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000049011 084__ $$2WoS$$aBiochemistry & Molecular Biology
000049011 1001_ $$0P:(DE-Juel1)VDB58067$$aDuy, C.$$b0$$uFZJ
000049011 245__ $$aThermostability of Irreversible Unfolding alpha-Amylases Analyzed by Unfolded Kinetics
000049011 260__ $$aBethesda, Md.$$bSoc.$$c2005
000049011 300__ $$a37360 - 37365
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000049011 440_0 $$03091$$aJournal of Biological Chemistry$$v280$$x0021-9258
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000049011 520__ $$aFor most multidomain proteins the thermal unfolding transitions are accompanied by an irreversible step, often related to aggregation at elevated temperatures. As a consequence the analysis of thermostabilities in terms of equilibrium thermodynamics is not applicable, at least not if the irreversible process is fast with respect the structural unfolding transition. In a comparative study we investigated aggregation effects and unfolding kinetics for five homologous alpha-amylases, all from mesophilic sources but with rather different thermostabilities. The results indicate that for all enzymes the irreversible process is fast and the precedent unfolding transition is the rate-limiting step. In this case the kinetic barrier toward unfolding, as measured by unfolding rates as function of temperature, is the key feature in thermostability. The investigated enzymes exhibit activation energies (E(a)) between 208 and 364 kJmol(-1) and pronounced differences in the corresponding unfolding rates. The most thermostable alpha-amylase from Bacillus licheniformis (apparent transition temperature, T(1/2) approximately 100 degrees C) shows an unfolding rate which is four orders of magnitude smaller as compared with the alpha-amylase from pig pancreas (T(1/2) approximately 65 degrees C). Even with respect to two other alpha-amylases from Bacillus species (T(1/2) approximately 86 degrees C) the difference in unfolding rates is still two orders of magnitude.
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000049011 650_2 $$2MeSH$$aAnimals
000049011 650_2 $$2MeSH$$aAspergillus oryzae: enzymology
000049011 650_2 $$2MeSH$$aBacillus: enzymology
000049011 650_2 $$2MeSH$$aCircular Dichroism
000049011 650_2 $$2MeSH$$aEnzyme Stability
000049011 650_2 $$2MeSH$$aHot Temperature
000049011 650_2 $$2MeSH$$aKinetics
000049011 650_2 $$2MeSH$$aProtein Denaturation
000049011 650_2 $$2MeSH$$aProtein Folding
000049011 650_2 $$2MeSH$$aSwine
000049011 650_2 $$2MeSH$$aThermodynamics
000049011 650_2 $$2MeSH$$aTransition Temperature
000049011 650_2 $$2MeSH$$aalpha-Amylases: chemistry
000049011 650_2 $$2MeSH$$aalpha-Amylases: metabolism
000049011 650_7 $$0EC 3.2.1.1$$2NLM Chemicals$$aalpha-Amylases
000049011 650_7 $$2WoSType$$aJ
000049011 7001_ $$0P:(DE-Juel1)131961$$aFitter, J.$$b1$$uFZJ
000049011 773__ $$0PERI:(DE-600)1474604-9$$a10.1074/jbc.M507530200$$gVol. 280, p. 37360 - 37365$$p37360 - 37365$$q280<37360 - 37365$$tThe @journal of biological chemistry$$v280$$x0021-9258$$y2005
000049011 8567_ $$uhttp://hdl.handle.net/2128/2652$$uhttp://dx.doi.org/10.1074/jbc.M507530200
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