| RABBANI, Gulam, Ejaz AHMAD, Mohsin Vahid KHAN, Mohd. Tashfeen ASHRAF, Rajiv BHAT and Rizwan Hasan KHAN. Impact of structural stability of cold adapted Candida antarctica lipase B (CaLB): in relation to pH, chemical and thermal denaturation. RSC Advances. Cambridge: Royal Society of Chemistry, 2015, vol. 5, No 26, p. 20115-20131. ISSN 2046-2069. Available from: https://dx.doi.org/10.1039/c4ra17093h. |
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@article{1342245,
author = {Rabbani, Gulam and Ahmad, Ejaz and Khan, Mohsin Vahid and Ashraf, Mohd. Tashfeen and Bhat, Rajiv and Khan, Rizwan Hasan},
article_location = {Cambridge},
article_number = {26},
doi = {http://dx.doi.org/10.1039/c4ra17093h},
keywords = {MOLTEN GLOBULE STATE; CIRCULAR-DICHROISM; YEAST HEXOKINASE; THIOFLAVIN-T; PROTEIN; ENZYMES; INTERMEDIATE; MICROORGANISMS; CHROMATOGRAPHY; TEMPERATURES},
language = {eng},
issn = {2046-2069},
journal = {RSC Advances},
title = {Impact of structural stability of cold adapted Candida antarctica lipase B (CaLB): in relation to pH, chemical and thermal denaturation},
url = {http://pubs.rsc.org/en/content/articlepdf/2015/ra/c4ra17093h},
volume = {5},
year = {2015}
}
TY - JOUR
ID - 1342245
AU - Rabbani, Gulam - Ahmad, Ejaz - Khan, Mohsin Vahid - Ashraf, Mohd. Tashfeen - Bhat, Rajiv - Khan, Rizwan Hasan
PY - 2015
TI - Impact of structural stability of cold adapted Candida antarctica lipase B (CaLB): in relation to pH, chemical and thermal denaturation
JF - RSC Advances
VL - 5
IS - 26
SP - 20115-20131
EP - 20115-20131
PB - Royal Society of Chemistry
SN - 20462069
KW - MOLTEN GLOBULE STATE
KW - CIRCULAR-DICHROISM
KW - YEAST HEXOKINASE
KW - THIOFLAVIN-T
KW - PROTEIN
KW - ENZYMES
KW - INTERMEDIATE
KW - MICROORGANISMS
KW - CHROMATOGRAPHY
KW - TEMPERATURES
UR - http://pubs.rsc.org/en/content/articlepdf/2015/ra/c4ra17093h
L2 - http://pubs.rsc.org/en/content/articlepdf/2015/ra/c4ra17093h
N2 - 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 that CaLB 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 DSC thermogram 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 1.4 does not produce a DSC peak which proves the existence of the molten globule state at pH 1.4 as supported by spectroscopic data. The Stokes radius of the MG state obtained by SEC experiments is found to be 33% larger than the native state, but essentially smaller than the denatured state.
ER -
RABBANI, Gulam, Ejaz AHMAD, Mohsin Vahid KHAN, Mohd. Tashfeen ASHRAF, Rajiv BHAT and Rizwan Hasan KHAN. Impact of structural stability of cold adapted Candida antarctica lipase B (CaLB): in relation to pH, chemical and thermal denaturation. \textit{RSC Advances}. Cambridge: Royal Society of Chemistry, 2015, vol.~5, No~26, p.~20115-20131. ISSN~2046-2069. Available from: https://dx.doi.org/10.1039/c4ra17093h.
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