%0 Journal Article
	%A Le Thuy Mai and  Vu Nguyen Thanh
	%D 2010
	%J International Journal of Bioengineering and Life Sciences
	%B World Academy of Science, Engineering and Technology
	%I Open Science Index 37, 2010
	%T Cloning of a β-Glucosidase Gene (BGL1) from Traditional Starter Yeast Saccharomycopsis fibuligera BMQ 908 and Expression in Pichia pastoris
	%U https://publications.waset.org/pdf/4787
	%V 37
	%X β-Glucosidase is an important enzyme for production
of ethanol from lignocellulose. With hydrolytic activity on
cellooligosaccharides, especially cellobiose, β-glucosidase removes
product inhibitory effect on cellulases and forms fermentable sugars.
In this study, β-glucosidase encoding gene (BGL1) from traditional
starter yeast Saccharomycosis fibuligera BMQ908 was cloned and
expressed in Pichia pastoris. BGL1 of S. fibuligera BMQ 908 shared
98% nucleotide homology with the closest GenBank sequence
(M22475) but identity in amino-acid sequences of catalytic domains.
Recombinant plasmid pPICZαA/BGL1 containing the sequence
encoding BGL1 mature protein and α-factor secretion signal was
constructed and transformed into methylotrophic yeast P. pastoris by
electroporation. The recombinant strain produced single extracellular
protein with molecular weight of 120 kDa and cellobiase activity of
60 IU/ml. The optimum pH of the recombinant β-glucosidase was 5.0
and the optimum temperature was 50°C.
	%P 90 - 94