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Stability Differences (stability + difference)
Selected AbstractsImproving the mechanical characteristics of faecal waste in rainbow trout: the influence of fish size and treatment with a non-starch polysaccharide (guar gum)AQUACULTURE NUTRITION, Issue 3 2009A. BRINKER Abstract This study (3 × 2 randomized factorial design) describes differences in the mechanical properties of faeces from rainbow trout of three size classes (small ,40 g, mid-size ,150 g, large ,650 g) and assesses the effects of a non-starch polysaccharide binder (guar gum). Observations made at the macroscopic level were reinforced by rheological measurements of viscosity and elastic modulus. Mid-sized fish excreted mechanically the most stable faeces, roughly twice as stable as those of small fish and three times more stable than faeces from large fish. The addition of 3 g kg,1 of guar gum saw some mechanical characteristics improve by about 700%. Faeces from large- and mid-sized fish were more easily stabilized than those of small fish. Mechanical recovery potential for faecal samples disrupted by water turbulence was determined. Stability differences observed for different fish size had no significant effect but the improvements imparted by guar gum reduced postfiltration effluent load to about 35% for large fish, about 24% for mid-size and about 22% for small fish. Faecal leaching decreased significantly with increasing stability. Guar gum was shown to have significant potential for improving the treatability of fish faecal waste. [source] Xanthan Enhances Water Binding and Gel Formation of Transglutaminase-Treated Porcine Myofibrillar ProteinsJOURNAL OF FOOD SCIENCE, Issue 3 2010Yongbiao Shang ABSTRACT:, In this study, the effect of xanthan on dynamic rheological properties, textural profile, and water binding of transglutaminase (TG)-treated myofibrillar protein (MP) gels was investigated. In experiment 1, MP suspensions (40 mg/mL protein, 0.6 M NaCl) at pH 6.45 with or without 0.05% xanthan were treated with 0%, 0.1%, 0.2%, 0.3%, 0.4%, and 0.5% TG; in experiment 2, MP suspensions (40 mg/mL protein, 0.6 M NaCl) at pHs 6.13, 6.30, 6.45, 6.69 with or without 0.05% xanthan were treated with 0.3% TG. Treated samples were analyzed with differential scanning calorimetry for thermal stability and oscillatory rheometry and Instron penetration tests for gelation properties. The TG treatments lowered the transition temperature (Tm) of MP by as much as 6 °C (P,< 0.05) but increased apparent enthalpy of denaturation. However, there was no detectable thermal stability difference between MP samples with or without xanthan. The shear storage modulus (G,) of MP gels increased markedly upon treatments with ,0.3% TG, and the presence of xanthan further enhanced the gel strength (P,< 0.05). The addition of 0.05% xanthan decreased cooking loss of TG-treated MP gels by 17% to 23% when compared with gels without xanthan at all pH levels evaluated (6.13 to 6.67). Thus, the combination of TG and xanthan offered a feasible means to promote cross-linking and gelation of MP while reducing cooking losses. [source] Drying-induced variations in physico-chemical properties of amorphous pharmaceuticals and their impact on stability (I): Stability of a monoclonal antibody,JOURNAL OF PHARMACEUTICAL SCIENCES, Issue 8 2007Ahmad M. Abdul-Fattah Abstract The present study was conducted to investigate the impact of drying method and formulation on the storage stability of IgG1. Formulations of IgG1 with varying levels of sucrose with and without surfactant were dried by different methods, namely freeze drying, spray drying, and foam drying. Dried powders were characterized by thermal analysis, scanning electron microscopy, specific surface area (SSA) analysis, electron spectroscopy for chemical analysis (ESCA), solid state FTIR, and molecular mobility measurements by both isothermal calorimetry and incoherent elastic neutron scattering. Dried formulations were subjected to storage stability studies at 40°C and 50°C (aggregate levels were measured by size exclusion chromatography initially and at different time points). Both drying method and formulation had a significant impact on the properties of IgG1 powders, including storage stability. Among the drying methods, SSA was highest and perturbations in secondary structure were lowest with the spray-dried preparations. Sucrose-rich foams had the lowest SSA and the lowest protein surface accumulation. Also, sucrose-rich foams had the lowest molecular mobility (both fast dynamics and global motions). Stability studies showed a log-linear dependence of physical stability on composition. Preparations manufactured by "Foam Drying" were the most stable, regardless of the stabilizer level. In protein-rich formulations, freeze-dried powders showed the poorest storage stability and the stability differences were correlated to differences in secondary structure. In stabilizer-rich formulations, stability differences were best correlated to differences in molecular mobility (fast dynamics) and total protein surface accumulation. © 2007 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 96:1983,2008, 2007 [source] Alteration of the disulfide-coupled folding pathway of BPTI by circular permutationPROTEIN SCIENCE, Issue 5 2004Grzegorz Bulaj BPTI, bovine pancreatic trypsin inhibitor; cBPTI, a circular form of BPTI generated by forming a peptide bond between the natural termini; cpBPTI, circularly permuted BPTI. Abstract The kinetics of disulfide-coupled folding and unfolding of four circularly permuted forms of bovine pancreatic trypsin inhibitor (BPTI) were studied and compared with previously published results for both wild-type BPTI and a cyclized form. Each of the permuted proteins was found to be less stable than either the wild-type or circular proteins, by 3,8 kcal/mole. These stability differences were used to estimate effective concentrations of the chain termini in the native proteins, which were 1 mM for the wild-type protein and 2.5 to 4000 M for the permuted forms. The circular permutations increased the rates of unfolding and caused a variety of effects on the kinetics of refolding. For two of the proteins, the rates of a direct disulfide-formation pathway were dramatically increased, making this process as fast or faster than the competing disulfide rearrangement mechanism that predominates in the folding of the wild-type protein. These two permutations break the covalent connectivity among the ,-strands of the native protein, and removal of these constraints appears to facilitate direct formation and reduction of nearby disulfides that are buried in the folded structure. The effects on folding kinetics and mechanism do not appear to be correlated with relative contact order, a measure of overall topological complexity. These observations are consistent with the results of other recent experimental and computational studies suggesting that circular permutation may generally influence folding mechanisms by favoring or disfavoring specific interactions that promote alternative pathways, rather than through effects on the overall topology of the native protein. [source] The Effects of Ligand Exchange and Mobility on the Peroxidase Activity of a Bacterial Cytochrome c upon UnfoldingCHEMBIOCHEM, Issue 4 2005Jonathan A. R. Worrall Dr. Abstract The effect on the heme environment upon unfolding Paracoccus versutus ferricytochrome c-550 and two site-directed variants, K99E and H118Q, has been assessed through a combination of peroxidase activity increase and one-dimensional NMR spectroscopy. At pH 4.5, the data are consistent with a low- to high-spin heme transition, with the K99E mutation resulting in a protein with increased peroxidase activity in the absence of or at low concentrations of denaturant. Furthermore, the mobility of the polypeptide chain at pH 4.5 for the wild-type protein has been monitored in the absence and presence of denaturant through heteronuclear NMR experiments. The results are discussed in terms of local stability differences between bacterial and mitochondrial cytochromes c that are inferred from peroxidase activity assays. At pH 7.0, a mixture of misligated heme states arising from protein-based ligands assigned to lysine and histidine is detected. At low denaturant concentrations, these partially unfolded misligated heme forms inhibit the peroxidase activity. Data from the K99E mutation at pH 7.0 indicate that K99 is not involved in heme misligation, whereas histidine coordination is proven by the data from the H118Q variant. [source] | ||||||||||