Danisco US Inc.

Jacquelyn A Huitink

Casper Vroemen

Kathleen A Clarkson

Bo Zhang

Martijn Scheffers

Ling Hua

Jing Ge

Zhongmei Tang

Paula Johanna Maria Teunissen

Marco Van Brussel-Zwijnen

Thomas P Graycar

Su Yin Marina Chow

David L Wong

Martijn Silvan Scheffers

Su Yin Maria Chow

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.

[object Object]

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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Burlingame, CA, United States of America

Jacquelyn A Huitink