FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2010333670> ?p ?o ?g. }

• W2010333670 endingPage "403" @default.
• W2010333670 startingPage "387" @default.
• W2010333670 abstract "The thermal denaturation of β-lactoglobulin solutions (8.5% protein concentration of which 5.8% was β-lactoglobulin) has been studied by differential scanning calorimetry. For solutions of pH between 1.5 and 8, the denaturation temperature Td was maximum at pH 3.5, and the apparent enthalpy change ΔHapp seemed to be constant from pH 1.5 to 6.6, and decreased significantly at pH 8.0. With addition of N-ethylmaleimide (NEM) to the β-lactoglobulin solution (pH 7) in a molar ratio of up to 1:1, the peak temperature Tp increased slightly and then remained constant, for higher molar ratio, while ΔHapp decreased. With addition of dithiolthreithol (DTT), both Tp and ΔHapp decreased drastically. The kinetic parameters of heat denaturation were determined by the Borchardt and Daniels method as a function of pH. At pH 1.5 and 2.5, the denaturation process presented some degree of reversibility which increased with the scan rate of the first heating of the solution. The process could be described as a second-order reaction at pH < pHi and at pH 8.0. It seemed to be a first-order reaction at pH 6.0 and 6.6. In the case of irreversibility of the denaturation process, the half-life time was verified by an isothermic method. The heat-induced gelation properties, the gelation time (heat treatment at 80°C) and gelation temperature (heat treatment from 40 to 90°C at 0.1°C min−1) were studied with an empirical test and an Instron machine, respectively. The addition of NEM (0–20 mM) and DTT (0–32 mM) gave rise to increasing and reducing gelation time (tg) at 80°C, respectively. The onset gelation temperature, determined from the first increase of the apparent Young's modulus, seemed to be lower than that of the denaturation temperature determined by extrapolation to 0.1°C min−1 of peak temperatures obtained at various scan rates. It was higher than that of the onset denaturation temperature, determined from the increasing edge of the heat flow measured at 5°C min−1 (7.5°C for pH 8 solution). The maximum apparent Young's modulus Eapp observed with increasing heat treatment displayed a higher value at pH 6.6. The experimental results are compared to published data, and they are discussed in terms of electrostatic and hydrophobic interactions and of SH/S—S interchange reactions." @default.
• W2010333670 created "2016-06-24" @default.
• W2010333670 creator A5031105496 @default.
• W2010333670 creator A5052893825 @default.
• W2010333670 creator A5074670550 @default.
• W2010333670 date "1994-11-01" @default.
• W2010333670 modified "2023-09-27" @default.
• W2010333670 title "Thermal denaturation and heat-induced gelation properties of β-lactoglobulin. Effects of some chemical parameters" @default.
• W2010333670 cites W1775749144 @default.
• W2010333670 cites W1967756218 @default.
• W2010333670 cites W1972004949 @default.
• W2010333670 cites W1972417941 @default.
• W2010333670 cites W1984178312 @default.
• W2010333670 cites W1984428974 @default.
• W2010333670 cites W1989068883 @default.
• W2010333670 cites W2002060415 @default.
• W2010333670 cites W2006370393 @default.
• W2010333670 cites W2008060944 @default.
• W2010333670 cites W2009189964 @default.
• W2010333670 cites W2015850549 @default.
• W2010333670 cites W2021076937 @default.
• W2010333670 cites W2036475567 @default.
• W2010333670 cites W2037698426 @default.
• W2010333670 cites W2038403595 @default.
• W2010333670 cites W2038475510 @default.
• W2010333670 cites W2044110936 @default.
• W2010333670 cites W2045388610 @default.
• W2010333670 cites W2075238973 @default.
• W2010333670 cites W2084822256 @default.
• W2010333670 cites W2092292432 @default.
• W2010333670 cites W2094879421 @default.
• W2010333670 cites W2121172016 @default.
• W2010333670 cites W2152806395 @default.
• W2010333670 cites W2166186941 @default.
• W2010333670 cites W2167453089 @default.
• W2010333670 cites W2170242301 @default.
• W2010333670 cites W2324220426 @default.
• W2010333670 cites W4211245206 @default.
• W2010333670 doi "https://doi.org/10.1016/0040-6031(94)80104-5" @default.
• W2010333670 hasPublicationYear "1994" @default.
• W2010333670 type Work @default.
• W2010333670 sameAs 2010333670 @default.
• W2010333670 citedByCount "38" @default.
• W2010333670 countsByYear W20103336702012 @default.
• W2010333670 countsByYear W20103336702013 @default.
• W2010333670 countsByYear W20103336702014 @default.
• W2010333670 countsByYear W20103336702016 @default.
• W2010333670 countsByYear W20103336702017 @default.
• W2010333670 countsByYear W20103336702020 @default.
• W2010333670 countsByYear W20103336702021 @default.
• W2010333670 crossrefType "journal-article" @default.
• W2010333670 hasAuthorship W2010333670A5031105496 @default.
• W2010333670 hasAuthorship W2010333670A5052893825 @default.
• W2010333670 hasAuthorship W2010333670A5074670550 @default.
• W2010333670 hasConcept C113196181 @default.
• W2010333670 hasConcept C121332964 @default.
• W2010333670 hasConcept C135502975 @default.
• W2010333670 hasConcept C13965031 @default.
• W2010333670 hasConcept C148898269 @default.
• W2010333670 hasConcept C161790260 @default.
• W2010333670 hasConcept C178790620 @default.
• W2010333670 hasConcept C185592680 @default.
• W2010333670 hasConcept C2776923230 @default.
• W2010333670 hasConcept C2994067411 @default.
• W2010333670 hasConcept C3288061 @default.
• W2010333670 hasConcept C39519442 @default.
• W2010333670 hasConcept C43617362 @default.
• W2010333670 hasConcept C62520636 @default.
• W2010333670 hasConcept C93391505 @default.
• W2010333670 hasConcept C97355855 @default.
• W2010333670 hasConceptScore W2010333670C113196181 @default.
• W2010333670 hasConceptScore W2010333670C121332964 @default.
• W2010333670 hasConceptScore W2010333670C135502975 @default.
• W2010333670 hasConceptScore W2010333670C13965031 @default.
• W2010333670 hasConceptScore W2010333670C148898269 @default.
• W2010333670 hasConceptScore W2010333670C161790260 @default.
• W2010333670 hasConceptScore W2010333670C178790620 @default.
• W2010333670 hasConceptScore W2010333670C185592680 @default.
• W2010333670 hasConceptScore W2010333670C2776923230 @default.
• W2010333670 hasConceptScore W2010333670C2994067411 @default.
• W2010333670 hasConceptScore W2010333670C3288061 @default.
• W2010333670 hasConceptScore W2010333670C39519442 @default.
• W2010333670 hasConceptScore W2010333670C43617362 @default.
• W2010333670 hasConceptScore W2010333670C62520636 @default.
• W2010333670 hasConceptScore W2010333670C93391505 @default.
• W2010333670 hasConceptScore W2010333670C97355855 @default.
• W2010333670 hasIssue "2" @default.
• W2010333670 hasLocation W20103336701 @default.
• W2010333670 hasOpenAccess W2010333670 @default.
• W2010333670 hasPrimaryLocation W20103336701 @default.
• W2010333670 hasRelatedWork W1521626205 @default.
• W2010333670 hasRelatedWork W1981945 @default.
• W2010333670 hasRelatedWork W2005323326 @default.
• W2010333670 hasRelatedWork W2015391817 @default.
• W2010333670 hasRelatedWork W2015850549 @default.
• W2010333670 hasRelatedWork W2046029094 @default.
• W2010333670 hasRelatedWork W2069222920 @default.
• W2010333670 hasRelatedWork W2321183086 @default.

• next