Increased enzymatic hydrolysis of sugarcane bagasse by a novel glucose- and xylose-stimulated β-glucosidase from Anoxybacillus flavithermus subsp. yunnanensis E13T

Table 1 Hydrolysis activities of BglP on various substrates

Substrate^a	Linkage of glycosyl group	Relative activity^b (%)
p-Nitrophenyl-β-D-glucopyranoside (pNPG)	(β-1,4) Glucose	100
o-Nitrophenyl-β-D-glucopyranoside (oNPG)	(β-1,2) Glucose	51 ± 1.6
p-Nitrophenyl-β-D-lactopyranoside (pNPLac)	(β-1,4) Lactose	15.3 ± 0.6
p-Nitrophenyl-β-D-fucopyranoside (pNPFuc)	(β-1,4) Fucose	13.2 ± 0.4
p-Nitrophenyl-β-D-galactoside (pNPGal)	(β-1,4) Galactose	8.2 ± 0.2
o-Nitrophenyl-β-D-galactoside (oNPGal)	(β-1,2) Galactose	2.0 ± 0.3
Cellobiose	(β-1,4) Glucose	17.5 ± 0.4
Cellotriose	(β-1,4) Glucose	7.9 ± 0.1
Cellotetraose	(β-1,4) Glucose	6.7 ± 0.4
Cellopentaose	(β-1,4) Glucose	4.9 ± 0.2
Lactose	(β-1,4) Galactose	11.0 ± 0.6
Laminaribiose	(β-1,3) Glucose	5.6 ± 0.2

^aNo activity or poorly activity was detected with p-Nitrophenyl-α-D-glucopyranoside, p-nitrophenyl-β-D-xyloside, CMC and Avicel®
^bThe relative activity of the most preferentially hydrolyzed substrate pNPG was taken as 100%. Values are the means ± SD of six experiments (n = 6)

ISSN: 1471-2091