Abstract:
Fungal glucoamylases from Aspergillus fumigatus—expressed in Trichoderma reesei host cells (AfGATR) are provided. Trichoderma reesei host cells express AfGATRs at higher, or at least comparable, levels to natively expressed AfGA Aspergillus fumigatus. AfGATRs, including AfGA1TR and AfGA2TR, exhibit high activity at elevated temperatures and at low pH, so AfGATRs can be used efficiently in a process of saccharification in the presence of alpha-amylase, such as Aspergillus kawachii alpha-amylase (AkAA). AfGATRs advantageously catalyze starch saccharification to an oligosaccharide composition significantly enriched in DP1 (i.e., glucose) compared to the products of saccharification catalyzed by Aspergillus niger glucoamylase (AnGA) or native AfGA expressed in Aspergillus fumigatus. AfGATRs such as AfGA1TR, AfGA2TR or a variant thereof can be used at a lower dosage than AnGA and natively expressed AfGAs to produce comparable levels of glucose.
Abstract:
The present disclosure relates to polypeptides having alpha-glucosidase activity isolated, derived or derivable from Rasamsonia or engineered polypeptides having alpha-glucosidase activity isolated, derived or derivable from Rasamsonia homologs. The present disclosure also pertains to polynucleotides encoding the polypeptides, nucleic acid constructs, vectors, host cells and mutant cells comprising the polynucleotides. The disclosure further pertains to compositions comprising such polypeptides, methods of producing the polypeptides and compositions, as well as methods for using such polypeptides and compositions for industrial applications.
Abstract:
Fungal glucoamylases from Aspergillus fumigatus that are expressed in Trichoderma reesei host cells (AfGATR) are provided. AfGATRs, including AfGA1TR and AfGA2TR, exhibit high activity at elevated temperatures and at low pH, so AfGATRs can be used efficiently in a simultaneous liquefaction and saccharification process in the presence of alpha amylase, such as Aspergillus kawachii alpha-amylase (AkAA). This greatly reduces the combined run time of liquefaction and saccharification reaction, where the pH and temperature must be readjusted for optimal use of the alpha-amylase or glucoamylase.
Abstract:
A fungal α-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 α-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 α-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:
Described are methods and compositions relating to granular starch-converting glucoamylases and α-amylases. The enzymes can be used to perform enzymatic starch hydrolysis of granular starch at or below the gelatinization temperature of insoluble granular starch.
Abstract:
Described are methods for saccharifying starch-containing materials using a glucoamylase, methods for producing fermentation products, and fermentation products produced by the method thereof as well as methods for increasing starch digestibility in a ruminant using at least one of the glucoamylases described herein.
Abstract:
Fungal glucoamylases from Aspergillus fumigatus—expressed in Trichoderma reesei host cells (AfGATR) are provided. Trichoderma reesei host cells express AfGATRs at higher, or at least comparable, levels to natively expressed AfGA Aspergillus fumigatus. AfGATRs, including AfGA1TR and AfGA2TR, exhibit high activity at elevated temperatures and at low pH, so AfGATRs can be used efficiently in a process of saccharification in the presence of alpha-amylase, such as Aspergillus kawachii alpha-amylase (AkAA). AfGATRs advantageously catalyze starch saccharification to an oligosaccharide composition significantly enriched in DP1 (i.e., glucose) compared to the products of saccharification catalyzed by Aspergillus niger glucoamylase (AnGA) or native AfGA expressed in Aspergillus fumigatus. AfGATRs such as AfGA1TR, AfGA2TR or a variant thereof can be used at a lower dosage than AnGA and natively expressed AfGAs to produce comparable levels of glucose.
Abstract:
Disclosed are compositions and methods relating to alpha-amylase from Exiguobacterium. The compositions and methods are useful, for example, for starch liquefaction and saccharification, for cleaning starchy stains in laundry, dishwashing, and other applications, for textile processing (e.g., desizing), in animal feed for improving digestibility, and and for baking and brewing.
Abstract:
A fungal α-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 α-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 α-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:
Described are polypeptides having glucoamylase activity, compositions comprising such polypeptides, and methods of using such polypeptides and compositions.