Chaetomella raphigera β-glucosidase D2-BGL has intriguing structural features and a high substrate affinity that renders it an efficient cellulase supplement for lignocellulosic biomass hydrolysis

Table 2 Comparison of kinetic parameters between D2-BGL and other Pichia pastoris-expressed fungal β-glucosidases

Organism	pNPGase activity		Cellobiase activity		References
Organism	K_m (mM)	V_max (U/mg)	K_m (mM)	V_max (U/mg)	References
A. fumigatus Z5	1.76	131	2.2	53	[15]
M. thermophila	0.39	47.9	2.64	49.4	[37]
N. crassa	0.21	147.9	ND	75	[38]
P. funiculosum NCL1	2.5	3332	1.25	2083	[17]
Periconia sp. BCC2871	0.19	761	0.5	627	[36]
T. leycettanus JCM12802	0.18	1309	10.4	618	[39]
T. leycettanus	1.1	469	7.6	526	[14]
C. raphigera D2	0.2	419	0.96	312.5	This study

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