4 research outputs found

    Influence of Levan on the Thermally Induced Gel Formation of β-Lactoglobulin

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    In this study, the influence of levan on the phase behavior and the thermally induced gelation of the mixed β-lactoglobulin—levan gels as a function of polymer content, molecular weight and ionic strength was characterized. For this purpose, rheology was used to study the mechanical properties of the gels and the water binding of the network structure was investigated by time domain nuclear magnetic resonance. Phase behavior and network type were analyzed by optical observation and electron microscopy. Levan enhanced the aggregation and gel formation of β-lg due to segregative forces between the polymer species. Segregation was caused by the excluded volume effect and was more pronounced at lower ionic strength, higher levan contents and higher levan molecular weights. The presence of levan increased the water binding of the gel networks. However, this effect decreased with increasing levan content. At high ionic strength and high levan content, phase separated gels were formed. While segregative forces enhanced network formation, and therefore, increased the gel strength of mixed gels at low ionic strength, levan had also antagonistic effects on the network formation at high ionic strength and high polymer contents

    Sublingual sufentanil for postoperative pain relief: First clinical experiences

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    Background: The sublingual sufentanil tablet system (SSTS) is a novel hand-held patientcontrolled analgesia device developed for treatment of moderate-to-severe postoperative pain. Here we present the first results of its clinical use. Methods: Adult patients undergoing major surgery in five hospitals in the Netherlands received the SSTS for postoperative pain relief as part of multimodal pain management that further included paracetamol and a nonsteroidal anti-inflammatory drug (NSAID). The following variables were collected: postoperative pain scores using the 11-point numerical rating score (NRS) at rest, number of tablets used, occurrence of nausea, and patient satisfaction scores. Results: We included 280 patients in the study; the majority underwent laparoscopic abdominal (49%) or orthopedic (knee replacement) surgery (34%). The median NRS was 3.5 (interquartile range 2.3–4.0) on the day of surgery, 3.3 (2.3–4.0) on the first postoperative day, and 2.8 (2.0–4.0) on the second postoperative day; pain scores did not differ between surgery types. Mean number of tablets used was 19 (range 0–86). Nausea occurred in 34% of patients, more often in women (45% vs 19%). Overall satisfaction was high in 73% of patients. Satisfaction was correlated with pain relief (p < 0.001) and inversely correlated with occurrence of nausea (p=0.01). Discussion: In this data set obtained under real-life conditions we show that the SSTS effectively managed postoperative pain in abdominal and orthopedic surgeries. Future studies should determine patient populations that benefit most from the SSTS, assess the added values versus intravenous patient-controlled analgesia, and determine the pharmacoeconomics of the system

    Conformational state and charge determine the interfacial film formation and film stability of β-lactoglobulin

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    The mechanical stability of protein-stabilized emulsions depends on physiochemical interactions within the interfacial protein film. However, intermolecular interactions vary with the protein's conformational state and charge and may in turn affect the mechanical stability through modifications in the three-staged interfacial stabilization; migration, adsorption and film formation at the oil/water-interface. Therefore, the aim of our study was to investigate the different protein conformations within the interfacial stabilization process by applying bulk water conditions and to determine the protein film stability against mechanical stress. For this purpose, we analyzed the structure and interactions of β-lactoglobulin in water and at the oil/water-interface at pH 7, pH 7NaCl (containing 100 mM NaCl) and pH 9 with membrane-osmometry, Fourier-transform-infrared-spectroscopy, extrinsic fluorescence and ζ-potential. Moreover, we characterized the conformational state and charge in context with the molecule density and interfacial film properties via Langmuir trough analysis, interfacial shear and dilatational rheology. Distinct unfolding of monomers and dimers at pH 9 resulted in the lowest interfacial molecule density but at the same time the highest film stability due to pronounced structural flexibility. In comparison, β-lactoglobulin at pH 7 was monomeric, unfolding was less pronounced, and interfacial molecule density was higher. Electrostatic shielding of β-lactoglobulin dimers at pH 7NaCl resulted in the highest density but least stable protein film that approached low molecular weight surfactant behavior due to few and weak intermolecular interactions. Our research contributes to the control of the emulsion stability against mechanical stress by varying intermolecular interactions within the interfacial protein film
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