Chia Nan University of Pharmacy & Science Institutional Repository:Item 310902800/26748
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    標題: Unfolding analysis of the mature and unprocessed forms of Bacillus licheniformis γ-glutamyltranspeptidase
    作者: Hung, Chih-Peng
    Yang, Jia-Ci
    Chen, Jiau-Hua
    Chi, Meng-Chun
    Lin, Long-Liu
    貢獻者: 食品科技系
    關鍵字: Bacillus licheniformis
    γ-Glutamyltranspeptidase
    Autocatalytic processing
    Thermal unfolding
    Chemical denaturation
    日期: 2011-06
    上傳時間: 2013-06-26 15:34:41 (UTC+8)
    出版者: Springer-Verlag
    摘要: Bacillus licheniformis γ-glutamyltranspeptidase (BlGGT) undergoes an autocatalytic process to generate 44.9 and 21.7 kDa subunits; however, a mutant protein (T399A) loses completely the processing ability and mainly exists as a precursor. For a comprehensive understanding of their structural features, the biophysical properties of these two proteins were investigated by circular dichroism and fluorescence spectroscopy. Tryptophan fluorescence and circular dichroism spectra were nearly identical for BlGGT and T399A, but unfolding analyses revealed that these two proteins had a different sensitivity towards temperature- and guanidine hydrochloride (GdnHCl)-induced denaturation. BlGGT and the unprocessed T399A displayed T m values of 61.4°C and 68.1°C, respectively, and thermal unfolding of both proteins was found to be highly irreversible. Fluorescence quenching analysis showed that T399A had a dynamic quenching constant similar to that of the wild-type enzyme. BlGGT started to unfold beyond ∼2.14 M GdnHCl and reached an unfolded intermediate, [GdnHCl]0.5, N − U, at 2.85 M, corresponding to free energy change (ΔG H 2 O ) of 12.34 kcal mol − 1, whereas the midpoint of the denaturation curve for T399A was approximately 3.94 M, corresponding to a ΔG H 2 O of 4.45 kcal mol − 1. Taken together, it can be concluded that the structural stability of BlGGT is superior to that of T399A.
    關聯: Journal of Biological Physics 37(4), pp.463-475
    显示于类别:[ 食品科技系 ] 期刊論文

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