High Molecular Weight Peptides Research Articles

Effect of Lactiplantibacillus plantarum CNPC003 and milk pasteurization on artisanal goat coalho cheese characteristics

This study evaluated the effect of adding Lactiplantibacillus plantarum CNPC003 (LP) and applying milk pasteurization on the microbiological, technological, and physicochemical characteristics and protein profile of artisanal goat coalho cheese during 60 days of ripening. Four types of cheese were produced, including cheeses made with raw and pasteurized goat milk and with and without LP (RC, PC, RCLP, and PCLP). All cheeses were safe for consumption and maintained high lactic acid bacteria counts (above 8 log CFU mL−1) at the end of the ripening period. RC and RCLP showed higher hardness and lower chewiness than cheeses made with pasteurized milk (PC and PCLP) after 60 days of ripening. As expected, there was a reduction in lactose content with a simultaneous increase in acidity and syneresis for all cheeses over the 60 days of ripening, with no significant change in the other evaluated physicochemical parameters. Proteolysis rates increased in all cheeses up to 60 days of ripening, aligning with elevated levels of soluble protein and free amino acids. After 60 days of ripening, PC showed a higher extent of proteolysis index, higher amount of high molecular weight peptides, higher number of identified proteins, and lower content of free amino acids. RCLP showed a higher depth of proteolysis index, higher free amino acids amount (1583 ± 3.95 mg 100 g−1), and fewer identified proteins. Among the peptides identified, it was possible to define 30 potential bioactive peptides according to the bioactivity score (>0.5), where both cheeses added with LP had 18 of these peptides, mostly potentially ACE inhibition sequences. The addition of LP and the pasteurization of milk positively affected the microbiological safety of ripened coalho goat cheeses, primarily contributing to the differentiation of their texture and protein and bioactivity profile.

Release of Bioactive Peptides from Erythrina edulis (Chachafruto) Proteins under Simulated Gastrointestinal Digestion.

The estimated and concerning rise in world population over the next few years and the consequent increase in food demand will lead to a deterioration in global food security. To avoid or reduce this world crisis, informed and empowered consumers are turning to sustainable and nutrient-rich foods that substitute animal products, also reducing their associated environmental impact. Moreover, due to the demonstrated influence of diet on the risk of high incidence and mortality of noncommunicable diseases, the current established food pattern is focused on the consumption of foods that have functionality for health. Among these new foods, traditional and underutilized plants are gaining interest as alternative protein sources providing nutritional and biological properties. In this work, the potential of Erythrina edulis (chachafruto) proteins as a source of multifunctional peptides after transit through the gastrointestinal tract has been demonstrated, with antioxidant and immunostimulating effects in both biochemical assays and cell culture. While low molecular weight peptides released during the digestive process were found to be responsible for protection against oxidative stress mediated by their radical scavenging activity, high molecular weight peptides exerted immunostimulating effects by upregulation of immunoresponse-associated biomarkers. The findings of this study support the promising role of chachafruto proteins as a new antioxidant and immunostimulatory ingredient for functional foods and nutraceuticals.

Exploring the underlying mechanisms on NaCl-induced reduction in digestibility of myoglobin

In this paper, the structural changes of myoglobin after salt treatment and the binding mode of substrate and pepsin/trypsin were studied by ultraviolet absorption spectroscopy, synchronous fluorescence spectroscopy, LC-MS/MS and molecular dynamics simulation. NaCl treatment changed the heme structure and hydrophobic cavity of myoglobin, which in turn decreased the digestibility of the protein. Trypsin was more effective for digestion of high molecular weight peptides. Molecular dynamics simulation showed that the binding of myoglobin and pepsin/trypsin was mainly maintained by hydrogen bond and hydrophobicity. In addition, the catalytic active center of pepsin is not suitable for long-time existence of low-molecular weight peptide under salt treatment. The findings provide a new insight into the low bioavailability of myoglobin.

Selection of indigenous Lacticaseibacillus paracasei CD 4 for production of gluten-free traditional fermented product Bhaturu

ABSTRACT Celiac disease is an autoimmune disorder triggered by immune-toxic peptides generated through incomplete hydrolysis of wheat gluten. This study reports the screening of potential probiotic strains to hydrolyze wheat gluten. The selected strain was used in the production of gluten-free traditional fermented and fried bread, Bhaturu. Lacticaseibacillus paracasei CD4 and Limosilactobacillus gastricus BTM7 produced halo zones on gluten containing agar plates. Lc. paracasei CD4 resulted in 2.3 folds higher free amino acid content in gluten-based medium. The SDS-PAGE analysis indicated that gluten was degraded into high and low molecular weight peptides. The fermentation of wheat flour was conducted with 7.0 log CFU/g of Lc. paracasei CD4 for 24 h. A fermentation time of 12 h was selected based on higher viable cell count, ammoniacal-nitrogen, and titratable acidity. The fermentation resulted in decrease in albumin, glutenin and gliadin contents (P > .05). The Bhaturu prepared from fermented dough had higher acceptability based on sensory evaluation.

Formulation and evaluation of fast dissolving tablets of captopril

Oral administration is the most popular route for systemic effects due to its ease of ingestion, pain, avoidance, versatility and most importantly, patient compliance. The development of enhanced oral protein delivery technology by mouth dissolving Tablets which may release these drugs in the mouth are very promising for the delivery of high molecular weight protein and peptide. Good mouth feel property of MDDS helps to change the basic view of medication as “bitter pill”, particularly for pediatric patients. To prepare mouth dissolving tablet using SSG & CCM by using Antihypertensive as model drug. Captopril is a potent, competitive inhibitor of angiotensin-converting enzyme and it is a key component of the renin-angiotensin-aldosterone system. The ƛmax of Captopril was determined by scanning the 10µg / ml solution of drug using UV-Spectrophotometer and was found to be 271nm. The linear correlation was found to be 0.9995.The Fast dissolving tablets of captopril were prepared by direct compression method. Captopril can be successfully formulated as mouth dissolving tablets using various super disintegrate in different concentrations by direct compression method. The formulation containing 10% of crospovidone as super disintegrated was found to be outstanding than other formulations in terms of disintegration time and rate of dissolution.

A Recent Update on Intranasal Delivery of High Molecular Weight Proteins, Peptides, and Hormones.

Proteins and hormones have a wide range of therapeutic uses that have emerged throughout the years. The increase in their clinical application nowadays has outgrown the need to deliver these macromolecules without deterioration. This is where the nasal route of delivery has proven to be the most helpful tool in providing ease of administration. Despite the obstacles, smart polymers, nasal enhancers, nanotechnology-based delivery systems, and computational modeling tools have all been used to increase the nasal route's residence time and absorption window. This review highlights the systemic delivery of macromolecules such as protein and hormones, which can also be delivered via nose-to-brain through various transportation pathways. This strategy has proved beneficial in treating several neurological disorders like brain tumors, Alzheimer's, Ischemic stroke, etc. Except for the marketed preparation and patents, several other drugs are still under clinical trials. We also like to conclude that many of the newer proteins and hormones are still under developmental stages, for which nasal delivery will be a boon in administering these newer molecules.

Magnetic solid-phase extraction of high molecular weight peptides using stearic acid-functionalized magnetic hydroxyapatite nanocomposite: determination of some hypothalamic agents in biological samples.

Therapeutic peptides have an important effect on physiological function and human health, so it is momentous to quantify and detect low levels of these biomolecules in biological samples for treatment and diagnostic purposes. In the present study, an efficient magnetic solid-phase extraction (MSPE) method was developed based on stearic acid-functionalized magnetic hydroxyapatite nanocomposite (MHAP/SA) as a novel and cost-effective adsorbent for extraction of five hypothalamic-related peptides (goserelin, octreotide, triptorelin, somatostatin, and cetrorelix) from biological samples. To characterize the morphology and physicochemical properties of MHAP/SA, Fourier transform infrared spectroscopy (FT-IR), energy-dispersive X-ray spectroscopy (EDS), field emission scanning microscopy (FE-SEM), CHNS elemental analysis, Brunauer-Emmett-Teller (BET), and vibrating sample magnetometry (VSM) were applied. Under optimum conditions, the proposed method (MSPE-HPLC-UV) represented favorable linearity with R2 ≥ 0.9987, suitable intra- and inter-day precisions (RSD ≤ 6.9% and RSD ≤ 8.1%, respectively, n = 3), and limits of detection and quantification in the range of 0.75-1.12ngmL-1 and 2.50-3.75ngmL-1, respectively. Eventually, the proposed method was used for the extraction and quantification of target therapeutic peptides in plasma and urine samples, and satisfactory relative recoveries were achieved in the range of 90.6-110.3%.

Effect of Physical and Enzymatic Pre-Treatment on the Nutritional and Functional Properties of Fermented Beverages Enriched with Cricket Proteins.

The aim of this study was to evaluate the effects of γ-irradiation (IR), ultrasound (US), and combined treatments of ultrasound followed by γ-irradiation (US-IR), ultrasound followed by enzymatic hydrolysis with and without centrifugation (US-E and US-EWC, respectively), and ultrasound followed by γ-irradiation and enzymatic hydrolysis (US-IRE), on the digestibility and the nutritional value of fermented beverages containing probiotics. Results showed that US (20 min), IR (3 kGy) and US-IR (tUS = 20 min, dose = 3 kGy) treatments raised protein solubility from 11.5 to 21.5, 24.3 and 29.9%, respectively. According to our results, these treatments were accompanied by the increased amount of total sulfhydryl groups, surface hydrophobicity and changes to the secondary structure of the proteins measured by Fourier-transform infrared spectroscopy (FTIR). Fermented probiotic beverages, non-enriched (C) and enriched with untreated (Cr) or treated cricket protein with combined treatments were also evaluated for their in vitro protein digestibility. Results showed that the soluble fraction of US-IRE fermented beverage had the highest digestibility (94%) as compared to the whole fermented tested beverages. The peptides profile demonstrated that US-IRE had a low proportion of high molecular weight (MW) peptides (0.7%) and the highest proportion of low MW peptides by over 80% as compared to the other treatments.

In vitro protein digestibility and physico-chemical properties of lactic acid bacteria fermented beverages enriched with plant proteins.

The objective of this study was to develop probiotic beverages, enriched with plant proteins, with high nutritional value. A rice-based beverage fermented with a specific probiotic formulation comprised Lactobacillus acidophilus CL1285, Lactobacillus casei LBC80R and Lactobacillus rhamnosus CLR2 has been enriched with a combination of pea and rice proteins (PR) or pea and hemp proteins (PH) at 13 and 11% total protein, respectively. These protein associations have been selected because their amino acid ratio was >1, as recommended by the FAO. The beverage enriched with protein significantly increased its viscosity by more than 10 times thanks to the enrichment, while the fermentation reduced it by 50% for PR and 20% for PH. In vitro protein digestibility results showed that the protein enrichment and the fermentation treatment significantly increased digestibility values of the beverages with value of 72.7% for fermented PR beverage and 61.4% for unenriched fermented control beverage (p ≤ 0.05). Peptide profiles of PR and PH enriched beverages indicated that the fermentation led to a reduced level of high molecular weight (HMW) peptides of about 60% and an increase of low molecular weight (LMW) peptides by over 50%. Therefore, both the fermentation and the enrichment in protein increased the nutritional value of the rice-based beverages. PRACTICAL APPLICATION: Good quality of probiotics formulation and high-protein products are in increasing demand and plant proteins as an alternative of animal protein are popular. This study has permit to develop rice-based commercial probiotic beverages enriched in a combination of pea and rice or pea and hemp proteins in order to obtain a complete protein in terms of amino acids composition. The lactic acid fermentation and the enrichment with a plant protein combination led to a better protein digestibility of beverage.

Targeting ovarian solid tumors by pH triggered thermosensitive peptide-doxorubicin conjugate

All anticancer drugs have undesirable side effects and lack target specificity. Drug delivery systems (DDS) developed so far have shown only limited success. Newer DDS with target specificity and undesirable side effects are, therefore, essential today. Given that sensitive polymers, peptides, dendrimers and hydrogels have been widely investigated as carriers for controlled release and target specificity, it is still a challenge to overcome the cumbersome problems faced in cancer treatment. In this context, we designed, synthesized and evaluated a high molecular weight, temperature and pH sensitive peptide (VPGVGVPGVG). Doxorubicin (Dox) was conjugated to the peptide using hydrazone linkage. The successful synthesis and conjugation of Dox was confirmed by FTIR, NMR and LCMS/MS studies. Isoelectric point calculator, UV-Spec, DSC, in vitro drug release studies revealed the thermosensitive and pH sensitive nature of the peptide. In vitro cytotoxic studies in SKOV-3 cell lines showed an IC50 value of 232.96 μg/ml for the dual sensitive peptide (DSP) compared to an IC50 value of 46.78 μg/ml for the dual sensitive peptide-Dox conjugate (DSP-DC) and 38.49 μg/ml for the free drug, Dox. In vivo fluorescence image analysis and histopathology studies revealed the site-specific capability of the DSP-DC.

Effects of microwave heating on the protein structure, digestion properties and Maillard products of gluten

As a kind of traditional food, gluten is widely studied for its physical and chemical properties after processing, while little attention is paid to the simulation cooking processing, digestion and safety. In this paper, gluten was heated with microwave to study its structural transformations, nutritional efficiency, and food safety under Chinese home cooking (CHC). After microwave treatment, intermolecular and intramolecular cross-linking of gluten were formed to result in more aggregation. The secondary structure of gluten changed significantly as well as the formation of α-helix and β-turn promoted under the high power input. Treated with 1000W for 5min, cross-linking between amino acids increased, leading the reduction of total amino acids, in vitro protein digestibility and the increase of high molecular weight peptides, while the proportion of essential amino acids kept the same. In the simulation of CHC, the highest content of 5-hydroxymethyl furfural was observed after adding all condiments under 1000W for 5min. In addition, sugar played a major role in Maillard reaction to promote the formation of melanoidin and fructosamine while salt and oil did not significantly affect these two Maillard products. Vinegar inhibited the reaction due to the acidic condition but provided some melanoidin and fructosamine itself.

Enzymatic hydrolysates of whey protein and chicken egg ppotein: production, physical-chemical and immunochemical characteristics

Whey protein concentrate (WPC) and chicken egg protein (CEP) and enzymes such as pancreatin and alkalase have been used. Proteolysis of proteins was carried out in an FA-10 fermenter for 3 hours at an enzyme : substrate ratio of 1:50 in dry matter, at optimal pH and temperature for pancreatin and alkalase. Enzymes were inactivated at +75 °C and fermentolizate was ultrafiltered. The solutions were concentrated by reverse osmosis and freeze-dried. The molecular weight distribution of the peptide fractions was evaluated by HPLC. Residual antigenicity was determined by the method of indirect enzyme-linked immunosorbent assay and expressed as the fold of antigenicity reduction relative to the original protein. During WPC proteolysis with pancreatin the hydrolyzate was obtained with a fold reduction of antigenicity of 2.3×103 relative to the initial WPC. A decrease in antigenicity of 4.7×104 times was achieved with proteolysis of WPC by alkalase. The combination of WPC fermentolysis with pancreatin or alkalase followed by ultrafiltration reduced the content of high molecular weight peptides with a mass more than 8.7 kDa. The multiplicity of decrease in antigenicity with respect to the starting protein was 1.64×105 and 1.90×105, respectively. After repeated ultrafiltration the reduction in antigenicity of the obtained WPC alkalase or pancreatin hydrolysate was more than 1.0×106 and more than 5.0×105, respectively. The decrease in antigenicity of the CEP hydrolyzate obtained with proteolysis by alkalase and ultrafiltration compared to the initial CEP was 1.0×105 times, and 5.0×105 times when we used repeated ultrafiltration. A significant decrease in the content of high molecular weight peptides and a decrease in the antigenicity of peptide mixtures based on WPC and CEP to the values that permit their use in hypoallergenic products is achieved by combining proteolysis and double ultrafiltration through a UF10 membrane.

Impact of D2O on peptidization of l-hydroxyproline

This is our fourth consecutive study carried out in an order to collect experimental evidence regarding the impact of heavy water (D2O) on the spontaneous oscillatory peptidization of proteinogenic α-amino acids and this time its subject matter is l-hydroxyproline (l-Hyp). Our three earlier studies have been focused on the two sulfur-containing α-amino acids, i.e., l-cysteine (l-Cys) and l-methionine (l-Met), and on one structurally related α-amino acid, i.e., l-proline (l-Pro). It seemed interesting to assess the effect induced by D2O on l-Hyp and to compare it with the effects valid for l-Cys, l-Met, and l-Pro. As analytical techniques, we used high-performance liquid chromatography with the evaporative light-scattering detection (HPLC-ELSD), mass spectrometry (MS), and scanning electron microscopy (SEM). The obtained results make it clear that the impact of heavy water on dynamics of spontaneous peptidization of l-Hyp differs from that exerted on three other α-amino acids discussed (although in all four cases, heavy water significantly hampers spontaneous oscillatory peptidization). With l-Hyp, an increasing proportion of D2O in the reaction mixture results in decreasing yields of both, the soluble lower molecular weight peptides and the insoluble higher molecular weight peptides. With the two sulfur-containing compounds (l-Cys and l-Met), an increasing proportion of D2O in the reaction mixture resulted in growing yields of the soluble lower molecular weight peptides at an expense of decreasing yields of the insoluble higher molecular weight peptides. With l-Pro, still different pattern was observed, namely that the hampering effect of D2O on peptidization was not monotonously dependent on the concentration of D2O in the system, but it was the strongest pronounced for 10% (v/v) D2O in the employed binary methanol–water solvent (with the investigated proportions of D2O in this solvent changing from 0 to 30%). We hope that firm quantitative results presented in this study (and also in the three earlier studies from this cycle) can prove an inspiration for future researchers interested in getting a deeper insight into the role of D2O in life processes, and more specifically in the kinetic and mechanistic aspects thereof. Perhaps it might be noteworthy to add that out of four α-amino acids investigated so far, which can be divided into two groups of the endogenous (l-Cys and l-Pro) and exogenous (l-Met and l-Hyp) species, the endogenous species undergo spontaneous peptidization following the circadian rhythm, whereas the exogenous ones (including l-Hyp) do not.

Rice (Oryza sativa japonica) albumin hydrolysates suppress postprandial blood glucose elevation by adsorbing glucose and inhibiting Na+-d-glucose cotransporter SGLT1 expression

Abstract The mechanism of the suppressive effect of rice albumin (RA) on postprandial hyperglycemia after glucose loading was investigated. In order to examine if small peptides derived from RA are responsible for prevention of postprandial hyperglycemia, RA was hydrolysed to indigestible high-molecular-weight peptides (HMP) and low-molecular-weight peptides (LMP) by trypsin, HMP and LMP being fractionated by gel-filtration chromatography. In oral glucose tolerance test (OGTT), both HMP and LMP suppressed the increase in blood glucose levels. In vitro diffusion test results showed that HMP adsorbed glucose and retarded its diffusion rate like dietary fibers. On the other hand, LMP suppressed the expression of sodium-dependent glucose transporter-1 (SGLT1) in STC-1 cells. Therefore, the suppressive effect of RA on postprandial hyperglycemia would be due to the dual actions of HMP and LMP. Our results demonstrated the potential use of RA as a functional food material to prevent diabetes.

Characterization of the Antimicrobial Substances Produced by Nibribacter radioresistens

This study characterized the antimicrobial substances produced by the radiation-resistant bacterium Nibribacter radioresistens. The antimicrobial substances showed activity against Salmonella Gallinarum, pathogenic Escherichia coli, Bacillus cereus, Streptococcus iniae, and Saccharomyces cerevisiae. The substances showed higher activity against Gram-positive bacteria than against Gram-negative bacteria and yeast. N. radioresistens showed the best growth rate in LB liquid medium at 37oC; however, production of the antimicrobial substances was not associated with growth. Since the activity of the antimicrobial substances was affected by proteinase K and EDTA, the substances were presumed to be antimicrobial peptides (AMPs). The antimicrobial substances produced by N. radioresistens were unstable at higher temperatures and in acidic and basic pH ranges, and most of the activity was attributed to either low ( 30 kDa) molecules. When S. Gallinarum was treated with the antimicrobial substances, the cell destruction was acted on the cell envelope. Therefore, we concluded that N. radioresistens produces broad-spectrum and very unstable antimicrobial substances that mostly consist of low- and high-molecular weight peptides.

Novel Peptidomic Approach for Identification of Low and High Molecular Weight Tauopathy Peptides Following Calpain Digestion, and Primary Culture Neurotoxic Challenges.

Tauopathy is a class of a neurodegenerative disorder linked with tau hyperphosphorylation, proteolysis, and aggregation. Tau can be subjected to proteolysis upon calpain activation in Alzheimer disease (AD), and traumatic brain injury (TBI). We and others have extensively researched calpain-mediated tau breakdown products (Tau-BDP; 45K, 35K, and 17K). Tau proteolysis might also generate low molecular weight (LMW ≤10K) proteolytic peptides after neurodegenerative damage. In this study, we have subjected purified tau protein (phospho and non-phospho) and mouse brain lysate to calpain-1 digestion to characterize the LMW generated by nano-liquid chromatography coupled to electrospray ionization to tandem mass spectrometry (nano-LC-ESI-MS/MS). We have also challenged differentiated primary cerebrocortical neuronal cultures (CTX) with neurotoxic agents (calcium ionophore calcimycin (A23187), staurosporine (STS), N-methyl-D-aspartate (NMDA), and Maitotoxin (MTX)) that mimic neurodegeneration to investigate the peptidome released into the conditioned cell media. We used a simple workflow in which we fractionate LMW calpain-mediated tau peptides by ultrafiltration (molecular weight cut-off value (MWCO) of 10K) and subject filtrate fractions to nano-LC-MS/MS analysis. The high molecular weight (HMW) peptides and intact proteins retained on the filter were analyzed separately by western blotting using total and phospho-specific tau antibodies. We have identified several novel proteolytic tau peptides (phosphorylated and non-phosphorylated) that are only present in samples treated with calpain or cell-based calpain activation model (particularly N- and C-terminal peptides). Our findings can help in developing future research strategies emphasizing on the suppression of tau proteolysis as a target.

A catalytic antioxidant for limiting amyloid-beta peptide aggregation and reactive oxygen species generation.

Alzheimer's disease (AD) is a multifaceted disease that is characterized by increased oxidative stress, metal-ion dysregulation, and the formation of intracellular neurofibrillary tangles and extracellular amyloid-β (Aβ) aggregates. In this work we report the large affinity binding of the iron(iii) 2,17-bis-sulfonato-5,10,15-tris(pentafluorophenyl)corrole complex FeL1 to the Aβ peptide (K d ∼ 10-7) and the ability of the bound FeL1 to act as a catalytic antioxidant in both the presence and absence of Cu(ii) ions. Specific findings are that: (a) an Aβ histidine residue binds axially to FeL1; (b) that the resulting adduct is an efficient catalase; (c) this interaction restricts the formation of high molecular weight peptide aggregates. UV-Vis and electron paramagnetic resonance (EPR) studies show that although the binding of FeL1 does not influence the Aβ-Cu(ii) interaction (K d ∼ 10-10), bound FeL1 still acts as an antioxidant thereby significantly limiting reactive oxygen species (ROS) generation from Aβ-Cu. Overall, FeL1 is shown to bind to the Aβ peptide, and modulate peptide aggregation. In addition, FeL1 forms a ternary species with Aβ-Cu(ii) and impedes ROS generation, thus showing the promise of discrete metal complexes to limit the toxicity pathways of the Aβ peptide.

Pigeon pea enzymatic protein hydrolysates and ultrafiltration peptide fractions as potential sources of antioxidant peptides: An in vitro study

Pigeon pea protein isolate was hydrolysed using food grade enzymes (alcalase, pancreatin, pepsin + pancreatin). The resulting hydrolysates were fractionated by membrane ultrafiltration and evaluated for their antioxidant activities. Fraction with molecular weight <1 kDa had the highest peptide yield (36.97%) for pepsin + pancreatin (PPHPp) hydrolysates, whereas fraction 1–3 kDa showed the highest yield (28.84%, 37.27%) for alcalase-derived peptide (PPHA) and pancreatin-derived peptide (PPHPa) respectively. Low molecular weight fractions of PPHPa showed highest inhibitory activity against DPPH•, superoxide (PPHA, PPHPa), and •OH scavenging activities. However, high molecular weight peptides exhibited better radical scavenging activity (DPPH) and reducing property (FRAP) than the low molecular weight peptides. All fractions exhibited higher ferric reducing and ABTS•+ scavenging activity than the crude hydrolysates. All the peptides also had a higher ABTS•+ scavenging activity than GSH. The low MW fractions (<5 kDa) were able to inhibit the progression of lipid peroxidation during the first four days of incubation for most of the peptides. Our findings show that membrane ultrafiltration significantly increased antioxidant properties and the peptides have the potential to be useful as functional ingredient in food and nutraceutical industry to maximise the use of underutilised protein sources.

Recovery and quantification of a myelin oligodendrocyte glycoprotein peptide from rat plasma after protein precipitation

The recovery of high molecular weight peptides from complex biological samples is a challenging task. Herein, a reliable, cost effective and rapid methodology was developed for the recovery and quantification of a myelin oligodendrocyte glycoprotein epitope namely (LysGly)5MOG35-55, from rat plasma. Removal of plasma proteins before quantification of the peptide was achieved after precipitation by an acetonitrile/water/formic acid solution. Using the developed protocol, average recoveries of the peptide from plasma ranged between 83.3 and 90.3%.

Antibacterial potential of venom extracted from wolf spider, Lycosa terrestris (Araneae: Lycosiade)

The wolf spider Lycosa terrestris (Araneae: Lycosidae) is a well known arthropod containing toxic compounds. It has significant predatory potential in addition to its uses in medicinal and insecticidal formulation. Current investigations were aimed to extract and partially characterize the venom of L. terrestris and the susceptibility tests to evaluate antibacterial potential of venom supernatant and venom pellets against four pathogenic bacterial strains i.e., Gram negative Acinetobacter sp. and Pasteurella sp. and Gram Positive Staphylococcus sp. and Streptococcus sp. Results of this study revealed that the venom of L. terrestris contained six relatively high molecular weight peptides ranging from 125 kDa to 35 kDa. Moreover, results of the susceptibility test confirmed the bacteriostatic action of venom supernatant against aerobic Gram negative Acinetobacter sp. in dose dependent manner. A reduced trend of bacteriostatic inhibition was also observed for venom pellets against Acinetobacter sp