Commenced in January 2007
Frequency: Monthly
Edition: International
Paper Count: 2

β-Glucosidase Related Publications

2 Bioethanol: Indonesian Macro-Algae as a Renewable Feedstock for Liquid Fuel

Authors: T. Poespowati, E. Marsyahyo, R. Kartika-Dewi

Abstract:

This experimental study aims at studying the conversion of macro-algae into bioethanol under several steps of procedure: preparation, pre-treatment, fermentation, and distillation. The main objective of this work was to investigate the role of buffer’s type as a stabiliser of pH level and fermentation time on the yield of ethanol. For this purpose, experiments were carried out on biomass macro-algae to de-couple the pre-treatment and fermentation processes from those associated with distillation process. β- glucosidase was used as cellulose decomposer during hydrolysis step and yeast was used during fermentation process. The species of macro-algae utilised as energy feedstock was Ulva lactuca and it was harvested from southern coast of Central of Java Island – Indonesia. Experiments were conducted in a simple fermenter over a different buffer: citrate buffer and acetic buffer, and over a range of fermentation times between 5 to 20 days. The ethanol production was found to be significantly affected by both variables. The optimum time of fermentation was 10 days with citrate buffer; result in 0.88458% of ethanol, and the ethanol content after distillation process was shown 0.985015%.

Keywords: Fermentation, Bioethanol, buffer, β-Glucosidase, ulva-lactuca

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1 Cloning of a β-Glucosidase Gene (BGL1) from Traditional Starter Yeast Saccharomycopsis fibuligera BMQ 908 and Expression in Pichia pastoris

Authors: Le Thuy Mai, Vu Nguyen Thanh

Abstract:

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.

Keywords: Recombinant Enzyme, Pichia pastoris, β-Glucosidase, Saccharomycopsisfibuligera

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