Impact of structural stability of cold adapted Candida antarctica lipase B (CaLB): in relation to pH, chemical and thermal denaturation
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F15%3A00087271" target="_blank" >RIV/00216224:14740/15:00087271 - isvavai.cz</a>
Výsledek na webu
<a href="http://pubs.rsc.org/en/content/articlepdf/2015/ra/c4ra17093h" target="_blank" >http://pubs.rsc.org/en/content/articlepdf/2015/ra/c4ra17093h</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1039/c4ra17093h" target="_blank" >10.1039/c4ra17093h</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Impact of structural stability of cold adapted Candida antarctica lipase B (CaLB): in relation to pH, chemical and thermal denaturation
Popis výsledku v původním jazyce
The effect of pH on the conformational behavior of Candida antartica lipase B (CaLB) has been monitored by spectroscopic and calorimetric studies. The results obtained from far and near-UV CD, intrinsic fluorescence and ANS binding studies indicate thatCaLB exhibits the characteristic properties of a molten globule in acidic (protonated) conditions at pH 1.4. The molten globule state retained about 67% of its secondary structure with a substantial loss of tertiary structure at pH 1.4. Moreover, equilibrium unfolding studies indicated that the 'molten-globule-like' state unfolds in a non-cooperative manner and is thermodynamically less stable than that of the native state. The molten globule possessed a slightly higher Rh than its native state. The DSCthermogram shows a high heat signal at pH 7.4, and a low heat signal at pH 2.6, and suggests that CaLB is likely to have undergone structural changes during the thermal unfolding. However partially unfolded CaLB at pH 1.
Název v anglickém jazyce
Impact of structural stability of cold adapted Candida antarctica lipase B (CaLB): in relation to pH, chemical and thermal denaturation
Popis výsledku anglicky
The effect of pH on the conformational behavior of Candida antartica lipase B (CaLB) has been monitored by spectroscopic and calorimetric studies. The results obtained from far and near-UV CD, intrinsic fluorescence and ANS binding studies indicate thatCaLB exhibits the characteristic properties of a molten globule in acidic (protonated) conditions at pH 1.4. The molten globule state retained about 67% of its secondary structure with a substantial loss of tertiary structure at pH 1.4. Moreover, equilibrium unfolding studies indicated that the 'molten-globule-like' state unfolds in a non-cooperative manner and is thermodynamically less stable than that of the native state. The molten globule possessed a slightly higher Rh than its native state. The DSCthermogram shows a high heat signal at pH 7.4, and a low heat signal at pH 2.6, and suggests that CaLB is likely to have undergone structural changes during the thermal unfolding. However partially unfolded CaLB at pH 1.
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
CE - Biochemie
OECD FORD obor
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Návaznosti výsledku
Projekt
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Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2015
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
RSC Advances
ISSN
2046-2069
e-ISSN
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Svazek periodika
5
Číslo periodika v rámci svazku
26
Stát vydavatele periodika
GB - Spojené království Velké Británie a Severního Irska
Počet stran výsledku
17
Strana od-do
20115-20131
Kód UT WoS článku
000350220400039
EID výsledku v databázi Scopus
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