Keratin: dissolution, extraction and biomedical application

Keratinous materials such as wool, feathers and hooves are tough unique biological co-products that usually have high sulfur and protein contents. A high cystine content (7–13%) differentiates keratins from other structural proteins, such as collagen and elastin. Dissolution and extraction of keratin is a difficult process compared to other natural polymers, such as chitosan, starch, collagen, and a large-scale use of keratin depends on employing a relatively fast, cost-effective and time efficient extraction method. Keratin has some inherent ability to facilitate cell adhesion, proliferation, and regeneration of the tissue, therefore keratin biomaterials can provide a biocompatible matrix for regrowth and regeneration of the defective tissue. Additionally, due to its amino acid constituents, keratin can be tailored and finely tuned to meet the exact requirement of degradation, drug release or incorporation of different hydrophobic or hydrophilic tails. This review discusses the various methods available for the dissolution and extraction of keratin with emphasis on their advantages and limitations. The impacts of various methods and chemicals used on the structure and the properties of keratin are discussed with the aim of highlighting options available toward commercial keratin production. This review also reports the properties of various keratinbased biomaterials and critically examines how these materials are influenced by the keratin extraction procedure, discussing the features that make them effective as biomedical applications, as well as some of the mechanisms of action and physiological roles of keratin. Particular attention is given to the practical application of keratin biomaterials, namely addressing the advantages and limitations on the use of keratin films, 3D composite scaffolds and keratin hydrogels for tissue engineering, wound healing, hemostatic and controlled drug release.info:eu-repo/semantics/publishedVersio

Fungal and bacterial proteases: Characteristics, and opportunities for the processing of plant proteins

The enzymatic hydrolysis of proteins has been successful in improving their functional and bioactive properties. Extensive work has been conducted in applying plant, fungal, and bacterial proteases to animal protein sources (Ryder et al., 2015; Ha et al., 2012). Less work has been conducted examining the effects of fungal and bacterial proteases on plant proteins. This study characterised a range of bacterial and fungal proteases and evaluated the effects of selected bacterial and fungal proteases on a plant protein substrate assay. Commercially available proprietary fungal (FPII, F31K, and F60K), bacterial (HT, 4000 P, BS Conc), and plant (papain) proteases were screened for activity using the BODIPY-FL-Casein substrate. The soluble protein concentration of the protease powders was also assessed using the Bradford method. Based on the results of the screening, one fungal protease (F31K) and one bacterial protease (HT) were selected for further experiments. The selected proteases were then used to hydrolyse brown rice protein powder. The hydrolysis was conducted for up to 120 min at optimal conditions for each respective protease (pH 8.5 at 45 ⁰C, and pH 6 at 65 °C for F31K and HT, respectively). The resulting hydrolsates were evaluated for their soluble protein content using the Bradford method. The breakdown of protein was also visualised using SDS-PAGE. The mean enzyme activities ranged from 3.55×104 to 39.5×104 Δfluo.min-1.mg soluble protein-1 (for FPII and 4000 P, respectively). Both HT and F31K significantly increased (p < 0.05) the soluble protein concentration of the brown rice protein powder (from 0.586 to 2.21 and 3.12 mg/mL for HT and F31K, respectively). SDS-PAGE showed substantially different hydrolysis patterns for each protease over time. This study provides insights into how proteases from non-gut origin may overcome some of the challenges currently faced in the production of alternative proteins

Validation Analysis of the Groundwater Flow and Transport Model of the Central Nevada Test Area

The Central Nevada Test Area (CNTA) is a U.S. Department of Energy (DOE) site undergoing environmental restoration. The CNTA is located about 95 km northeast of Tonopah, Nevada, and 175 km southwest of Ely, Nevada (Figure 1.1). It was the site of the Faultless underground nuclear test conducted by the U.S. Atomic Energy Commission (DOE's predecessor agency) in January 1968. The purposes of this test were to gauge the seismic effects of a relatively large, high-yield detonation completed in Hot Creek Valley (outside the Nevada Test Site [NTS]) and to determine the suitability of the site for future large detonations. The yield of the Faultless underground nuclear test was between 200 kilotons and 1 megaton (DOE, 2000). A three-dimensional flow and transport model was created for the CNTA site (Pohlmann et al., 1999) and determined acceptable by DOE and the Nevada Division of Environmental Protection (NDEP) for predicting contaminant boundaries for the site

Modulatory and Toxicological Perspectives on the Effects of the Small Molecule Kinetin

Plant hormones are small regulatory molecules that exert pharmacological actions in mammalian cells such as anti-oxidative and pro-metabolic effects. Kinetin belongs to the group of plant hormones cytokinin and has been associated with modulatory functions in mammalian cells. The mammalian adenosine receptor (A2a-R) is known to modulate multiple physiological responses in animal cells. Here, we describe that kinetin binds to the adenosine receptor (A2a-R) through the Asn253 residue in an adenosine dependent manner. To harness the beneficial effects of kinetin for future human use, we assess its acute toxicity by analyzing different biochemical and histological markers in rats. Kinetin at a dose below 1 mg/kg had no adverse effects on the serum level of glucose or on the activity of serum alanine transaminase (ALT) or aspartate aminotransferase (AST) enzymes in the kinetin treated rats. Whereas, creatinine levels increased after a kinetin treatment at a dose of 0.5 mg/kg. Furthermore, 5 mg/kg treated kinetin rats showed normal renal corpuscles, but a mild degeneration was observed in the renal glomeruli and renal tubules, as well as few degenerated hepatocytes were also observed in the liver. Kinetin doses below 5 mg/kg did not show any localized toxicity in the liver and kidney tissues. In addition to unraveling the binding interaction between kinetin and A2a-R, our findings suggest safe dose limits for the future use of kinetin as a therapeutic and modulatory agent against various pathophysiological conditions

Identifying and validating MMP family members (MMP2, MMP9, MMP12, and MMP16) as therapeutic targets and biomarkers in kidney renal clear cell carcinoma (KIRC).

Kidney Renal Clear Cell Carcinoma (KIRC) is a malignant tumor that carries a substantial risk of morbidity and mortality. The MMP family assumes a crucial role in tumor invasion and metastasis. This study aimed to uncover the mechanistic relevance of the MMP gene family as a therapeutic target and diagnostic biomarker in Kidney Renal Clear Cell Carcinoma (KIRC) through a comprehensive approach encompassing both computational and molecular analyses. STRING, Cytoscape, UALCAN, GEPIA, OncoDB, HPA, cBioPortal, GSEA, TIMER, ENCORI, DrugBank, targeted bisulfite sequencing (bisulfite-seq), conventional PCR, Sanger sequencing, and RT-qPCR based analyses were used in the present study to analyze MMP gene family members to accurately determine a few hub genes that can be utilized as both therapeutic targets and diagnostic biomarkers for KIRC. By performing STRING and Cytohubba analyses of the 24 MMP gene family members, MMP2 (matrix metallopeptidase 2), MMP9 (matrix metallopeptidase 9), MMP12 (matrix metallopeptidase 12), and MMP16 (matrix metallopeptidase 16) genes were denoted as hub genes having highest degree scores. After analyzing MMP2, MMP9, MMP12, and MMP16 via various TCGA databases and RT-qPCR technique across clinical samples and KIRC cell lines, interestingly, all these hub genes were found significantly overexpressed at mRNA and protein levels in KIRC samples relative to controls. The notable effect of the up-regulated MMP2, MMP9, MMP12, and MMP16 was also documented on the overall survival (OS) of the KIRC patients. Moreover, targeted bisulfite-sequencing (bisulfite-seq) analysis revealed that promoter hypomethylation pattern was associated with up-regulation of hub genes (MMP2, MMP9, MMP12, and MMP16). In addition to this, hub genes were involved in various diverse oncogenic pathways. The MMP gene family members (MMP2, MMP9, MMP12, and MMP16) may serve as therapeutic targets and prognostic biomarkers in KIRC. [Abstract copyright: © 2024 Kunlun et al.

An Update of Lectins from Marine Organisms: Characterization, Extraction Methodology, and Potential Biofunctional Applications

Lectins are a unique group of nonimmune carbohydrate-binding proteins or glycopro-teins that exhibit specific and reversible carbohydrate-binding activity in a non-catalytic manner. Lectins have diverse sources and are classified according to their origins, such as plant lectins, animal lectins, and fish lectins. Marine organisms including fish, crustaceans, and mollusks produce a myriad of lectins, including rhamnose binding lectins (RBL), fucose-binding lectins (FTL), mannose-binding lectin, galectins, galactose binding lectins, and C-type lectins. The widely used method of extracting lectins from marine samples is a simple two-step process employing a polar salt solution and purification by column chromatography. Lectins exert several immunomodulatory functions, including pathogen recognition, inflammatory reactions, participating in various hemocyte functions (e.g., agglutination), phagocytic reactions, among others. Lectins can also control cell prolifer-ation, protein folding, RNA splicing, and trafficking of molecules. Due to their reported biological and pharmaceutical activities, lectins have attracted the attention of scientists and industries (i.e., food, biomedical, and pharmaceutical industries). Therefore, this review aims to update current information on lectins from marine organisms, their characterization, extraction, and biofunctionali-ties. © 2022 by the authors. Licensee MDPI, Basel, Switzerland.Ural Federal University, UrFUThe author O.N.K is grateful to the “Priority 2030” program of the Ural Federal University for support

Mupirocin-resistant Staphylococcus aureus in Africa: a systematic review and meta-analysis

Background Mupirocin is widely used for nasal decolonization of Staphylococcus aureus to prevent subsequent staphylococcal infection in patients and healthcare personnel. However, the prolonged and unrestricted use has led to the emergence of mupirocin-resistant (mupR) S. aureus. The aim of this systematic review was to investigate the prevalence, phenotypic and molecular characteristics, and geographic spread of mupR S. aureus in Africa. Methods We examined five electronic databases (EBSCOhost, Google Scholar, ISI Web of Science, MEDLINE, and Scopus) for relevant English articles on screening for mupR S. aureus from various samples in Africa. In addition, we performed random effects meta-analysis of proportions to determine the pooled prevalence of mupR S. aureus in Africa. The search was conducted until 3 August 2016. Results We identified 43 eligible studies of which 11 (26%) were obtained only through Google Scholar. Most of the eligible studies (28/43; 65%) were conducted in Nigeria (10/43; 23%), Egypt (7/43; 16%), South Africa (6/43; 14%) and Tunisia (5/43; 12%). Overall, screening for mupR S. aureus was described in only 12 of 54 (22%) African countries. The disk diffusion method was the widely used technique (67%; 29/43) for the detection of mupR S. aureus in Africa. The mupA-positive S. aureus isolates were identified in five studies conducted in Egypt (n = 2), South Africa (n = 2), and Nigeria (n = 1). Low-level resistance (LmupR) and high-level resistance (HmupR) were both reported in six human studies from South Africa (n = 3), Egypt (n = 2) and Libya (n = 1). Data on mupR-MRSA was available in 11 studies from five countries, including Egypt, Ghana, Libya, Nigeria and South Africa. The pooled prevalence (based on 11 human studies) of mupR S. aureus in Africa was 14% (95% CI =6.8 to 23.2%). The proportion of mupA-positive S. aureus in Africa ranged between 0.5 and 8%. Furthermore, the frequency of S. aureus isolates that exhibited LmupR, HmupR and mupR-MRSA in Africa were 4 and 47%, 0.5 and 38%, 5 and 50%, respectively. Conclusions The prevalence of mupR S. aureus in Africa (14%) is worrisome and there is a need for data on administration and use of mupirocin. The disk diffusion method which is widely utilized in Africa could be an important method for the screening and identification of mupR S. aureus. Moreover, we advocate for surveillance studies with appropriate guidelines for screening mupR S. aureus in Africa

Upgrading the utilization of brassica wastes: Physicochemical properties and sensory evaluation of fermented brassica stalks

The potential to utilize brassica harvest residue and processing waste to add-value and /or to eliminate environmental concerns through fermentation was investigated. Some physicochemical properties (moisture, protein, ash, acid detergent fibre, vitamin C, total phenolic and amino acids contents, acidity and shear and compression forces) for broccoli and cauliflower stalks before and after fermentation were measured. Considerable vitamin C and total phenolics concentrations were found in fresh broccoli and cauliflower stalks. Fermentation decreased (P < 0.001) vitamin C concentration to about 55% of that found in fresh stalks of broccoli and cauliflower and decreased (P < 0.001) total phenolics concentrations (by 15% and 28% for broccoli and cauliflower, respectively). The results from the sensory analysis indicated that the fermented broccoli and cauliflower stalks may be successful as condiment products for consumers familiar with fermented products