The isolation of pentose-assimilating yeasts and their xylose fermentation potential.

For the implementation of cellulosic ethanol technology, the maximum use of lignocellulosic materials is important to increase efficiency and to reduce costs. In this context, appropriate use of the pentose released by hemicellulose hydrolysis could improve de economic viability of this process. Since the Saccharomyces cerevisiae is unable to ferment the pentose, the search for pentose-fermenting microorganisms could be an alternative.

Saccharification of ozonated sugarcane bagasse using enzymes from Myceliophthora thermophila JCP 1-4 for sugars release and ethanol production.

The saccharification of ozonated sugarcane bagasse (SCB) by enzymes from Myceliophthora thermophila JCP 1-4 was studied. Fungal enzymes provided slightly higher sugar release than commercial enzymes, working at 50°C. Sugar release increased with temperature increase.

Production and characterization of β-glucosidase obtained by the solid-state cultivation of the thermophilic fungus Thermomucor indicae-seudaticae N31.

In this paper, several agro-industrial wastes (soybean meal and wheat straw, rice and peanut husks, corn cob and corn stover, and sugarcane bagasse) were tested for the production of β-glucosidase by the cultivation of thermophilic fungus Thermomucor indicae-seudaticae N31 in solid-state fermentation (SSF). Among the tested substrates, the highest yields were obtained in soybean meal. Other fermentation parameters were also evaluated, such as initial pH, merge substrates, and fermentation time, as well as the physicochemical characterization of the enzyme.

Influence of different substrates on the production of a mutant thermostable glucoamylase in submerged fermentation.

Three mutations, Ser54→Pro, Thr314→Ala, and His415→Tyr, were identified in Aspergillus awamori glucoamylase gene expressed by Saccharomyces cerevisiae. The mutant glucoamylase (GA) was substantially more thermostable than a wild-type GA at 70 °C, with a 3.0 KJ mol(-1) increase in the free energy of thermo-inactivation.