Danisco US Inc.

Danisco US Inc., Genencor Division

Casper Vroemen

Marc Kolkman

Martijn Scheffers

Richard Ray Bott

Wolfgang Aehle

Brian E Jones

Walter Weyler

Piet Van Solingen

Melodie Estabrook

Clement K Choy

Chris Leeflang

George R England

Claudine Chang

Jacquelyn A Huitink

Kathleen A Clarkson

James T Kellis, Jr

Bo Zhang

Thomas P Graycar

Luis Gustavo Cascao-Pereira

Igor Nikolaev

Neelam S Amin

Ling Hua

Jing Ge

Zhongmei Tang

Paula Johanna Maria Teunissen

Marco Van Brussel-Zwijnen

Brian Miller

Scott Douglas Power

Andrew Shaw

Karsten Matthias Kragh

Sandra W Ramer

Peter Edvard Degn

Brian S Miller

Mansi Goyal

Victoria E Huang

Igor Nikoaev

Su Yin Marina Chow

David L Wong

Embodiments of the present disclosure relate toglucoamylase (TrGA) variants having improved properties (e.g., improved thermostability, improved specific activity, and/or resistant to oxidation-related activity loss). Also provided are compositions comprising variant glucoamylases. These compositions are useful in various starch process applications.

Trichoderma reesei glucoamylase variants resistant to oxidation-related activity loss and the use thereof

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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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

Described are variants (mutants) of a parent alpha-amylase having alpha-amylase activity and exhibiting altered properties relative to the parent alpha-amylase, and methods of use, thereof.

TS-23 alpha-amylase variants with altered properties

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 method of making aalpha-amylase variant that increases alpha-amylase production and the alpha-amylases produced thereby. The recombinant alpha-amylases can be placed in compositions and used for purposes of laundry detergents, cleaning and dishwashing detergents, fabric desizing, starch liquefaction, cereal liquefaction, starch saccharification, biofilm removal, and starch hydrolysis in cane sugar processing.

Enhanced amylase production by N-terminal addition to mature amylase protein

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

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.

Glucoamylase variants with altered properties

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.

Disclosed herein are compositions comprising an alpha-amylase enzyme obtained fromsp. no. 195, and methods of using the enzyme to clean surfaces and textiles. Also disclosed are variants of the enzyme with different signal sequences.

The invention relates to novel variants of the enzymatic peptide pullulanase, the gene sequences encoding said novel peptides, expression vectors comprising those gene sequences as well as organisms expressing the novel pullulanase variants. The novel pullulanase variants of the present invention were made empirically by the use of codon-optimization procedures, selective truncation of 'wild-type' molecules and through the replacement of selected amino acid residues. Furthermore, the invention relates to the use of these novel pullulanase peptides in the textile, fermentation, food and other industries.

Pullulanase variants with increased productivity

TS23 alpha-amylase variants with altered properties

Variants ofsp. TS-23 strain alpha-amylases exhibit improved enzymatic performance, including increased themostability, reduced calcium dependence, increased washing/cleaning performance, and baking ability. Compositions comprising these variants are useful in methods of starch processing, starch liquefaction, fermatation, starch saccharification, cleaning, laundrying, textile desizing, baking, and biofilm removal.

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Oegstgeest, Netherlands

Casper Vroemen