Danisco US Inc.

Dupont Nutrition Biosciences Aps

International N&h Denmark Aps

Martijn Scheffers

Richard Ray Bott

Wolfgang Aehle

Piet Van Solingen

Casper Vroemen

Pieter Van Solingen

Jayarama K Shetty

Bo Zhang

Ling Hua

Gang Duan

Casper Willem Vroemen

Kathy Qian

Kathleen A Clarkson

Igor Nikolaev

Shukun Yu

Jing Ge

Zhongmei Tang

Jacob Flyvholm Cramer

Paula Johanna Maria Teunissen

Peter Edvard Degn

Jacquelyn A Huitink

Marco Van Brussel-Zwijnen

Zhengong Zhang

Igor Nikoaev

Elin Petersen

Marco Van Brussel

Zhen Ma

Marc Anton Bernhard Kolkman

Stepan Shipovskov

The present invention relates to variants of a parent glucoamylase having altered properties (e.g., improved thermostability and/or specific activity). In particular, the present invention provides compositions comprising the variant glucoamylases, including starch hydrolyzing compositions, animal feed compositions and cleaning compositions. The invention also relates to DNA constructs encoding the variants and methods of producing the glucoamylase variants in host cells.

Glucoamylase variants with altered properties

A fungal alpha-amylase is provided from(AfAmyl). AfAmyl has an optimal pH of 3.5 and is operable at 30-75 degrees C., allowing the enzyme to be used in combination with a glucoamylase and an isoamylase 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 alpha-amylase or glucoamylase. AfAmyl also catalyzes the saccharification of starch substrates to an oligosaccharide composition significantly enriched in DP2 and (DPI+DP2) compared to the products of saccharification catalyzed by an alpha-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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The present invention relates to combinatorial variants of a parent glucoamylase that have altered properties for reducing the synthesis of condensation products during hydrolysis of starch. Accordingly, the variants of a parent glucoamylase are suitable such as for use within brewing and glucose syrup production. Also disclosed are DNA constructs encoding the variants and methods of producing the glucoamylase variants in host cells.

Variants of glucoamylase

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.

The present disclosure relates to variants of a parent glucoamylase having altered properties (e.g., improved thermostability and/or specific activity). In particular, the present disclosure provides compositions comprising the variant glucoamylases, including starch hydrolyzing compositions and cleaning compositions. The disclosure also relates to DNA constructs encoding the variants and methods of producing the glucoamylase variants in host cells.

The present invention relates to glucoamylase variants. In particular, the invention relates to variants in the starch binding domain (SBD) of a glucoamylase. The invention also relates to variants having altered properties (e.g., improved thermostability and/or increased specific activity) as compared to a corresponding parent glucoamylase. The present invention also provides enzyme compositions comprising the variant glucoamylases; DNA constructs comprising polynucleotides encoding the variants; and methods of producing the glucoamylase variants in host cells.

Glucoamylase variants

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.

A maltogenic a-amylase from(TrAA) and variants thereof are useful in the production of high-maltose syrups from liquefied starch. Particularly high maltose concentrations are achieved when TrAA is used in the presence of a pullulanase. Expression hosts and encoding nucleic acids useful for producing TrAA and its variants also are provided.

The present invention relates to combinatorial variants of a parent glucoamylase that have altered properties for reducing the synthesis of condensation products during hydrolysis of starch. Accordingly the variants of a parent glucoamylase are suitable such as for use within brewing and glucose syrup production. Also disclosed are DNA constructs encoding the variants and methods of producing the glucoamylase variants in host cells.

A maltogenic &#x3b1;-amylase from(TrAA) and variants thereof in the presence of a glucoamylase are useful in the production of high-glucose syrups from liquefied starch, where the high-glucose syrups produced thereby contain at least about 97% glucose. In this process, TrAA advantageously suppresses the reversion of glucose to malto-oligosaccharides. Expression hosts and encoding nucleic acids useful for producing TrAA and its variants also are provided.

The present invention relates to variant glucoamylases wherein the variant has altered properties (e.g., improved thermostability and/or specific activity) compared to a corresponding parent glucoamylase. The present invention also relates to enzyme compositions comprising a variant glucoamylase (e.g., starch hydrolyzing compositions); DNA constructs comprising polynucleotides encoding the variants and methods of producing the variant glucoamylases in host cells.

Growing community of inventors

Leiden, Netherlands

Martijn Scheffers