Abstract: A fungal ?-amylase is provided from Aspergillus clavatus (AcAmy1). AcAmy1 has an optimal pH of 4.5 and is operable at 30-75° C., allowing the enzyme to be used in combination with a glucoamylase in a saccharification reaction. This obviates the necessity of running a saccharification reaction as a batch process, where the pH and temperature must be readjusted for optimal use of the ?-amylase or glucoamylase. AcAmy1 also catalyzes the saccharification of starch substrates to an oligosaccharide composition significantly enriched in DP2 and (DP1+DP2) compared to the products of saccharification catalyzed by an ?-amylase from Aspergillus kawachii. This facilitates the utilization of the oligosaccharide composition by a fermenting organism in a simultaneous saccharification and fermentation process, for example.

Abstract: A process for mechanical destructuring of starch-based biomass was developed that makes use of a short application of high compression, impact, and shearing forces. The biomass may be destructured using a specific energy input that is less than 40% of the total combustible energy of the biomass. The destructured starch-based biomass, with or without saccharification and/or in-feed glycosyl hydrolase enzymes, may be used in feed applications. The destructured starch-based may saccharified to produce syrups and fermentable sugars, and for production of products including ethanol using a biocatalyst.

Abstract: Embodiments of the present disclosure relate to a process for producing isoprenoid precursor molecules and/or isoprenoids from a starch substrate by saccharification and/or fermentation. The saccharification is effectively catalyzed by a glucoamylase at a pH in the range of 5.0 to 8.0. At a pH of 6.0 or above, the glucoamylase possesses at least 50% activity relative to its maximum activity. The saccharification and fermentation may be performed as a simultaneous saccharification and fermentation (SSF) process.

Abstract: A fungal ?-amylase is provided from Aspergillus clavatus (AcAmyl). AcAmyl has an optimal pH of 4.5 and is operable at 30-75° C., allowing the enzyme to be used in combination with a glucoamylase in a saccharification reaction. This obviates the necessity of running a saccharification reaction as a batch process, where the pH and temperature must be readjusted for optimal use of the ?-amylase or glucoamylase. AcAmyl also catalyzes the saccharification of starch substrates to an oligosaccharide composition significantly enriched in DP2 and (DP1+DP2) compared to the products of saccharification catalyzed by an ?-amylase from Aspergillus kawachii. This facilitates the utilization of the oligosaccharide composition by a fermenting organism in a simultaneous saccharification and fermentation process, for example.

Abstract: Embodiments of the present disclosure relate to a process for producing isoprene from a starch substrate by saccharification and/or fermentation. The saccharification is effectively catalyzed by a glucoamylase at a pH in the range of 5.0 to 8.0. At a pH of 6.0 or above, the glucoamylase possesses at least 50% activity relative to its maximum activity. The saccharification and fermentation may be performed as a simultaneous saccharification and fermentation (SSF) process.

Abstract: Embodiments of the present disclosure relate to a process for producing downstream products, such as high-density glucose syrups and high-glucose fermentation feedstock, from a starch-containing substrate without a pH adjustment before the saccharification step. The saccharification is effectively catalyzed by a glucoamylase at a pH in the range of 5.2 to 5.6.

Abstract: Embodiments of the present disclosure relate to a process for producing downstream products, such as high-density glucose syrups and high-glucose fermentation feedstock, from a starch-containing substrate without a pH adjustment before the saccharification step. The saccharification is effectively catalyzed by a glucoamylase at a pH in the range of 5.2 to 5.6.

Abstract: A fungal ?-amylase is provided from Aspergillus clavatus (AcAmyl). AcAmyl has an optimal pH of 4.5 and is operable at 30-75° C., allowing the enzyme to be used in combination with a glucoamylase in a saccharification reaction. This obviates the necessity of running a saccharification reaction as a batch process, where the pH and temperature must be readjusted for optimal use of the ?-amylase or glucoamylase. AcAmyl also catalyzes the saccharification of starch substrates to an oligosaccharide composition significantly enriched in DP2 and (DP1+DP2) compared to the products of saccharification catalyzed by an ?-amylase from Aspergillus kawachii. This facilitates the utilization of the oligosaccharide composition by a fermenting organism in a simultaneous saccharification and fermentation process, for example.

Abstract: Provided herein are compositions and methods related to the direct conversion of the starch in a ground or fractionated grain into a fermentable sugar feedstock capable of serving as a carbon source for the industrial production of one or more products by a fermenting organism, such as isoprene, isoprenoid precursor molecules, and/or isoprenoids. Such conversions may be performed at temperatures at or below the initial gelatinization temperature of the starch present in the grain and may utilize one or more isolatable endogenous enzymes present in certain unrefined grains.

Abstract: Embodiments of the present disclosure relate to a process for producing isoprenoid precursor molecules and/or isoprenoids from a starch substrate by saccharification and/or fermentation. The saccharification is effectively catalyzed by a glucoamylase at a pH in the range of 5.0 to 8.0. At a pH of 6.0 or above, the glucoamylase possesses at least 50% activity relative to its maximum activity. The saccharification and fermentation may be performed as a simultaneous saccharification and fermentation (SSF) process.

Abstract: The present disclosure relates to composition comprising EG cellulase and methods of use, thereof. The compositions are useful, e.g., for reducing the viscosity of plant material slurry.

Abstract: Embodiments of the present disclosure relate to a process for producing isoprene from a starch substrate by saccharification and/or fermentation. The saccharification is effectively catalyzed by a glucoamylase at a pH in the range of 5.0 to 8.0. At a pH of 6.0 or above, the glucoamylase possesses at least 50% activity relative to its maximum activity. The saccharification and fermentation may be performed as a simultaneous saccharification and fermentation (SSF) process.

Abstract: Embodiments of the present disclosure relate to a process for producing downstream products, such as fermentable sugars and end products, from a starch substrate by saccharification and/or fermentation. The saccharification is effectively catalyzed by a glucoamylase at a pH in the range of 5.0 to 8.0. At a pH of 6.0 or above, the glucoamylase possesses at least 50% activity relative to its maximum activity. The saccharification and fermentation may be performed as a simultaneous saccharification and fermentation (SSF) process.