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  • 1
    Electronic Resource
    Electronic Resource
    The deconvolution of multi-state transition DSC curves of biological macromolecules: bovine serum albumin and bovine seminal ribonuclease
    Amsterdam : Elsevier
    Thermochimica Acta 227 (1993), S. 185-195 
    Details
    ISSN: 0040-6031
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0040-6031(93)80261-8
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Starch Gelatinization Kinetics in Bread Dough. DSC investigations on 'simulated' baking processes (2000)
    Springer
    Journal of thermal analysis and calorimetry 61 (2000), S. 411-423 
    Details
    ISSN: 1572-8943
    Keywords: bread baking ; DSC ; starch gelatinization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Starch gelatinization in wheat flour dough of various moisture contents was quantitatively evaluated by means of DSC. The experimental records were worked out in the form of excess heat capacity vs. T traces which were deconvoluted to single out the contribution of starch gelatinization from that of the decomposition of amylose-lipid complexes. The quantitative procedure used put into evidence that a third endothermic process would take place in the dough with a poor moisture content. DSC runs carried out with sealed pans (i.e., at constant moisture level) and open pans (from which some water was free to evaporate) allow simulation of two extreme conditions of a real baking process, namely that relevant to the central core and to superficial layer of a dough loaf, respectively. The extent of starch gelatinization occurred in these conditions was quantitatively assessed. These data were collected at various heating rates and used to define temperature-time-transformation(TTT) diagrams which are useful tools to predict the progress of baking for any given thermal history of the system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1010161216120
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    γ-Radiation Effects on the Thermal Stability of Bovine γ-Globulin (1998)
    Springer
    Journal of thermal analysis and calorimetry 52 (1998), S. 745-751 
    Details
    ISSN: 1572-8943
    Keywords: bovine γ-globulin ; calorimetry ; food irradiation ; γ-radiation ; protein denaturation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Low-dose γ-radiation produces subtle effects on bovine γ-globulin, as revealed by calorimetric investigations carried out on concentrated aqueous solutions. The irradiation rate used seems below the threshold that allows complete protein denaturation; the denaturation temperature, Td, remained unaffected; nonetheless, modifications of the shape of the calorimetric signal reveal that other changes, such as the dissociation of protein oligomers, could take place.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1010154321619
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Theseus: A new software package for the handling and analysis of thermal denaturation data of biological macromolecules (1992)
    Springer
    Journal of thermal analysis and calorimetry 38 (1992), S. 2779-2790 
    Details
    ISSN: 1572-8943
    Keywords: denaturation ; new software package
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Zusammenfassung Bei der Analyse von DSC-Daten der thermischen Zersetzung von biologischen Makromolekülen wurde ein neues Softwarepaket (THESEUS) angewendet. Unter Umgehung der in derartigen Experimenten oft vorkommenden gelegentlichen und systematischen Fehler eignet sich dieses System, um genaue Physikalisch-chemische Informationen zu erhalten. Außerdem kann es zur Verarbeitung von Daten verwendet werden, welche von anderen Instrumenten und Methoden stammen, die thermodynamische, spektroskopische oder andere Daten als Funktion der Temperatur liefern. Da viele der Untersuchungen auf diesem Gebiet Forschungs-Charakter tragen und in der gegen-wärtigen Literatur ständig neue Dekonvolutionsmechanismen beschrieben oder angenommen werden, haben wir dieses leistungsstarke, flexible und allgemein anwendbare Programm geschrieben und umgesetzt, um den Operator in die Lage zu versetzen, jeden Phase des Rechenvorganges kontrollieren und seine eigene Erfahrung benutzen zu können, um den besten Weg zur Lösung unvorhergesehener Probleme zu finden.
    Notes: Abstract A new software package (THESEUS) has been assembled for the analysis of the DSC data, Concerning the thermal denaturation of biological macromolecules. The system is useful to obtain accurate physico-chemical information, bypassing the casual and systematic errors, very common in these experiments. It can also be used for handling data from other instruments and methodologies giving thermodynamic, spectroscopic or other kind of data as a function of temperature. Because many of the researches in this field are of exploratory nature and continuously new unfolding mechanisms are described or hypothesized in the current literature, we have written and assembled this powerful and flexible program of general applicability, in order to put the operator in a position to control each step of the calculation procedure and use his own experience for choosing the better way to solve unexpected problems.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01979752
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  • 5
    Electronic Resource
    Electronic Resource
    Thermal denaturation of ribonuclease T1 a DSC study (1992)
    Springer
    Journal of thermal analysis and calorimetry 38 (1992), S. 2791-2802 
    Details
    ISSN: 1572-8943
    Keywords: microbial Ribonuclease T1 ; denaturation temperature ; enthalphy change ; heat capacity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Zusammenfassung Mittels DSC Mikrokalorimetrie wurde die thermische Denaturierung von mikrobieller Ribonuklease T1 (RNAase T1) als eine Funktion despH-Wertes untersucht. Die mittleren Denaturierungstemperaturen, Enthalpieänderungen und Wärmekapazitätsänderungen von Ribonuklease T1 wurden mit denen von pankreatischer Ribonuklease A (RNAase A) verglichen. Man fand, daß das mikrobielle Protein T1 einen komplizierteren Konformationsübergang zeigt, als die bei Ribonuklease A auftretende einfache Zweizustandsänderung. Es wird weiterhin die Hypothese des Auftretens einer “geschmolzenen Kügelchen” Form diskutiert. Die Konformationsbeständigkeit von RNAase T1 ist bei hohenpH-Werten niedriger als die von RNAase A. Die größte Stabilität von RNAase T1 liegt bei einempH-Wert von etwa 5, während die von RNAase A bei etwapH=8. Bei einempH-Wert von 3.7 wird durch einen reproduzierbaren exothermen Peak das Auftreten einer irreversiblen Aggregation angezeigt. Die Konformationsänderungen von RNAase T1 sind impH-Wertbereich 4.5 bis 7.0 reversibel, die von RNAase A sind irreversibel bei einempH-Wert von mindestens 8.0.
    Notes: Abstract The thermal denaturation of microbial Ribonuclease T1 (RNAase T1) as a function ofpH, was studied by means of DSC microcalorimetry. The midpoint denaturation temperatures, enthalpy changes and heat capacity changes of Ribonuclease T1 were compared with those obtained for pancreatic Ribonuclease A (RNAase A). It was found that the microbial T1 protein undergoes a more complex conformational transition than the simple two-state transition shown by Ribonuclease A. The hypothesis of the presence of a ‘molten globule’ form is discussed. The conformational stability of RNAase T1 is lower than that of RNAase A at highpH values. Indeed, the maximum stability of RNAase T1 occurs atpH ≈ 5, whereas that of RNAase A occurs atpH ≈ 8. AtpH=3.7 an irreversible aggregation phenomenon was indicated by the existence of a reproducible exothermic peak. The conformational transition of RNAase T1 is reversible in the range ofpH 4.5–7.0, whereas it becomes irreversible atpH≥8.0 as for RNAase A.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01979753
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  • 6
    Electronic Resource
    Electronic Resource
    Calorimetric Characterization of Different Yeast Strains in Doughs (1998)
    Springer
    Journal of thermal analysis and calorimetry 52 (1998), S. 753-764 
    Details
    ISSN: 1572-8943
    Keywords: calorimetry ; dough ; microbial growth
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract In this work microbial growth and metabolism of Saccharomyces cerevisiae from three different strains in a bread dough system were investigated by means of SETARAM C80D twin calorimeter in isothermal conditions at various temperatures. The overall calorimetric signal accounts for two main contributions, namely oxidative and anaerobic degradation of substrate. Parallel measurements of the biomass growth N(t), the substrate (maltose) consumption, fermentation gases (CO2) production, dough volume increase, were also performed. Differences were observed between the three yeasts both in the metabolic energetics and growth and metabolism kinetics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1010106405689
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    Paper (German National Licenses)
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