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

Table 1 Hydrodynamic and spectroscopic properties of purified rThBgl

Technique	Property
Predicted hydrodynamic data^a	MM_pred = 53.24 kDa
Predicted hydrodynamic data^a	R ₀ = 25.15 Å
Analytical SEC	MM_app = 54.72 ± 3 kDa
	R _s = 31.39 Å
	ƒ/ƒ ^b₀ = 1.25 ± 0.2
AUC^c	\(S_{20,w}^{0}\) = 4.53 ± 0.03 S
	MM_exp = 58.26 ± 7 kDa
	ƒ/ƒ ₀ = 1.23 ± 0.05
CD^d	α-Helix = 35 ± 4 %
CD^d	β-Sheet = 10 ± 2 %
CD thermal-induced unfolding	Tm = 49 ± 1 °C
Fluorescence	λ ^{rThBgl−folded}_max = 334 ± 1 nm
	〈λ〉^{rThBgl−folded} = 353 ± 1 nm
	λ ^{rThBgl−denatured}_max = 354 ± 2 nm
	〈λ〉^{rThBgl−denatured} = 363 ± 1 nm

MM _prep predicted molecular mass, MM _exp experimental molecular mass, MM _app apparent molecular mass
^aPredicted data from the amino acid sequence of rThBgl using the Sednterp server (http://sednterp.unh.edu/)
^bFrom the ratio of R _s:R ₀
^cObtained from a SedFit analysis
^dSecondary structure generated by deconvolution of the experimental CD spectra using the CDNN Deconvolution program

ISSN: 2731-3654