Trypsin Inhibitor Activity Research Articles

CENTIPEDE VENOM TOXINS AND ITS BIOMEDICAL AND PHARMACOLOGICAL PROPERTIES

The present review article explains venoms from various centipede species with their biomedical and pharmacological properties. Centipede venom is a natural source of bioactive proteins, peptides and other small molecules. These use venoms as defense arsenals to paralyze prey. This review paper sketch out important physiological effects like platelet aggregation, anticoagulant, phospholipase A2 and trypsin inhibiting activity. Centipede venom toxins selectively bind Kv2.1 channel and block them. Centipede venom disrupts cardiovascular, respiratory, muscular and nervous systems by targeting the broadly distributed KCNQ channels. It also signifies toxin-voltage-gated integrations and its inhibition. These peptides can be used for developing drugs for treatments as well as bio-insecticides for insect control.

Immunohistological visualization of the effect of soybean processing on Kunitz trypsin inhibitor

Anti-nutritional factors such as trypsin inhibitors represent a major hindrance in the usage of soybean-based products as feed for non-ruminant feedstock. Here we studied the effect of four different methods of soybean processing to generate soybean meal (oil-extraction with a solvent, toasting, mechanical extraction, and fermentation) on the Kunitz trypsin inhibitor and soy protein. We visualized both proteins in situ using indirect immunofluorescence on resin sections with specific rabbit-raised polyclonal antibodies and laser-scanning confocal microscopy We characterized their cellular localization in raw soybeans and show that Kunitz trypsin inhibitor and soy protein occupy different domains related to protein globoids. Semi-quantification of the signal intensities showed an only moderate reduction in detectable Kunitz trypsin inhibitor epitopes after any type of processing. On the other hand, a considerable loss of trypsin inhibitor activity was shown with a standardized assay. The effect of toasting can be seen as significantly increased green fluorescence possibly due to the production of advanced glycosylation end products. This work introduces antibody-based in situ visualization as a new promising way to study anti-nutritional factors in soybean-derived products.

Стимулювання системи протеїназа-інгібітор протеїназ у результаті імерсійної гіпотермії

The effect of immersion hypothermia (IН) on proteolysis activity in adult male rats, which was performed at 0 °C for 5 min in the “forced swimming” test, studied; the body temperature decreased to 27.5 ± 0.5°C. In blood serum and non-nuclear fractions of homogenates of cerebral cortex, hypothalamus, cerebellum, brainstem, lungs, heart, liver and kidneys tissues were determined the total proteinase activity (TPA), non-trypsin-like proteinases (NTPs), such as chymase, prostate-specific antigen, partially tonin, kallikrein rK9, as well as trypsin-inhibitory activity of α-1-proteinase inhibitor (α-1-PI), α-2-macroglobulin (α-2-MG) by highly sensitive (10-9–10-10 g) enzymatic methods. It is noted that IH led to the TPA increase in all studied tissues (4-84 times), which corresponds to the psycho-emotional effects and the phenomenon of hormesis. After 24 h, TPA decreased, remaining above the control level, and in the kidneys increased further (90 times). NTLP activity as a result of IH increased in blood serum and cerebellum, decreased in the hypothalamus, and after 24 h increased further in serum (7 times), cerebellum, and heart. The activity of α-1-PI also increased in the brainstem, lungs, heart and kidneys, and decreased after 24 h in serum below the control level, and in the brainstem remained high, protecting against proteolytic attack. The activity of α-2-MG increased in the hypothalamus, heart, and cerebral cortex, maximum in the brainstem (2-5 times), and after 24 h - more significantly (24 times), but there were no changes in the cerebellum, where its initial level is the biggest. Thus, the development of IG as a result of swimming in cold water for 5 min at 0oC has a stimulating effect on the body and leads to a significant activation of the reactions of limited proteolysis.

LIGHT INTENSITY AND ACTIVITY OF TRYPSIN INHIBITORS IN AMARANTH LEAVES AND SEEDS

The effect of exposing Amaranthus hypochondriacus plants to different levels of photosynthetic photon flux densities (PPFD) duringdevelopment was analyzed in this work. Mature plants exposed to full sunlight (38.8 mol m-2 d-1) had higher instantaneous rates of net CO2 uptake (An), reducing sugars content and thicker leaves, but lower chlorophyll content and leaf number per plant than those developed under reduced levels of PPFD (19.4 and 12.8 mol m-2 d-1). A physiological response to varying levels of PPFD was the differential accumulation of trypsin inhibitors in leaves and seeds. Leaves from plants grown under full sunlight conditions, showed a significantly higher trypsin inhibitor activity than leaves from plants partially shaded with plastic nets. In contrast, seeds collected from plants fully exposed to sunlight, showed the lowest level of trypsin inhibitors and higher rates of germination than seeds produced by plants exposed to the lowest level of sunlight. The capacity of A. hypochondriacus to adjust its morphology and physiology in response to light indicates ecological plasticity that might be helpful to face both biotic and abiotic stresses during their development.

Trypsin-inhibitor activity in colostrum - an overview

The crucial role of colostrum for the neonatal immune system is well recognized. Following ingestion, proteins and especially immunoglobulins must pass the gastrointestinal tract and its proteolytic enzymes intact in order to be absorbed into the neonatal blood circulation. For this reason colostrum exhibits trypsin-inhibitor activity. This activity is not exerted by a single molecule but represents a general characteristic of the first colostrum. In artiodactyl species, high-level trypsin inhibition has been demonstrated along with a rapid decrease during the first days of lactation. In equine colostrum, trypsin-inhibitor activity has also been detected. Its importance is however controversially discussed in the literature due to the fact that the anti-trypsin activity is less pronounced in comparison to artiodactyl species and exhibits reduced stability in acidic environment. In the colostrum of carnivores, anti-trypsin activity has also been proven, this however is less prominent than in ungulates. The presented overview of the literature aims at summarizing the current understanding of trypsin inhibition in the colostrum of different species.

A superior approach for production of protein isolates from de‐oiled soy meal and its comparison with conventional method

SummaryProtein isolates were prepared from de‐oiled soy meal by a superior approach, i.e. biological precipitation using two lactic acid bacterial strains and a conventional acid precipitation method. The isolates were characterised for physico‐chemical, functional, anti‐nutritional and structural properties and compared with isolates prepared using the conventional method. The purity, yield, lightness, whiteness index and degree of hydrolysis were higher (P ≤ 0.05) for biologically precipitated soy protein isolates (BPSPIs). The functional properties of BPSPI samples were also superior. BPSPIs showed 1.85 mg g−1 and 1.44 TIU mL−1, whereas acid‐precipitated soy protein isolates (APSPIs) showed 3.65 mg g−1 and 3.16 TIU mL−1 of phytic acid and trypsin inhibition activity respectively. A sharp bend in the wavelength ranges from 3700 to 3900 cm−1 was observed in BPSPI samples, which depicts structural changes owing to fermentation by lactic acid bacteria. Two characteristic peaks at 2Ɵ = 20° and 2Ɵ = 15° were observed in both the samples; however, intensity and crystallinity were higher in BPSPIs. Hexagonal‐shaped particles of different sizes were displayed by field emission scanning electron microscopy images. The results thus confirm that the soy protein samples prepared through the biological precipitation process had better properties over conventionally prepared soy protein samples, which can be further used as novel ingredients in protein‐based functional products.

Nutritional composition, bioactivity, starch characteristics, thermal and microstructural properties of germinated pigeon pea flour

There is an increase in the use of adoptable bioprocessing methods for the development of high-quality pulse ingredients. This study investigated the nutritional composition, physicochemical, bioactivity, in vitro digestibility, functional, pasting, thermal and colour characteristics of germinated (24–72 h) pigeon pea. Germination increased (p ≤ 0.05) protein, dietary fiber, calcium, iron, zinc, vitamins B, vitamin C (1.25–8.46 mg/100 g), resistant starch, protein digestibility (72.30–82.66 g/100 g), total phenolic content, antioxidant activities and most amino acids. Phytic acid, tannin and trypsin inhibitor activity decreased significantly during germination. Germination also increased water absorption capacity, protein solubility, foaming capacity, emulsion stability and activity of the flours while bulk density decreased. Functional, pasting, thermal and color, properties of pigeon pea was modified following germination. This study demonstrated that short-term germination is a natural means for the development of functional pigeon pea flour to promote its application in the food industry.

Physical Treatment Reduces Trypsin Inhibitor Activity and Modifies Chemical Composition of Marama Bean (Tylosema esculentum).

The utility of the marama bean (MB) as an alternative protein source to soybean (SB) can be limited by the high concentration of trypsin inhibitors (TI). The physical treatment of MB has the potential to ameliorate the antinutritional activities of TI and modify other chemical components. Thus, this study investigated the effects of physical treatments on the chemical components and trypsin inhibitor activity (TIA) of raw MB and SB. The bean substrates were subjected to each of the following treatment methods: (1) room temperature (20–22 °C) soaking for 24 h; (2) electric stove cooking at 100 °C for 10, 20, and 30 min; (3) steam autoclaving at a temperature of 110 °C and pressure of 7 pounds per square inch (psi), as well as a temperature of 121 °C and 7 psi for 5, 15, and 30 min; (4) pre-soaked autoclaving at 110 °C (7 psi) and 121 °C (17 psi) for 5, 15, and 30 min. Treated MB and SB had greater (p < 0.05) crude protein content than untreated samples. All the treatments (except 24 h soaking of MB) reduced (p < 0.05) the TIA and ash content. Marama and SB are similar in protein content, but their amino acids profile and TIA are quite different. Soaking for 24 h was less effective in reducing TIA in MB and SB, compared to the thermal methods, and it was detrimental to the ash and amino acids profile of the two beans. Soaking prior to autoclaving yielded beans with the lowest TI concentrations. In conclusion, thermal methods reduced the TI contents and modified the level of proximate components and amino acids profile of the beans.

Nutritional prospective of Sesbania species: an underutilized wild legume from Northern Western Ghats, Maharashtra, India

Nutrition plays very important role in longevity of life. Processed food has created various health disorders at a very alarming rate. Wild genotypes have potent nutritive characteristics which are relatively less explored. In the current investigation, two species of Sesbania were evaluated for their potent nutritional value. Sesbania grandiflora and Sesbania bispinosa seeds contained 37.78% and 30.2% crude proteins, 4.24% and 2.06% albumins, 7.20% and 5.16% globulins, 1.75% and 8.34% free amino acids, 34.91% and 59.08% total carbohydrates and 5.2% and 5.02% total lipids respectively. DPPH Radical scavenging assay revealed notable antioxidant potential with 62.27% and 65.45% inhibition respectively. Antinutrient analysis indicated the presence of total free phenols (0.29% and 0.63%), tannins (0.28% and 0.34%), phytic acid (1.70% and 1.59%) and trypsin inhibitor activity (41.8 and 54.4 TIU/mg) respectively. Both Sesbania species had excellent nutritional potential as well as antioxidant activity and a low antinutrient profile. Based on the findings, Sesbania species may be investigated further as a potential alternative food source in the near future, particularly in economically disadvantaged areas, and may pave the way toward the wider aim of food security.

Evaluation of interaction between Ponceau 4R (P4R) and trypsin using kinetic, spectroscopic, and molecular dynamics simulation methods

Azo-dyes, a diverse group of synthetic dyes, are commonly used for coloring food products. However, these dyes are persistent in nature with the potential to cause harmful effects on the human body. Hence, it seems that studies are required about the effects of azo dyes on the structure and function of biomacromolecules. Ponceau 4R (P4R) is an azo-dye found in foods, beverages, and pharmaceuticals, but its potential risk on gastrointestinal enzymes such as trypsin is poorly characterized. Thus, this study focused on analyzing the binding behavior between trypsin and P4R by spectroscopic, kinetic, and theoretical methods. Intrinsic fluorescence revealed that there was an interaction between P4R and trypsin, and P4R could quench the trypsin fluorescence by a static model. The resonance light scattering (RLS) method was used to confirm the formation of the P4R-trypsin complex. The thermodynamic data indicated that the predominant interactions between P4R and trypsin were Van der Waals and hydrogen bonds, consistent with docking results. The distance between P4R and trypsin after the interaction was calculated based on fluorescence resonance energy transfer (FRET) theory and found to be 3.36 nm. Synchronous fluorescence, three-dimensional fluorescence, UV–Visible spectrophotometry, and circular dichroism (CD) analyses indicated that the conformation of trypsin was changed upon binding with P4R, which could affect the trypsin function. Kinetic studies revealed that P4R inhibited trypsin activity in a non-competitive model, and docking analysis confirmed that P4R was not bound to the active site of the trypsin. The molecular dynamics (MD) simulation studies showed that the root mean square deviation (RMSD) in the trypsin-P4R complex (0.270 ± 0.02 nm) was larger than that of the free trypsin system (0.221 ± 0.01 nm), which agreed with CD and thermal stability experiments. Thus, P4R was shown to be a potent inhibitor and quencher of trypsin.

The effect of radiofrequency heat treatment on trypsin inhibitor activity and in vitro digestibility of soybean varieties (Glycine max. (L.) Merr.)

Kunitz (KTI) and Bowman-Birk (BBI) trypsin inhibitors were characterized in soybean seeds. Cultivars having KTI/BBI (Pannónia Kincse, PK) or lacking KTI (Aries; Hilario; Bahia) were assessed with well-characterized soybean varieties having Ti-a or ti types of KTI mobility. The TIA values of Pannónia Kincse (9.8 ± 0.48 mg/g) were not significantly different (p ≤ 0.05) from Ti-a samples (10.07 ± 1.86 mg/g), while of Aires, Bahia, Hilario (6.19 ± 1.89) were identical (p ≤ 0.05) with ti samples (6.63 ± 1.99). Radiofrequency heat treatment (RF) decreased TIA values (p ≤ 0.05) at ≥ 100 °C. However, in the traditional soybean variety, the RF at 110 °C was more effective in eliminating the residual KTI activity. The remaining or the disapperaing bioactive form of trypsin inhibitors were succesfully characterized by the means of a standardized in vitro digestion model. It showed that residual BBI-originated trypsin inhibitor activity was in the stomach even after RF at 110 °C, whereas its chymotrypsin inhibitor activity was not detectable at all. Although PK and KTI null types of soybean seeds still required an energy-saving, gentle heat treatment to inactive the trypsin inhibitors before using them as food or feed, the physicochemical properties and processing quality of soybean products were protected, improved.

Color and texture of surimi-like gels made of protein isolate extracted from catfish byproducts are improved by washing and adding soy whey.

Protein extraction from catfish byproducts has been proven economically and technically feasible. However, the gel prepared from protein isolate was dark and lacked elasticity. Byproduct mince washing and application of soy whey were adopted in this study to address the above gel quality issues. Heating soy whey at 75°C for 3min could eliminate over 99.9% lipoxygenase activity and retain more than 50% trypsin inhibitor activity. Washing byproduct mince for 2min with water-to-mince ratio of 2:1 could achieve satisfactory gel color, which was comparable to that of commercial surimi gels. When soy whey was applied, the autolytic enzyme-induced proteolysis was inhibited in a dose-dependent manner by up to 74%. With addition of soy whey, resilience, hardness at maximum force, hardness at 5mm compression, springiness, cohesiveness, chewiness, fracturability, and deformation could be increased by up to 43.10%, 66.92%, 36.72%, 14.59%, 29.17%, 143.25%, 93.82%, and 27.97%, respectively. However, the texture was still inferior to the gel made from fillet mince. SDS-PAGE revealed that myosin was most susceptible to proteolysis and application of soy whey could effectively protect it from degradation. Different from tropomyosin, myosin and actin were greatly involved in disulfide bond formation. PRACTICAL APPLICATION: Catfish byproducts and soy whey, a byproduct from soy protein isolation, are normally treated as waste. The current study proved the possibility to utilize these two byproducts to make value-added surimi-like gel products. Utilization of byproducts would not only increase profitability of catfish and soy processing, but also preserve the precious fish proteins and other health-promoting components.

Impact of the Structural Modifications of Potato Protein in the Digestibility Process under Semi-Dynamic Simulated Human Gastrointestinal In Vitro System.

The raising consumer demand for plant-derived proteins has led to an increased production of alternative protein ingredients with varying processing histories. In this study, we used a commercially available potato protein ingredient with a nutritionally valuable amino acid profile and high technological functionality to evaluate if the digestibility of a suspension with the same composition is affected by differences in the structure. Four isocaloric (4% protein, w/w) matrices (suspension, gel, foam and heat-set foam) were prepared and their gastrointestinal fate was followed utilizing a semi-dynamic in vitro digestion model. The microstructure was observed by confocal laser scanning microscopy, protein breakdown was tested by electrophoresis and free amino acids after intestinal digestion was estimated using liquid chromatography/triple-quadruple-mass spectrometry (LC-TQMS). The heat-treated samples showed a higher degree of hydrolysis and lower trypsin inhibitory activity than the non-heat-treated samples. An in vitro digestible indispensable amino acid score was calculated based on experimental data, showing a value of 0.9 based on sulfur amino acids/valine as the limiting amino acids. The heated samples also showed a slower gastric emptying rate. The study highlights the effect of the food matrix on the distribution of the peptides created during various stages of gastric emptying.

Physicochemical and nutritional assessment of soy milk and soymilk products and comparative evaluation of their effects on blood gluco-lipid profile

This research work presents the physicochemical and nutritional evaluation of soymilk and soymilk based products like tofu and its by-product okhara and soy yoghurt and a comparative study of their effect on blood gluco-lipid profile in both animal models and Type 2 diabetic patient volunteers. Their nutritional effect were also assessed amongst children and young mothers. All products have significant protein, fat, carbohydrate and crude fiber content. Total polyphenolic content of soymilk was determined to be 2.26±1.02 mg GAE/g; the phytate content in raw soy milk ranged between 0.1-0.3%; trypsin inhibitory activity of soybean was found to be 46.52±0.98. Results have shown the significant nutritional potentials of soymilk and soymilk based products. The average baseline BMI of 16.5 and 19.1 for child and young mothers participants were improved to 18.1 and 19.8 after intake of soy milk and soymilk based products. Okhara significantly (p<0.001) reduced the escalated blood gluco-lipid parameters, followed by soymilk, soy yoghurt and tofu as evident both in animal and human studies. Thus soy milk and soy milk based products not only improve the nutritional status but also an effective nutraceutical adjunct therapy against hyperglycaemia.

Chemo-profiling by UPLC-QTOF MS analysis and in vitro assessment of Anti-inflammatory activity of Field Milkwort (Polygala arvensis Willd.)

P. arvensis has traditionally been used in folk herbal therapy to treat a variety of ailments. This study looked at the phytochemical, antioxidant, and anti-inflammatory effects of P. arvensis stem, leaf, and root water and methanol extracts. When compared to stem and root extracts, the dry methanolic leaf extract had the highest phenolic and flavonoid concentrations of 291.56±0.01 mg GAE/gm DW and 65.53±0.08 mg RE/gm DW. Methanol root extract contained the greatest quantities of terpenoids and saponins, with 94.62±0.013 mg UAE/gm DW and 165.77±0.04 mg DE/gm DW, respectively. Methanol leaf extract contains much more alkaloids (52.19±0.08mg CE/gm FW) than stem and root extract. Although fresh leaf methanol extract has superior DPPH scavenging activity (79.79 ±0.003 percent), fresh leaf aqueous extract has higher ABTS scavenging capacity (64.35 ±0.09 percent) than the other extracts. P. arvensis has potential anti-inflammatory chemicals, according to UPLC-QTOF MS study. These chemicals may be responsible for membrane stabilization (87.78±0.03%), inhibition of protein denaturation (96.27±0.01%), inhibition of trypsin activity (80.97±0.05), and inhibition of NO generation. The suppression of NO generation was studied using LPS-treated RAW 264.7 macrophage cells. P. arvensis plant portions are also less harmful to cultured RAW 264.7 macrophage cells when tested using the MTT assay. The obtained results suggested that the plant is an effective anti-inflammatory agent.

SAXS Analysis and Characterization of Anticancer Activity of PNP-UDP Family Protein from Putranjiva roxburghii.

A class of plant defense and storage proteins, including Putranjiva roxburghii PNP protein (PRpnp), belongs to PNP-UDP family. The PRpnp and related plant proteins contain a disrupted PNP-UDP domain as revealed in previous studies. In PRpnp, the insert disrupting the domain contains the trypsin inhibitory site. In the present work, we analyzed native PRpnp (nPRpnp) complex formation with trypsin and inosine using SAXS experiments and established its dual functionality. Results indicated a relatively compact nPRpnp:Inosine structure, whereas trypsin complex showed conformational changes/flexibility. nPRpnp also exhibited a strong anti-cancer activity toward breast cancer (MCF-7), prostate cancer (DU-145) and hepatocellular carcinoma (HepG2) cell lines. MCF-7 and DU-145 were more sensitive to nPRpnp treatment as compared to HepG2. However, nPRpnp treatment showed no effect on the viability of HEK293 cells indicating that nPRpnp is specific for targeting the viability of only cancer cells. Further, acridine orange, DAPI and DNA fragmentation studies showed that cytotoxic effect of nPRpnp is mediated through induction of apoptosis as evident from the apoptosis-associated morphological changes and nuclear fragmentation observed after PRpnp treatment of cancer cells. These results suggest that PRpnp has the potential to be used as an anticancer agent. This is first report of anticancer activity as well as SAXS-based analysis for a PNP enzyme with trypsin inhibitory activity.

Chemical or enzymatic deglycosylation and germination abrogates the inhibitory activity of Cyamopsis tetragonoloba trypsin inhibitor

Chemical or enzymatic deglycosylation and germination abrogates the inhibitory activity of Cyamopsis tetragonoloba trypsin inhibitor

Effect of cereal based traditional malting technology on nutritional quality of iron-rich bean flour

Iron deficiency is a major public health challenge affecting the health of about 18 and 13.8% of children and women globally, respectively. About 43% children and 29% women in sub-Saharan Africa suffer from Iron Deficiency Anemia. In Uganda, recent demographic health statistics indicate that the prevalence of anaemia among children of 6-59 months stands at 53%; while that for women of child bearing age stands at 32%. Biofortified iron-rich bean varieties have been developed and adopted in Uganda to contribute to alleviation of iron deficiency challenges. The objective of this study was to investigate the effect of traditional malting technology on nutritional quality of biofortified iron-rich beans (Phaseoulus vulgaris L.). The study examined the effect of the traditional malting technology on: (i) the contents of anti-nutritional factors (phytates, oxalates, polyphenols, tannins, trypsin inhibitor activity); (ii) digestibility of protein and bioavailability of iron and zinc; and (iii) retention of proximate constituents and mineral micronutrient contents in bean varieties. We used three bean varieties, namely NAROBEAN 1, hereafter referred to as NB1, NAROBEAN 2 (NB2), and NAROBEAN 3 (NB3), all of which are widely produced and consumed in Acholi sub-region. Application of paired t-test revealed that the traditional malting technology reduced only the content of oxalates by 42.3-54.8 % and trypsin inhibitor activity by 6.2-34.6 %, from the three varieties. The content of total phenols was reduced by 22.3 % only in NB 1 (P&lt; 0.05). The traditional malting technology improved protein digestibility for the three varieties by 38-43.6 % (P&lt; 0.05). Bioavailability of iron improved from in NB1 by 26.7 % and NB2 by 11.5 %; while that of zinc improved for only NB2 by 51.5 % (P&lt;0.05). The contents of micronutrients and proximate constituents were not adversely affected by the traditional malting technology, except for phosphorus in NB1 and magnesium in NB3. Overall, traditional malting technology is effective at reducing trypsin inhibitors and oxalates, and improving protein digestibility and iron bioavailability.

JcTI-PepI, a synthetic peptide bioinspired in the trypsin inhibitor from Jatropha curcas, presents potent inhibitory activity against C. krusei, a neglected pathogen

Antimicrobial resistance has been increasing globally, posing a global public health risk. It has prompted the scientific community to look for alternatives to traditional drugs. Antimicrobial Peptides (AMPs) have stood out in this context because they have the potential to control infectious diseases while causing no or little harm to mammalian cells. In the present study, three peptides, JcTI-PepI, JcTI-PepII, and JcTI-PepIII, were designed and tested for antimicrobial activity based on the primary sequence of JcTI-I, a 2S albumin with trypsin inhibitory activity from Jatropha curcas. JcTI-PepI strongly inhibited C. krusei growth, and it caused severe disruptions in cellular processes and cell morphology. C. krusei cells treated with JcTI-PepI showed indicative of membrane permeabilization and overproduction of Reactive Oxygen Species. Moreover, the yeast's ability to acidify the medium was severely compromised. JcTI-PepI was also effective against pre-formed biofilm and did not harm human erythrocytes and Vero cells. Overall, these characteristics indicate that JcTI-PepI is both safe and effective against C. krusei, an intrinsically resistant strain that causes serious health problems and is frequently overlooked. It implies that this peptide has a high potential for use as a new antimicrobial agent in the future.

Cold-pressed sesame seed meal as a protein source: Effect of processing on the protein digestibility, amino acid profile, and functional properties

Alternative protein sources for the human diet may help overcome the food security challenge for a growing population and its environmental impact. Edible oil extraction by-products are potential sources due to high protein content. This study characterized cold-pressed sesame seed meals about the proximate composition, antinutritional factors, amino acid profile and score, and in vitro protein digestibility (IVPD). A central composite experimental design supported evaluating the impact of cooking, microwave, and ultrasound on the nutritional quality of this meal. The raw sample presented 35% of protein and 89% of IVPD. Optimized conditions were 87.8 ºC, pH 8.0, and 37 min for all processes studied, increasing IVPD up to 95%. The treatments effectively reduced up to 55% trypsin inhibitor activity and 81% phytic acid content. Lysine was the only limiting amino acid before or after processing. Sesame seed by-product has high-quality protein and can be a plant-based source for food formulations.