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Impact of structural stability of cold adapted Candida antarctica lipase B (CaLB): in relation to pH, chemical and thermal denaturation

The result's identifiers

  • Result code in 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>

  • Result on the web

    <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>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Impact of structural stability of cold adapted Candida antarctica lipase B (CaLB): in relation to pH, chemical and thermal denaturation

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2015

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    RSC Advances

  • ISSN

    2046-2069

  • e-ISSN

  • Volume of the periodical

    5

  • Issue of the periodical within the volume

    26

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    17

  • Pages from-to

    20115-20131

  • UT code for WoS article

    000350220400039

  • EID of the result in the Scopus database