Danisco US Inc.

E.i. Dupont De Nemours and Company

Dupont Industrial Biosciences USA, LLC

Zhongmei Tang

Ling Hua

Jayarama K Shetty

Zheyong Yu

Jing Ge

Robert DiCosimo

Susan Marie Hennessey

Kevin D Nagy

Rodrigo Ramirez

Bo Zhang

Kathleen A Clarkson

Martijn Scheffers

Casper Vroemen

Paula Johanna Maria Teunissen

Jacquelyn A Huitink

Erwin F Columbus-Hago

Erwin Columbus Hago

Marco Van Brussel-Zwijnen

Kun Zhong

Karsten Matthias Kragh

Sung Ho Lee

Zhen Qian

Zhenghong Zhang

Shukun Yu

Xiaogang Gu

Zhiyong Xie

Zhengzheng Zou

Bo Zhong

Guoqing Liu

Jalsen Li

Helong Hao

Jinahua (Jalsen) Li

Wenting Li

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.

Glucoamylases and methods of use, thereof

Fungal glucoamylases from&#x2014;expressed inhost cells (AfGATR) are provided.host cells express AfGATRs at higher, or at least comparable, levels to natively expressed AfGA. 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 asalpha-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 byglucoamylase (AnGA) or native AfGA expressed in. 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.

host cells expressing a glucoamylase fromand methods of use thereof

A method is disclosed for hydrolyzing an alpha-1,3 or alpha-1,6 glucosyl-glucose linkage in a saccharide (disaccharide or oligosaccharide). This method comprises contacting the saccharide with an alpha-glucosidase enzyme such as transglucosidase under suitable conditions, during which contacting step the enzyme hydrolyzes at least one alpha-1,3 or alpha-1,6 glucosyl-glucose linkage of the saccharide. This method is useful for reducing the amount of oligosaccharides in a filtrate isolated from a glucan synthesis reaction, for example.

Enzymatic hydrolysis of disaccharides and oligosaccharides using alpha-glucosidase enzymes

A method is disclosed for hydrolyzing an alpha-1,5 glucosyl-fructose linkage in a saccharide (disaccharide or oligosaccharide) such as leucrose. This method comprises contacting the saccharide with an alpha-glucosidase enzyme such as transglucosidase or glucoamylase under suitable conditions, during which contacting step the enzyme hydrolyzes at least one alpha-1,5 glucosyl-fructose linkage of the saccharide. This method is useful for reducing the amount of leucrose in a filtrate isolated from a glucan synthesis reaction, for example.

The present disclosure relates to polypeptides having alpha-glucosidase activity isolated, derived or derivable fromor engineered polypeptides having alpha-glucosidase activity isolated, derived or derivable fromhomologs. 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.

Alpha-glucosidase, compositions and methods

A fungal &#x3b1;-amylase is provided from(AcAmy1). AcAmy1 has an optimal pH of 4.5 and is operable at 30-75&#xb0; 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 &#x3b1;-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 &#x3b1;-amylase from. This facilitates the utilization of the oligosaccharide composition by a fermenting organism in a simultaneous saccharification and fermentation process, for example.

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A fungal &#x3b1;-amylase is provided from(AcAmyl). AcAmyl has an optimal pH of 4.5 and is operable at 30-75&#xb0; 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 &#x3b1;-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 &#x3b1;-amylase from. This facilitates the utilization of the oligosaccharide composition by a fermenting organism in a simultaneous saccharification and fermentation process, for example.

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Shanghai, China

Zhongmei Tang