Relationship between thermal inactivation and conformational change of Yarrowia lipolytica lipase and the effect of additives on enzyme stability

被引：25
作者：
Fu, Dayan [1 ]
Li, Cong [1 ]
Lu, Jike [1 ]
Rahman, Ata ur [1 ]
Tan, Tianwei [1 ]
机构：
[1] Beijing Univ Chem Technol, Coll Life Sci & Technol, Beijing Key Lab Bioproc, Beijing 100029, Peoples R China
来源：
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | 2010年 / 66卷 / 1-2期
关键词：
Inactivation; Conformational change; Stability; Additives; Lipase; CANDIDA-RUGOSA LIPASE; CIRCULAR-DICHROISM; AGGREGATION; ESTERS; ENANTIOSELECTIVITY; IMMOBILIZATION; HYDROLYSIS; RESOLUTION; BEHAVIOR; IMPROVE;
D O I：
10.1016/j.molcatb.2010.04.008
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The relationship between thermal inactivation and conformational changes of Yarrowia lipolytica lipase has been investigated. The enzyme loses activity over 40 degrees C, with a half-life of 0.325 h at 50 degrees C. The thermal inactivation kinetics fits with a first-order expression. The conformational transition from ordered to unfolded structures during thermal denaturation has been studied by fluorescence, circular dichroism (CD), ultraviolet (UV) spectra, and dynamic light-scattering (DLS). The thermal unfolding occurs in three stages where changes in tertiary and secondary structure, are accompanied by molecular aggregation. Additives such as span 85 can prolong the half-life of the lipase by a factor ca. 850 at 50 degrees C. The increase in denaturation temperature is confirmed by differential scanning calorimetry (DSC). (C) 2010 Elsevier B.V. All rights reserved.
引用
收藏
页码：136 / 141
页数：6
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