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%.
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.