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Table 1 Hydrodynamic and spectroscopic properties of purified rThBgl

From: Crystal structure and biochemical characterization of the recombinant ThBgl, a GH1 β-glucosidase overexpressed in Trichoderma harzianum under biomass degradation conditions

Technique Property
Predicted hydrodynamic dataa MMpred = 53.24 kDa
R 0 = 25.15 Å
Analytical SEC MMapp = 54.72 ± 3 kDa
R s = 31.39 Å
ƒ/ƒ b0  = 1.25 ± 0.2
AUCc \(S_{20,w}^{0}\) = 4.53 ± 0.03 S
MMexp = 58.26 ± 7 kDa
ƒ/ƒ 0 = 1.23 ± 0.05
CDd α-Helix = 35 ± 4 %
β-Sheet = 10 ± 2 %
CD thermal-induced unfolding Tm = 49 ± 1 °C
Fluorescence λ rThBgl−foldedmax  = 334 ± 1 nm
〈λ〉rThBgl−folded = 353 ± 1 nm
λ rThBgl−denaturedmax  = 354 ± 2 nm
〈λ〉rThBgl−denatured = 363 ± 1 nm
  1. MM prep predicted molecular mass, MM exp experimental molecular mass, MM app apparent molecular mass
  2. aPredicted data from the amino acid sequence of rThBgl using the Sednterp server (http://sednterp.unh.edu/)
  3. bFrom the ratio of R s:R 0
  4. cObtained from a SedFit analysis
  5. dSecondary structure generated by deconvolution of the experimental CD spectra using the CDNN Deconvolution program