting 25 to 30% of the world's population. One of the primary causes of hypertension is angiotensin-converting enzyme-I (ACE), which plays a crucial role in regulating blood pressure through the modulation of the renin-angiotensin-aldosterone system. Consequently, there is a wide range of drugs available that can inhibit ACE. However, these drugs can cause adverse side effects such as cough, headache, skin rash, altered taste, angioedema, nausea, and allergic reactions. For this reason, there is considerable interest in obtaining ACE inhibitors from natural sources that reduce side effects and dependence on drugs. Specifically, bioactive peptides present in enzymatic protein hydrolysates have shown anti-hypertensive properties by inhibiting ACE, making them a promising alternative in the prevention and treatment of hypertension. The objective of this study was to evaluate the ACE inhibitory activity (in vitro) of enzymatic hydrolysates obtained from cocoa bean proteins (albumin and globulin), with the purpose of considering them as a natural source of potential anti-hypertensive agents. The results demonstrated that the enzymatic treatment (with alcalase) of albumin and globulin from cocoa beans is a viable bioprocess for producing hydrolysates with ACE inhibitory activity. In particular, hydrolysates and peptide fractions (&lt; 3000 Da) with greater ACE inhibitory capacity were generated from globulin, making them a suitable choice for designing functional foods.

Formulation and organoleptic characteristics of flavor enhancer from shrimp head protein hydrolysate

Protein hydrolysate can be produced from by-products of the fishing industry, such as shrimp heads. This product is made by enzyme hydrolysis through the breakdown of shrimp head protein into short-chain peptides and amino acids. Enzymatic hydrolysis produces protein hydrolysate, which has savory, umami, and water-soluble characteristics. The savory and umami taste results from the high content of glutamic acid and other free amino acids. This study aimed to determine the best formulation and organoleptic characteristics of the shrimp head protein hydrolysate flavor enhancer. Production of shrimp head protein hydrolysate (SPH) using alkalase enzyme at a temperature of 55°C with an enzyme concentration of 20,000 units/kg substrate for 7 hrs. Parameters tested were yield, proximate and amino acid analysis, and organoleptic test for SPH flavor enhancer. SPH has an amino acid composition dominated by arginine, alanine, glycine, glutamic acid, leucine and lysine. The flavor enhancer with 40% SPH composition was chosen as the best formula because it has sensory characteristics close to P0 commercial flavoring. The dominant sensory attributes were spicy, salty, umami and sweet. Overall, protein hydrolysate-based flavor enhancers' solubility and color properties are close to commercial flavor enhancers. The flavor enhancer made from SPH has the potential to be used as a substitute for commercial flavor enhancers which are rich in essential amino acids.

Study on the structure–activity relationship of rice immunopeptides based on molecular docking

Research on food-derived immunoregulatory peptides has attracted increasing attention of scientists worldwide. However, the structure–activity relationship of rice immunopeptides was not clearly. Herein, 114 rice immunopeptides were obtained by simulating the enzymatic hydrolysis of rice proteins and were further analyzed by NetMHCIipan-4.0. Subsequently, the molecular docking was used to simulate the binding of immunoreactive peptides to major histocompatibility complex class II (MHC-II) molecules. Results show that S, R, D, E, and T amino acid could easily form hydrogen bonds with MHC-II molecules, thus enhancing innate and adaptive immunity. Finally, glucose-modified rice immunopeptides were to investigate the binding of the peptides with MHC-II molecules after glycosylation modification; this provided a theoretical basis for the targeted modification of the generated immunopeptides. All in all, the present study provides a theoretical foundation to further utilize rice processing byproducts and other food products to enhance immunity.

Amino acid and protein specificity of protein fatty acylation in Caenorhabditis elegans

Protein lipidation plays critical roles in regulating protein function and localization. However, the chemical diversity and specificity of fatty acyl group utilization have not been investigated using untargeted approaches, and it is unclear to what extent structures and biosynthetic origins of S-acyl moieties differ from N- and O-fatty acylation. Here, we show that fatty acylation patterns in Caenorhabditis elegans differ markedly between different amino acid residues. Hydroxylamine capture revealed predominant cysteine S-acylation with 15-methylhexadecanoic acid (isoC17:0), a monomethyl branched-chain fatty acid (mmBCFA) derived from endogenous leucine catabolism. In contrast, enzymatic protein hydrolysis showed that N-terminal glycine was acylated almost exclusively with straight-chain myristic acid, whereas lysine was acylated preferentially with two different mmBCFAs and serine was acylated promiscuously with a broad range of fatty acids, including eicosapentaenoic acid. Global profiling of fatty acylated proteins using a set of click chemistry-capable alkyne probes for branched- and straight-chain fatty acids uncovered 1,013 S-acylated proteins and 510 hydroxylamine-resistant N- or O-acylated proteins. Subsets of S-acylated proteins were labeled almost exclusively by either a branched-chain or a straight-chain probe, demonstrating acylation specificity at the protein level. Acylation specificity was confirmed for selected examples, including the S-acyltransferase DHHC-10. Last, homology searches for the identified acylated proteins revealed a high degree of conservation of acylation site patterns across metazoa. Our results show that protein fatty acylation patterns integrate distinct branches of lipid metabolism in a residue- and protein-specific manner, providing a basis for mechanistic studies at both the amino acid and protein levels.

Amino Acids Biostimulants and Protein Hydrolysates in Agricultural Sciences.

The effects of different types of biostimulants on crops include improving the visual quality of the final products, stimulating the immune systems of plants, inducing the biosynthesis of plant defensive biomolecules, removing heavy metals from contaminated soil, improving crop performance, reducing leaching, improving root development and seed germination, inducing tolerance to abiotic and biotic stressors, promoting crop establishment and increasing nutrient-use efficiency. Protein hydrolysates are mixtures of polypeptides and free amino acids resulting from enzymatic and chemical hydrolysis of agro-industrial protein by-products obtained from animal or plant origins, and they are able to alleviate environmental stress effects, improve growth, and promote crop productivity. Amino acids involve various advantages such as increased yield and yield components, increased nutrient assimilation and stress tolerance, and improved yield components and quality characteristics. They are generally achieved through chemical or enzymatic protein hydrolysis, with significant capabilities to influence the synthesis and activity of some enzymes, gene expression, and redox-homeostasis. Increased yield, yield components, and crop quality; improved and regulated oxidation-reduction process, photosynthesis, and physiological activities; decreased negative effects of toxic components; and improved anti-fungal activities of plants are just some of the more important benefits of the application of phenols and phenolic biostimulants. The aim of this manuscript is to survey the impacts of amino acids, different types of protein hydrolysates, phenols, and phenolic biostimulants on different plants by presenting case studies and successful paradigms in several horticultural and agricultural crops.

Effect of hydrolysis degree with Alcalase on antioxidant and antigenic properties of whey and colostrum protein hydrolysates

Enzymatic hydrolysis of dairy proteins is aimed to increase their nutritional value and reduce their allergenic properties. It is relevant to study the effects of enzymatic hydrolysis with highly active endopeptidase alсalase on the bioactivity of the whey and colostrum protein components. Dairy hydrolysates with various degree of Alcalase treatment were obtained in the present study. A comparative analysis of cleaved dairy proteins and their peptide fractions with a 5 and 10 kDa cutoff was performed. The protein and peptide composition of hydrolysates was determined using various techniques. The bioactivity of hydrolyzed whey and colostrum samples were estimated. The antioxidant activity of hydrolyzed and fractionated (5 kDa cutoff) whey samples increased by 5.91/6.62-fold and that of colostrum by 14.22/7.24-fold in fluorimetric/spectrophotometric assay, respectively. A significant decrease in the antigenic potential of milk peptides was observed with increasing degree of hydrolysis and subsequent ultrafiltration. Thus, bioactive dairy protein hydrolysates were obtained, which are applicable as a component of specialized foods with proven hypoallergenic properties and high antioxidant activity.