to glucose by the T. reesei extract and the lack of the required bglucosidase
activity by S. cerevisiae. Therefore, we tested the
efficiency of SSF when cellobiase activity was added either
exogenously in the form of a commercial preparation (Novozyme
188) or by heterologous expression of the enzyme in the yeast
used for fermentation. For heterologous expression, we used
AaBGL1 because of its high cellobiase activity and robustness to
changes in temperature or pH. The substrate, 1 g converge-milled
Japanese cedar, was presaccharified with T. reesei cellulase at
50C for 24 h before the SSF process, with the addition of yeast
expressing recombinant AaBGL1 or supplementation with
Novozyme 188. The concentration of glucose and mannose after
presaccharification of 5 mg protein of T. reesei culture
supernatant were 7.9 and 1.2 mg/mL, respectively.
Fig. 5 shows the concentrations of cellobiose
to glucose by the T. reesei extract and the lack of the required bglucosidaseactivity by S. cerevisiae. Therefore, we tested theefficiency of SSF when cellobiase activity was added eitherexogenously in the form of a commercial preparation (Novozyme188) or by heterologous expression of the enzyme in the yeastused for fermentation. For heterologous expression, we usedAaBGL1 because of its high cellobiase activity and robustness tochanges in temperature or pH. The substrate, 1 g converge-milledJapanese cedar, was presaccharified with T. reesei cellulase at50C for 24 h before the SSF process, with the addition of yeastexpressing recombinant AaBGL1 or supplementation withNovozyme 188. The concentration of glucose and mannose afterpresaccharification of 5 mg protein of T. reesei culturesupernatant were 7.9 and 1.2 mg/mL, respectively.Fig. 5 shows the concentrations of cellobiose
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