Danisco US Inc.

Jing Ge

Ling Hua

Michael C Ward

Ayrookaran J Poulose

Michael D Ward

Zhongmei Tang

Xiaogang Gu

Bo Zhang

Susan Mampusti Madrid

Mingmin Song

Danfeng Song

Kathleen A Clarkson

Benjamin S Bower

Martijn Scheffers

Casper Vroemen

Paula Johanna Maria Teunissen

Jacquelyn A Huitink

Jimmy Chan

Kun Zhong

Marco Van Brussel-Zwijnen

Jayarama K Shetty

Karsten Matthias Kragh

Sung Ho Lee

Zheyong Yu

Zhen Qian

Zhenghong Zhang

Shukun Yu

Steven Sungin Kim

Zhiyong Xie

Zhengzheng Zou

Bo Zhong

Guoqing Liu

Wenting Li

Jinahua (Jalsen) Li

Helong Hao

Jalsen Li

Martijn Silvan Scheffers

Kirstin Yasuko Nosé Crotty

Steven Sungjin Kim

Pim Van Der Kley

Monica Tse

Bradley Roger Kelemen

Igor Nikolaev

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

Compositions and methods are provided for genome modification at a target site in the genome of a filamentous fungal cell. The methods and compositions are drawn to a guide polynucleotide/Cas endonuclease system for modifying or altering the target site. Aspects in which the filamentous fungal cell being modified has a defective non-homologous end joining pathway are also provided.

Fungal genome modification systems and methods of use

Compositions and methods are provided for genome modification at a target site in the genome of a fungal cell. The methods and compositions are drawn to a guide polynucleotide/Cas endonuclease system for promoting modification of the DNA sequence at a target site in a fungal host cell genome.

Compositions and methods are provided for genome modification at a target site in the genome of a fungal cell. Aspects of methods and compositions are drawn to a guide polynucleotide/Cas endonuclease system for promoting insertion of a donor DNA at a desired target site in a fungal host cell genome.

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

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

The present compositions and methods relate to a thermostable carbonic anhydrases, polynucleotides encoding the carbonic anhydrase, and methods of make and/or use thereof. Formulations containing the carbonic anhydrase are suitable for use in extracting carbon dioxide.

Thermostable carbonic anhydrases and methods of 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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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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Palo Alto, CA, United States of America

Jing Ge