Abstract：
:The stability of enzymes with no reduction in their catalytic activity still remains a critical issue in industrial applications. Naturally occurring osmolytes are commonly used as protein stabilizers. In this study we have investigated the effects of sorbitol and trehalose on the structural stability and activity of Pseudomonas cepacia lipase (PCL), using UV-visible, circular dichroism (CD) and fluorescence spectroscopy. Surface plasmon resonance (SPR) technique was used to trace changes in the refractive index and dielectric constant of the environment. The results revealed that catalytic activity and intrinsic fluorescence intensity of PCL increased in the presence of both osmolytes. Far-UV CD spectra indicated that the protein has undergone some conformational changes upon interacting with these osmolytes. Increasing the concentration of sorbitol led to changes in the refractive index and consequently the dielectric constant of environment; whereas in the case of trehalose, such changes were not significant. Unfavorable interactions of trehalose with protein surface induced higher preferential exclusion from the enzyme-water interface than that of sorbitol. Results of this report could give further insights about the stabilization mechanism of osmolytes.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Azizi A,Ranjbar B,Khajeh K,Ghodselahi T,Hoornam S,Mobasheri H,Ganjalikhany MRdoi
10.1016/j.ijbiomac.2011.06.025subject
Has Abstractpub_date
2011-11-01 00:00:00pages
652-6issue
4eissn
0141-8130issn
1879-0003pii
S0141-8130(11)00272-8journal_volume
49pub_type
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