Comparison of the molten globule states of thermophilic and mesophilic alpha-amylases

Biophysical Chemistry
Maryam Monsef ShokriMehdi Sadeghi

Abstract

In recent years great interest has been generated in the process of protein folding, and the formation of intermediates during the folding process has been proven with new experimental strategies. In the present work, we have examined the molten globule state of Bacillus licheniformis alpha-amylase (BLA) by intrinsic fluorescence and circular dichroism spectra, 1-anilino naphthalene-8-sulfonate (ANS) binding and proteolytic digestion by pepsin, for comparison to its mesophilic counterpart, Bacillus amyloliquefaciens alpha-amylase (BAA). At pH 4.0, both enzymes acquire partially folded state which show characteristics of molten globule state. They unfold in such a way that their hydrophobic surfaces are exposed to a greater extent compared to the native forms. Chemical denaturation studies by guanidine hydrochloride and proteolytic digestion with pepsin show that molten globule state of BLA is more stable than from BAA. Results from gel filtration indicate that BAA has the same compactness at pH 4.0 and 7.5. However, molten globule state of BLA is less compact than its native state. The effects of polyols such as trehalose, sorbitol and glycerol on refolding of enzymes from molten globule to native state were also studied. These...Continue Reading

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Aug 11, 2010·Protein Engineering, Design & Selection : PEDS·Khawar Sohail SiddiquiRicardo Cavicchioli
Jun 28, 2008·Biophysical Chemistry·Yan Liu, Rong Guo
Jul 2, 2009·Chemical Biology & Drug Design·Bijan Ranjbar, Pooria Gill
Jul 16, 2019·International Journal of Biological Macromolecules·P Prasanthan, N Kishore

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