Protein Agglomeration Research Articles

Biodegradable active composite film based on pea protein isolate, sage seed gum, and cumin essential oil: Fabrication and characterization

The present study perused the physicochemical, mechanical, thermal, barrier, and optical properties of pea protein isolate (PPI)-Sage seed gum (SG) (3:1, 1:1, and 1:3) composite films incorporated with cuminum essential oil (CEO, 0, 1, and 2 %). Results indicated that the thickness, contact angle (CA), yellowness index (a*), total color differences (∆E), and opacity (OP) significantly enhanced with increasing PPI portion and CEO concentration (p < 0.05), as well as heterogeneous and inconsistent structure were increased in film surface due to protein agglomeration and oil droplets. However, the moisture content (MC), water solubility (WS), and swelling ratio (SR) decreased. Results also indicated that the antioxidant property significantly increased (P < 0.05) following the increase in CEO concentration. The highest tensile strength (TS) and elastic modulus (EM) and the least elongation at break (EAB) in PPI 3-SG 1–0 % were estimated. The potential antimicrobial property of CEO containing film was confirmed, and the maximum inhibition zone for E.coli, S.aureus, C.albicans, and A.niger were measured in film containing 2 % CEO. The barrier properties of the film against water and oxygen (WVP, OXP) diminished with increases the SG ratios, due to the hydrophilic nature of SG. The FTIR analysis identified the functional groups in film components and the interaction between film components. The DSC thermogram indicated the thermal stability of films and the highest decomposition temperature in PPI 3-SG 1–2 % film. XRD revealed a semi-crystalline structure of biopolymer active films. With the increase of SG portion and CEO concentration, the crystallinity of the films was enhanced. Results also indicated that prepared films were more than 90 % biodegradable.

Sodium Phenylbutyrate and Tauroursodeoxycholic Acid: A Story of Hope Turned to Disappointment in Amyotrophic Lateral Sclerosis Treatment.

The absence of a definitive cure for amyotrophic lateral sclerosis (ALS) emphasizes the crucial need to explore new and improved treatment approaches for this fatal, progressive, and disabling neurodegenerative disorder. As at the end of 2023, five treatments - riluzole, edaravone, dextromethorphan hydrobromide + quinidine sulfate (DHQ), tofersen, and sodium phenylbutyrate-tauroursodeoxycholic acid (PB-TUDCA) - were FDA approved for the treatment of patients with ALS. Among them PB-TUDCA has been shown to impact DNA processing impairments, mitochondria dysfunction, endoplasmic reticulum stress, oxidative stress, and pathologic folded protein agglomeration defects, which have been associated with ALS pathophysiology. The Phase 2 CENTAUR trial demonstrated significant impact of PB-TUDCA on the ALS Functional Rating Scale-Revised (ALSFRS-R) risk of death, hospitalization, and the need for tracheostomy or permanent assisted ventilation in patients with ALS based on post hoc analyses. More recently, contrasting with the CENTAUR trial results, results from the Phase 3 PHOENIX trial (NCT05021536) showed no change in ALSFRS-R total score at 48 weeks. Consequently, the sponsor company initiated the process with the USFDA and Health Canada to voluntarily withdraw the marketing authorizations for PB-TUDCA. In the present article, we review ALS pathophysiology, with a focus on PB-TUDCA's proposed mechanisms of action and recent clinical trial results and discuss the implications of conflicting trial data for ALS and other neurological disorders.

Rapid quantification models for assessing melamine adulteration in sport nutrition supplements via benchtop and portable NIRS instruments

Sport nutrition supplements (SNS) are vulnerable to adulteration with melamine, artificially augmenting their protein content as determined by conventional assay methodologies. Vibrational spectroscopy techniques are suitable for the detection of adulteration because they allow rapid analysis, require minimal sample preparation, and can perform numerous analyses in a short time. The aim of this study was to develop rapid quantification models for the determination of melamine adulteration in a variety of SNS matrices using NIRS (near-infrared spectroscopy) in combination with multivariate data processing. Moreover, a comparison of benchtop and portable NIR instruments was carried out. Employing a stepwise approach involving OPLS-DA and PLS analysis, matrix discrimination and prediction ability were investigated. The benchtop instrument effectively discriminated among matrices (R2Y = 0.964, Q2 = 0.933), while the portable device, although showing a slightly altered pattern, maintained favorable discrimination capability (R2Y = 0.966, Q2 = 0.931). The quantitative PLS models for each SNS matrix exhibited comparable statistical indicators for both instruments with reasonable errors for melamine content estimation and prediction (RMSEE: 0.3–2.4 %, RMSEP: 0.98–2.99 %). Higher estimation and prediction errors were observed for protein-containing samples in both acquisition modes, probably due to the tendency of protein agglomeration and adhesion to different surfaces, which affects the homogeneity of the powder. Despite data loss due to the narrower spectral range and lower resolution of the portable instrument, all models were found to be suitable for predicting melamine content in sport nutrition supplements.

The LOV-domain blue-light receptor LreA of the fungus Alternaria alternata binds predominantly FAD as chromophore and acts as a light and temperature sensor

Light and temperature sensing are important features of many organisms. Light may provide energy but may also be used by non-photosynthetic organisms for orientation in the environment. Recent evidence suggests that plant and fungal phytochrome and plant phototropin serve dual functions as light and temperature sensors. Here we characterized the fungal LOV-domain blue-light receptor LreA of Alternaria alternata and show that it predominantly contains FAD as chromophore. Blue-light illumination induced ROS production followed by protein agglomeration in vitro. In vivo ROS may control LreA activity. LreA acts as blue-light photoreceptor but also triggered temperature-shift induced gene expression. Both responses required the conserved amino acid cysteine 421. We therefore propose that temperature mimics the photoresponse, which could be the ancient function of the chromoprotein. Temperature-dependent gene expression control with LreA was distinct from the response with phytochrome suggesting fine-tuned, photoreceptor-specific gene regulation.

Development of value-added beverages using sheep and goat cheese whey and secondary whey

Fermented (F) and neutral (non-fermented) (N) beverages were developed to add value to cheese whey (CW) and secondary whey (SW) from goat (G) and sheep (S) cheese. All products were microbiologically safe. Regarding physical stability, sedimentation of 3–20% was observed, with higher values at the beginning of storage for SW beverages (P < 0.05) due to protein agglomeration (explained by the 22%-larger size of small particles, P < 0.05). F beverages exhibited pseudoplastic behavior (n < 0.8) and higher apparent viscosity (napp). Sensory evaluation showed that the ingredients/additives used masked the unpleasant taste of whey; however, N samples were preferred due to coffee and sweet/vanilla flavors (P < 0.05). The overall results indicated that treatment (N or F) overcame any differences observed in relation to animal source (G or S) or whey type (CW or SW) and that, for the fermented samples, the animal source was more important than the type of whey.

Heat-induced agglomeration of water-soluble cod proteins toward gelled structures

Cod proteins (CPs) have potential applications in designing desirable gel-based products, and this study aimed to unravel their heat-induced aggregation pattern and further probe the roles in protein gels. SDS-PAGE analysis indicated that high-precipitation-coefficient aggregates (HPCAs) of CPs aggregates were composed of considerable polymers of myosin heavy chains and actin, and their low-precipitation-coefficient aggregates (LPCAs) contained myosin light chains and tropomyosin. Studies from correlation analysis between the structure and aggregation kinetics revealed that the generation of β-sheet and SS bonds were responsible for their spontaneous thermal aggregation induced by heating temperature and protein concentration, respectively. Additionally, as protein denaturation ratio increased, more and larger HPCAs were formed, which was evidenced driving the network formation of protein gels and resulting in higher storage modulus (G') values. These novel findings may be applicable to other animal proteins for better tailoring the manufacturing of muscle gel-based products.

Gamma radiation vs high pressure pretreatment on physicochemical characteristics of rice bran hydrolysate

This study investigated the effect of using gamma radiation and high-pressure processing as pretreatment, to consider the structural and amino acid composition changes in rice bran hydrolysate (RBH). The extraction yield and degree of hydrolysis of the irradiated sample were greater than those of the pressurized and control samples, which radiation at 10 kGy gave 31 % yield. Protein content of the control was the highest at 36.1 %, with 32.4 % in pressurized sample at 500 MPa. Control had the highest concentration of total and branched-chain amino acids, with a value of 25,834 mg/100g. Before and after extraction, the microstructure changed visibly and protein agglomeration can be significantly induced by applying a high-pressure. Therefore, this study showed the potential of using both pretreatment methods prior to enzymolysis extraction, with radiation producing more extract. High-pressure produced more protein content, but neither method produced any difference in amino acid content.

Operando spectroscopy investigations of the redox reactions in heme and heme-proteins.

Operando spectroscopic investigations during molecular redox processes provide unique insights into complex molecular structures and their transformations. Herein, a combination of a potentiodynamic method with spectroscopy has been employed to holistically investigate the structural transformations during Fe-redox (Fe3+ ↔ Fe2+) of hemin vis á vis heme-proteins, e.g. myoglobin (Mb), hemoglobin (Hb) and cytochrome-C (Cyt-C). The UV-vis findings reveal the formation of hemozoin (≈heme-dimer), which can be selectively prevented via a high concentration of strongly interacting ligands, e.g. histidine (the fifth coordinating ligand in the heme-based protein). On the other hand, methionine does not prevent the formation of hemozoin. In Mb, Hb, and Cyt-C, as the fifth coordination site is occupied by histidine, hemozoin formation is inhibited. During Fe3+→ Fe2+, operando circular dichroism exhibits a decrease in the initial helical component in Hb from nearly 40% to 28%, which is close to the initial helix component of Mb (≈25%), strongly indicating denaturation of the protein in the redox pathway. The rate of change of the helices versus potential is almost identical for Mb and Hb, but comparatively faster than Cyt-C. In addition, from the Raman bands of M-N dynamics and protein agglomeration, it is concluded that Cyt-C prefers to agglomerate in the 2+ state, whereas Mb/Hb in the 3+ state. In this report, the power of operando spectroscopy is utilized to unearth the dynamics of hemin and heme-based proteins for comprehending the underlying complexities associated with the molecular redox, which have deep implications in electrocatalysis, energy storage, and sensing.

Effect of different salts on the foaming properties of model protein systems for infant formula

This multiscale study aimed to evaluate the effects of different salts (NaCl, KCl, MgCl2, and CaCl2) on the foaming capacity (FC) and foam stability (FS) of model protein systems (MPS) for infant formula via changes in surface and structural properties. Our results showed that the FC and FS of MPS were increased with the addition of NaCl, KCl, and MgCl2, whereas CaCl2 significantly decreased FC (79.5 ± 10.6%) and increased FS (93.2 ± 2.2%). The surface hydrophobicity was increased and the net charge and surface tension were reduced after the addition of salts. Structural analysis revealed the reduction of intensity of intrinsic fluorescence spectroscopy and UV absorption, and the conversion of α-helix into β-strand, which was attributed to protein agglomeration. Additionally, MgCl2 and CaCl2 exhibited larger size and lower net charge compared with NaCl and KCl, indicating a greater ability to bind to charged amino acids and form larger aggregates. Correlation analysis indicated that FC was positively related to adsorbed protein and β-turn and negatively correlated with particle size. In addition, FS showed a positive correlation with β-strand, apparent viscosity, and zeta potential. However, it exhibited a negative correlation with β-turn, α-helix, and sulfhydryl content. These results provide a theoretical reference for further understanding of the effect of salts on the foaming properties of MPS.

Hemoglobin-BSA separation and purification by internally staged ultrafiltration

Separation and purification of a binary protein mixture having close molecular weights was studied using ultrafiltration (UF) membranes. The binary system of hemoglobin (Hb; MW 64.7 kDa; isoelectric point (pI) 6.8) and bovine serum albumin (BSA; MW 66.4 kDa; pI 4.7) having a molecular weight ratio (MWR) of only 1.03 was studied. It has been demonstrated that the internally staged ultrafiltration (ISUF) technique, which used a stack of three UF membranes without any gaskets/spacers in-between, can yield nearly pure Hb in the permeate from its mixture with BSA in an Amicon® stirred cell. Further, the highest purity of BSA, 99 %, was achieved at a pH 7.8 at 10.66 diavolume. This study achieved these results by avoiding membrane fouling by adjusting the pH of the buffer/solution close to 7.8 and operating at a low applied pressure difference of 10.34 kPa. When pH is at around 7.8, BSA is much more negatively charged than Hb; so BSA was much more strongly repelled by the negatively charged UF membranes. A slight net negative charge on the Hb will affect the permeability of Hb to a small extent through the negatively charged UF membrane. However, this can considerably reduce the attraction between BSA and Hb, avoid higher protein agglomeration and alleviate membrane fouling. Low membrane fouling improved UF membrane performance; the recovery of Hb, retention of BSA, and purification of Hb and BSA show good results. Besides, the reusability of UF membranes by in situ cleaning continued to show good performance even after undergoing regeneration 7 times. The results suggest ISUF technique may be used in practical systems for separating and purifying protein mixtures.

Evaluation of the interactions of typical wood extracts on the bonding performance of soybean-based adhesives

The substitution of environmentally friendly, renewable soybean-based adhesives (SBAs) for formaldehyde-based synthetic resins to produce formaldehyde-free wood composites is of great significance for resource recycling and environmental protection. However, SBA-bonded wood composites often exhibit great variations in bonding properties, due to the diverse interactions of the extractive components in wood. In this study, the extracts of four typical commercial fast-growing timbers were isolated, and their effects on the structures and properties of the SBAs were systematically investigated using FTIR, NMR, TGA, contact angle, buffer capacity, sol–gel test, and plywood evaluation. The analytical data indicated that some of the wood extracts could cause important effects on the bonding properties of the SBAs by impacting the PAE cross-linking capacity and unfolding degree of the globular soybean proteins. Fast-growing hardwood extracts from poplar and eucalyptus timbers containing active groups resulted in increased cross-linking density and improved water resistance of the SBAs. Meanwhile, fast-growing softwood extracts from Chinese fir and Scotch pine containing inert hydrophobic components had slight impacts on PAE cross-linking, but resulted in the agglomeration of unfolded soybean proteins. This formed a weak boundary layer on the wood surface, causing a significant decrease in the water resistance of the SBAs by >35%. These findings presented available analytic approaches of wood extract–SBA interactions and useful guidance for the proper applications of SBAs in the commercial production of wood composites.

Microstructural evolution during acid induced gelation of cow, goat, and sheep milk probed by time-resolved (ultra)-small angle neutron scattering

Milks from small ruminant animals, such as goat and sheep, have gained increasing interest from the industry for the manufacture of various dairy products such as yoghurts. Heat treatment of milk is typically applied to improve the yoghurt texture. Here, time-resolved ultra-small angle neutron scattering (USANS) and small-angle neutron scattering (SANS) were employed to probe in situ the microstructural evolution of cow, goat, and sheep milks in D2O during acidification as affected by the heat treatment. Milk gelation can be envisaged as the progressive aggregation of the building blocks (casein micelles) in a fractal manner, which leads to the formation of micron scaled (∼3–10 μm) protein agglomerates. The heat treatment considerably enhanced the gelation of all milks, which is reflected by a faster increase in the fractal dimensions and aggregate sizes. For all three types of milks, similar final plateau fractal dimensions were observed for unheated (∼2.2–2.4) and heated milks (∼2.4–2.5), suggesting similar mass fractal microstructures in the size range probed by USANS. The final storage modulus after 10 h (G′final) follow the order of heated sheep milk ≈ sheep milk ≈ heated cow milk > cow milk > heated goat milk > goat milk. The colloidal calcium phosphate (CCP) dissolution kinetics tracked by SANS followed a similar trend as the evolution of the sample acidity (pD-value) and are not significantly affected by the types of milk or the heat treatment. This study shows a great potential of using time resolved USANS and SANS to investigate the microstructural evolution of protein aggregation and gelation.

Dextran-coated nanoparticles as immunosensing platforms: Consideration of polyaldehyde density, nanoparticle size and functionality

Magnetic nanoparticles (MNPs) can be used as antibody carriers in a wide range of immunosensing applications. The conjugation chemistry for preparing antibody-MNP bionanohybrids should assure the nanoparticle's colloidal dispersity, directional conformation and high biofunctionality retention of attached antibodies. In this work, peroxidase (HRP) was selected as model target analyte, and stable antibody-MNP conjugates were prepared using polyaldehyde-dextrans as multivalent linkers, also to prevent nanoparticles agglomeration and steric shielding of non-specific proteins. Under the manipulation of the oxidation variables, MNP-conjugated antibody showed the highest Fab accessibility, of 1.32 μmol analyte per μmol antibody, corresponding to 139 μmol aldehyde per gram of nanocarrier (5 mM NaIO4, 4 h). Demonstrating anti-interference advantage up to 10% serum, colorimetric immunoassay gave a detection limit (LOD) of 300 ng mL−1, while electrochemical transduction led to a considerable (680 times) improvement, with a LOD of 0.44 ng mL−1. In addition, polyaldehyde-dextran showed priority over polycarboxylated-dextran as the multivalent antibody crosslinker for MNPs in terms of sensitivity and LOD value, while immunosensors constructed with carboxylated magnetic microbeads (HOOC-MBs) outperformed MNPs-based immunoplatforms. This work sheds light on the importance of surface chemistry (type and density of functional groups) and the dimension (nanosize vs micrometer) of magnetic carriers to conjugate antibodies with better directional orientation and improve the analytical performance of the resulting immunosensors.

Effect of NaCl and CaCl2 concentration on the rheological and structural characteristics of thermally-induced quinoa protein gels

The effect of ionic strength on the heat-induced gelation of quinoa protein isolates (QPI) at pH 7 was investigated. The gelation behaviour and gel strength were characterised by oscillatory rheology. The microstructural characteristics of QPI solutions and gels were probed by ultra-small angle neutron scattering (USANS), small-angle X-ray and neutron scattering (SAXS, SANS), and confocal laser scanning microscopy (CLSM). This suite of techniques provided structural details covering a wide range of length scales from tens of micron to nanometre. It was found that the gelation temperature decreased from 73 °C to 40 °C and the G* (1 Hz) increased from ∼67 Pa to ∼1285 Pa with increasing concentration of NaCl from 0 to 200 mM. A particle size of ∼32 Å and ∼57 Å was identified within the QPI gel containing 0–200 mM NaCl from SAXS and SANS, respectively and whose size decreased upon addition of CaCl2. For all QPI samples, heat treatment promoted protein aggregation on the micron scale, while a larger structural unit (Rg∼ 170 nm) was kept intact as revealed by USANS. A similar mass fractal structure (df = 2) was observed in the QPI gels containing 0–200 mM NaCl, while CaCl2 addition caused the formation of large protein agglomerates (Rg∼2.5–4.0 μm) with a more compact and denser structural organisation (df = 2.5) inside the protein blobs. CLSM showed that the QPI gels containing CaCl2 are prone to phase separation. Overall, this finding shows the thermal gelation behaviour of QPI can be modulated by the ion type and concentration, which is similarly observed in other globular protein systems. These results provide useful information for the design and preparation of quinoa gels for food applications.

Coagulation of turbid wastewater with an active component extracted from Moringa oleifera seeds

ABSTRACT The oil and carbohydrates contained in the Moringa oleifera seeds (MO) are two parameters that inhibit its coagulant potential. Oil extraction and protein purification are therefore necessary to improve its performance. The extraction process to recover the maximum oil yield was carried out using the solvent chloroform: ethanol C: E in a ratio (3:1). At a temperature of 100°C, the yield was higher than 44%. Purification was carried out by salting-in the protein with 1 M NaCl combined with ethanol precipitation and heat treatment. Analysis of the protein powder by the Kjeldahl method revealed 92% pure protein and 14% nitrogen; energy dispersive X-ray (EDX) analysis revealed high percentages of carbon (45%) and oxygen (39%). Scanning electron microscopy (SEM) showed a porous surface, and X-ray diffraction identified a crystalline phase of protein. The isoelectric point of Moringa oleifera protein (MOP) is in the range of pH 6.5–7.5 and its zeta potential varies between −19 mv and + 25.49 mV. It indicates a lower level of dispersion stability, implying a high capacity for protein agglomeration and flocculation. By reducing the zeta potential of water from −16 mv to −1.18 mv after treatment without modifying its pH, the Moringa protein has proven its ability to destabilise organic colloids. Moringa protein as a coagulat aid is effective for high turbidity wastewater with removal up to 86.78% and DOC removal up to 56.52%. The study reveals that coagulation with Moringa protein is a cost-effective alternative since it reduces the quantity of coagulant and time required for wastewater treatment.

Autophagic Dysfunction in Dementia: Scope for Development of Potential Remedies.

Dementia is a diverse category of chronic and progressive disorder, which is commonly associated with a loss of memory, difficulty in judgment, impaired language, cognitive impairment, and various other symptoms that affect a person's daily routine life and social life. Dementia affects about 50 million people around the globe. Dementia exists in varied forms and is associated with various neurodegenerative disorders. Alzheimer's disease is the most common form, which accords for about 60% of thecases. Abnormal agglomeration of proteins in the brain has been linked to the pathogenesis of dementia. Autophagy is a necessary protein clearance mechanism, which is dependent on lysosomes. It is a basic physiological process that performs the crucial function of maintaining protein homeostasis within the cells. The autophagic dysfunction in dementia further complicates the disease by hampering the degradation and removing abnormal pathogenic proteins. In order to understand autophagic dysfunction, it is essential to know the genetics of autophagy as well as the mutations This understanding at the genetic level helps definethe relationship between dementia and autophagic dysfunction for developing the potential remedies for the treatment of dementia.

Influence of Transglutaminase on Glucono-δ-lactone-Induced Soy Protein Gels

Enzymatic cross-linking of proteins can be used to create a variety of foods with appealing textures and facilitate further processing such as slicing or packaging. Transglutaminase (TG), a protein-glutamine-γ-glutamyltransferase, has been used in the production of processed meat and fish products. However, it has a reaction optimum at pH 7 and is therefore typically unsuitable for application in up-and-coming acidic food products such as fermented vegan meat product alternatives. To determine whether a simultaneous addition of slowly acidifying glucono-δ-lactone (GDL) and TG can facilitate protein cross-linking prior to the pH becoming too low, TG and GDL were added separately or in combination to soy protein suspensions composed of 10–15% soy protein concentrates or isolates (SPI). Texture analysis showed that SPI gels at pH 5–6, induced by GDL and TG combined, were harder than only GDL-induced gels and as hard as TG-induced gels at the optimum pH of 7. Decreased tan δ values and confocal laser scanning microscopy images indicated that protein cross-linking had taken place in combined gels. The results suggest an initial network formation induced by TG, which later in the acidification is being supplemented by an agglomeration of proteins due to weakened electrostatic repulsion. Taken together, the combination of slow acidification by GDL and TG addition leads to acidic gels with enhanced textural properties and shelf life.

Effect of ultrasound on mill starch and protein in ultrasound-assisted laboratory-scale corn wet-milling

Ultrasound was applied to facilitate starch-protein separation during ultrasound-assisted laboratory-scale corn wet-milling. The effects of ultrasound on the properties of mill starch and protein were investigated to explore the possible mechanisms in this study. A higher starch yield was obtained with sonication treatment in starch-protein separation (15 min, 200 W) and the results showed that ultrasound did not induce damage to the product starch. The differences in the distribution of water proton transverse relaxation time for mill starch suggested that the interaction between starch granules and protein in mill starch was destroyed. The free sulfhydryl content increased by 37.21% and the disulfide bond content decreased by 43.66% of the separated proteins indicated that ultrasound destroyed the disulfide bonds effectively (p < 0.05). Sonication treatment for longer time or at higher power decreased α-helix and β-turn while increased β-sheet and random coil (p < 0.05). Ultrasound increased surface hydrophobicity and decreased the thermal stability of the protein (p < 0.05). The higher intensity of ultraviolet–visible spectroscopy and ultraviolet-difference absorption spectroscopy indicated the unfolding of protein by sonication treatments. Ultrasound may break down the disulfide bonds and hydrogen bonds of protein molecules, effectively releasing starch from the disintegrated protein agglomerates.

Components interactions and changes at molecular level in maize flour-based blends as affected by the extrusion process. A multi-analytical approach

The aim of this work was to evaluate the influence of partial replacement of maize flour by sub-valuated whole grain flours on the interactions and spatial distribution of the main components of extruded snacks. Non-destructive, fast spectroscopic and microscopic complementary tools were employed. All blends (composed by maize + 25% of pearl millet, red sorghum, quinoa or hairless canary seed) presented lower carbohydrate and lipid contents and higher protein, ash and dietary fiber levels than the control maize extrudates. These compositional changes were reflected in FT-MIR and FT-Raman spectra which also allowed detecting modifications at molecular level, such as protein agglomeration, amylose-lipids complexes formation and surface exposure of carotenoids. Tridimensional distribution and spatial arrangements of the main components in the extruded samples were studied through CLSM and XPS. These properties are related to quality aspects such as lipid oxidation sensitivity and textural properties. The combined FT-MIR, FT-Raman, CLSM and XPS were helpful tools to understand thermo-mechanical modifications of starch, proteins and lipids as a consequence of the extrusion process.

Protease Enzymes: Highlights on Potential of Proteases as Therapeutics Agents

In the era of advancement of biotechnology and molecular biology, the structure, catalytic site specification, role in biochemical processes, and many diseases of an enzyme have been discovered. Enzymes are protein in nature and are formulated in the human body from amino acids. Each enzyme carries its specific functions in the body and has particular substrates to work with. The enzymes are present in the optimal amount in the body to carry out essential functions for life and health. Proteases or proteinases or peptidases are the largest family of proteolytic enzymes whose primary function is cleaving proteins into smaller fragments. Due to their structural and functional diversity, these enzymes carry out many functions, including intracellular protein formation or recycling, nutrient digestion, and immune system cascade formation. Proteases have been used for years commercially in leather industries, in beer industries to prevent agglomeration of proteins, and detergent formulations. Still, in recent years their therapeutic functions have been discovered and utilized in the pharmaceutical industry. They have been used in the curing, diagnosis, and replacement therapies, etc. Proteases with the development of microbiology and protein engineering have been hitting the market now quite frequently as drugs/therapeutic agents. The U.S. FDA (Food and Drug Administration) now has approved various therapies utilizing protease enzymes as a therapeutic entities, and many next-generation or completely new proteases are in clinical development. There are multiple proteases in the development stage of clinical and preclinical trials. The utilization of enzymes has not achieved 100 percent of its potential mainly due to two reasons: the first reason is the economical difficulties in obtaining pure and homogeneous enzymes leading to higher cost issues, and second the immunogenicity, fast degradation, and inactivation in the body by inhibitors and secretions and due to Physiological pH and temperature barriers. The present article attempts to introduce various therapeutic roles of these enzymes and methods to utilize them to the maximum of their potential in the medical/pharmaceutical field.