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Nanocomposite gels consist of nanoparticles dispersed in a gel matrix. The main aim of this work was to develop nanocomposite gels for topical delivery of Flurbiprofen (FB) for humans and farm animals. Nanocomposite gels were prepared stemming from nanoparticles (NPs) freeze-dried with two different cryoprotectants, D-(+)-trehalose (NPs-TRE) and polyethylene glycol 3350 (NPs-PEG), sterilized by gamma (γ) irradiation, and gelled with Sepigel® 305. Nanocomposite gels with FB-NPs-TRE and FB-NPs-PEG were physiochemically characterized in terms of appearance, pH, morphological studies, porosity, swelling, degradation, extensibility, and rheological behavior. The drug release profile and kinetics were assessed, as well as, the ex vivo permeation of FB was assessed in human, porcine and bovine skin. In vivo studies in healthy human volunteers were tested without FB to assess the tolerance of the gels with nanoparticles. Physicochemical studies demonstrated the suitability of the gel formulations. The ex vivo skin permeation capacity of FB-NPs nanocomposite gels with different cryoprotectants allowed us to conclude that these formulations are suitable topical delivery systems for human and veterinary medicine. However, there were statistically significant differences in the permeation of each formulation depending on the skin. Results suggested that FB-NPs-PEG nanocomposite gel was most suitable for human and porcine skin, and the FB-NPs-TRE nanocomposite gel was most suitable for bovine skin. [ABSTRACT FROM AUTHOR]

Corynebacterium ulceribovis strain IMMIB L-1395(T) (= DSM 45146(T)) is an aerobic to facultative anaerobic, Gram-positive, non-spore-forming, non-motile rod-shaped bacterium that was isolated from the skin of the udder of a cow, in Schleswig Holstein, Germany. The cell wall of C. ulceribovis contains corynemycolic acids. The cellular fatty acids are those described for the genus Corynebacterium, but tuberculostearic acid is not present. Here we describe the features of C. ulceribovis strain IMMIB L-1395(T), together with genome sequence information and its annotation. The 2,300,451 bp long genome containing 2,104 protein-coding genes and 54 RNA-encoding genes and is part of the Genomic Encyclopedia of Type Strains, Phase I: the one thousand microbial genomes (KMG) project.

Two plant enzymes, namely actinidin (A) and papain (P), were used to pretreat bovine skin at the respective optimum pH and temperature of the enzymes for 48 h at the level of 0, 5, 10, 15, 20, and 25 unit/g of skin, and gelatin extraction was done at 60°C for 6 h. Gelatin yield from actinidin at level 20 (A20) (22.67%) and papain at level 20 (P20) (23.59%) were significantly (P

Bovine skin was incubated with plant enzymes bromelain (B) and zingibain (Z) at the level of 0, 5, 10, 15, 20 and 25 unit/g of skin and gelatin was extracted at 60 °C for 6 h. Control gelatin was extracted without enzymatic pretreatment. The yield and gel strength were 17.90% and 283.35 g for the control samples and 22.26% and 160.88 g for B20 samples. The zingibain extracted gelatin (GEZ) samples failed to form gel. Viscosities of GEZ gelatins were significantly (P < 0.05) lower than the gelatins extracted using bromelain (GEB). β and α chains were absolutely degraded in all GEB and GEZ samples. Only smear bands were observed in GEZ gelatins whereas GEB samples revealed presence of low molecular weight polypeptides. Loss of molecular order was noticed in Z5 as elaborated by Fourier transform infrared (FTIR) spectroscopy. Larger particle size, denser and inter-connected irregular network was observed in B20 under scanning electron microscopy. Based on the results obtained, bromelain, particularly at level 20, could be used to obtain a better quality gelatin with higher yield compared to zingibain. [ABSTRACT FROM AUTHOR]

Leather is a high tech material with different application fields, such as automotive, manufacturing of leatherwear articles or clothing and footwear. Leather is a biomaterial obtained by processing animal skins. Unfortunately, raw animal hides are practically inutilizable, due to their microbiological instability and are affected by rotting. Microbiological stability is achieved by tanning, when the protein is crosslinked, followed by drying. After crosslinking and drying, the new material shows the required properties of sustainability, availability and an esthetically pleasing aspect to the touch, making it available across its entire range of applications. From a structural point of view the animal skins are constituted of collagen, which is a fibrilar protein with a high degree of supramolecular organization in triple helix form that endows softness, elasticity and mechanical strength. High quality standards and lack of toxicity are required in all cases. Leather colour changes during exposure to light radiations are considered a consequence of the presence of some products with weak photochemical resistance during fabrication. The study aims to compare changes in properties of leathers obtained using mineral tanning agents such as Cr III salts and those obtained with the more environment-friendly technology using acid hydrolysis. Accelerated aging studies were conducted on tanned leathers by exposing the samples to UV radiation with different irradiation doses and two wavelengths (254 and 365 nm) under controlled humidity and temperature conditions. Structural changes caused by irradiation were studied by FTIR. Colour changes on the sample surfaces were assessed during irradiation with the CIEL a*b* system. The colour parameters variation (L*, a*, b*) and colour differences have been discussed in correlation with structural changes, tanning method and irradiation conditions.

Pepsin enzyme was used to pretreat the bovine skin at the rate of 5, 15, and 25 units of enzyme/g of skin to recover gelatin, and the recovered gelatins were referred to as Pe5, Pe15, and Pe25, respectively. The gelatin yield increased significantly (p < 0.05) from 18.17% for Pe5 to 24.67% for Pe25 as the level of pepsin increased, but the corresponding gel strength and viscosity decreased significantly (p < 0.05) from 215.49 to 56.06 g and 9.17 to 8.17 mPa·s for Pe5 and Pe25, respectively. β- and α1- and α2-chains were degraded entirely in all the gelatins samples as observed in protein pattern elaborated by gel electrophoresis. 1H nuclear magnetic resonance (1H NMR) analysis indicated the coiled structure of gelatin protein chains. The lowest amide III amplitude of Pe25 as found by Fourier transform infrared (FTIR) spectroscopy indicated that α-helix structure of protein chains were lost to more irregular coiled structure. Thus, it could be summarized that pepsin might be used at the lower level (5 units/g of wet skin) to extract gelatin from bovine skin with good functional properties and at higher level (15/25 units/g of wet skin) to obtain gelatin of industrial grade with high yield.

Two plant enzymes, namely actinidin (A) and papain (P), were used to pretreat bovine skin at the respective optimum pH and temperature of the enzymes for 48 h at the level of 0, 5, 10, 15, 20, and 25 unit/g of skin, and gelatin extraction was done at 60°C for 6 h. Gelatin yield from actinidin at level 20 (A20) (22.67%) and papain at level 20 (P20) (23.59%) were significantly (P < 0.05) higher than control (17.90%). The gel strength values for gelatin extracted using actinidin enzyme (GEA) were significantly (P < 0.05) higher than the control (283.35 g), and the gel strength for A20 was 366.39 g. However, gelatin extracted using papain enzyme (GEP) showed relatively lower gel strength. The GEA sample viscosities were significantly (P < 0.05) higher than control (12.10 mPa.s). GEA samples revealed overall degradation of β chains and presence of α chains and lower molecular weight peptides, whereas β and α chains were completely absent and lower molecular weight peptides were seen in all the GEP samples. Fourier-transform infrared (FTIR) spectra indicated a greater loss of molecular order and more disruption in the α helical structure of P20 compared to A20 and control gelatins. Scanning electron microscopy (SEM) revealed interconnected bigger particle size and denser structure with least number of voids in A20 than P20 and control gelatin samples. Thus, it was concluded that actinidin, particularly at level 20 unit/g of skin, could be used to improve the yield and properties of gelatin from bovine skin. [ABSTRACT FROM AUTHOR]

In today's move to "sustainable production" the leather industry, as well as many other industries is recognized as a polluting one. Traditional chemical operations are polluting because of the levels of inorganic chemical waste. Process chemicals which are not consumed within the reactions necessary to convert collagen to leather are currently discharged to waste. These are usually applied during bulk production, such as inorganic agents from beam house and tanning processes, e.g. lime, sulphide, ammonium salts, sulphuric acid and sodium chloride, mineral tanning agents – mainly Cr(III) and the less common Al(III), Zr(III), Ti(III), Fe(III) salts -, whereas depending on the tanning process and the leather article produced organic chemical waste discharged comprises aldehydic and polyphenolic tanning products, bating enzymes, organic carboxylic acids and excess electrolyte stable synthetic fat liquors. It is rare for chemicals and water to be recovered for re-use from several of these process steps. Moreover, tanners worldwide are required to operate within strict legislative boundaries. Serious drawbacks continuously arise concerning the chrome–tanning process in leather industry and the environmental hazardous consequences of chromium containing effluents. In order to overcome this impediment, a great deal of research has been focused on developing chrome–free tanning methods in the past years, such as titanium tanning. In the present study, Ti–Al tanned bovine leather was characterized by means of SEM microscopy, EDAX elemental analysis, ATR–FTIR spectroscopy, thermogravimetry TGA, and differential scanning calorimetry DSC techniques.

The autolysis of pretreated bovine skin (PBS) (treated with 0.1 M NaOH and 1% HCl), its endogenous proteases, inhibitors and their effects on quality attributes of gelatin were examined. PBS was subjected to different temperatures (20–90 °C) and pH (2–9) and treated with different protease inhibitors. Maximum autolytic activity of PBS was observed at 40 °C and pH 5. Ethylene-bis (oxyethylenenitrilo) tetraacetic acid (EGTA) was the most effective in impeding the degradation of γ-, β- and α- chains of PBS protein indicating that metallocollagenases were the predominant endogenous proteases in bovine skin. Gelatin was extracted in the absence (GAE) and presence (GPE) of EGTA, and EGTA with papain enzyme (GPEP). GPEP had a higher yield and lower gel strength than GEA and GPE. Metallocollagenases partook in the degradation of gelatin thereby affecting its functional properties. Pretreating PBS with or without EGTA, and papain influenced the quality attributes of gelatin. [ABSTRACT FROM AUTHOR]

Corynebacterium ulceribovis strain IMMIB L-1395T (= DSM 45146T) is an aerobic to facultative anaerobic, Gram-positive, non-spore-forming, non-motile rod-shaped bacterium that was isolated from the skin of the udder of a cow, in Schleswig Holstein, Germany. The cell wall of C. ulceribovis contains corynemycolic acids. The cellular fatty acids are those described for the genus Corynebacterium, but tuberculostearic acid is not present. Here we describe the features of C. ulceribovis strain IMMIB L-1395T, together with genome sequence information and its annotation. The 2,300,451 bp long genome containing 2,104 protein-coding genes and 54 RNA-encoding genes and is part of the Genomic Encyclopedia of Type Strains, Phase I: the one thousand microbial genomes (KMG) project. [ABSTRACT FROM AUTHOR]

Corynebacterium ulceribovis strain IMMIB L-1395T (= DSM 45146T) is an aerobic to facultative anaerobic, Gram-positive, non-spore-forming, non-motile rod-shaped bacterium that was isolated from the skin of the udder of a cow, in Schleswig Holstein, Germany. The cell wall of C. ulceribovis contains corynemycolic acids. The cellular fatty acids are those described for the genus Corynebacterium, but tuberculostearic acid is not present. Here we describe the features of C. ulceribovis strain IMMIB L-1395T, together with genome sequence information and its annotation. The 2,300,451 bp long genome containing 2,104 protein-coding genes and 54 RNA-encoding genes and is part of the Genomic Encyclopedia of Type Strains, Phase I: the one thousand microbial genomes (KMG) project. [ABSTRACT FROM AUTHOR]

The main objective of this research is to perform the biomechanical testing on bovine skin. This paper attempts to highlight the success in determining the biomechanical properties and its comparison of three categories of bovine skin via experimental-numerical integration. Initially, four samples for each category of bovine skin were stretched using a mechanical tensile test machine (category 1: I-shape with hair; 2: I-shape shaved and 3: rectangular shape). Concurrently, a stress-stretch equation was re-derived based from the Ogden's constitutive equation and a Matlab Program was written as a tool to quantify the biomechanical properties. Finally, the findings show the Ogden constitutive parameters (biomechanical properties) in terms of μ (Pa) and α for the three categories I-shape with hair, I-shape-shaved and rectangular shape. The quantified values were (0·023 Pa, 17·78); (0·040 Pa, 13·55) and (0·029 Pa, 12·5), respectively. Thus, the results obtained were in close agreement with the results reported by other researchers. [ABSTRACT FROM AUTHOR]

Pepsin enzyme was used to pretreat the bovine skin at the rate of 5, 15, and 25 units of enzyme/g of skin to recover gelatin, and the recovered gelatins were referred to as Pe5, Pe15, and Pe25, respectively. The gelatin yield increased significantly (p < 0.05) from 18.17% for Pe5 to 24.67% for Pe25 as the level of pepsin increased, but the corresponding gel strength and viscosity decreased significantly (p < 0.05) from 215.49 to 56.06 g and 9.17 to 8.17 mPa·s for Pe5 and Pe25, respectively. β- and α1- and α2-chains were degraded entirely in all the gelatins samples as observed in protein pattern elaborated by gel electrophoresis. 1H nuclear magnetic resonance (1H NMR) analysis indicated the coiled structure of gelatin protein chains. The lowest amide III amplitude of Pe25 as found by Fourier transform infrared (FTIR) spectroscopy indicated that α-helix structure of protein chains were lost to more irregular coiled structure. Thus, it could be summarized that pepsin might be used at the lower level (5 units/g of wet skin) to extract gelatin from bovine skin with good functional properties and at higher level (15/25 units/g of wet skin) to obtain gelatin of industrial grade with high yield. [ABSTRACT FROM AUTHOR]

Corynebacterium ulceribovis strain IMMIB L-1395(T) (= DSM 45146(T)) is an aerobic to facultative anaerobic, Gram-positive, non-spore-forming, non-motile rod-shaped bacterium that was isolated from the skin of the udder of a cow, in Schleswig Holstein, Germany. The cell wall of C. ulceribovis contains corynemycolic acids. The cellular fatty acids are those described for the genus Corynebacterium, but tuberculostearic acid is not present. Here we describe the features of C. ulceribovis strain IMMIB L-1395(T), together with genome sequence information and its annotation. The 2,300,451 bp long genome containing 2,104 protein-coding genes and 54 RNA-encoding genes and is part of the Genomic Encyclopedia of Type Strains, Phase I: the one thousand microbial genomes (KMG) project.