Danisco US Inc.

Genencor International, Inc.

William Albert Cuevas

Sang-Kyu Lee

Sandra W Ramer

Amr R Toppozada

Scott Douglas Power

Louise Wallace

David Aaron Estell

Andrew Shaw

Luis Gustavo Cascao-Pereira

Elizabeth Ann Bodie

Michael Jay Pepsin

Vivek Sharma

Carol A Requadt

Regina Chin

David E Estell

Marja Koljonen

Joseph Charles McAuliffe

Jayarama K Shetty

Kathleen A Clarkson

Katherine D Collier

Gopal K Chotani

Risha Lindig Bond

Sung Ho Lee

Anthony R Calabria

Gang Duan

Andrew J Morgan

Paula Johanna Maria Teunissen

Bruce A Strohm

David E Wildes

Ying Qian

Hongxian Xu

Sura H Hadi

Martien H Bergsma

Dina Finan

Disclosed are compositions and methods relating to variant alpha-amylases. The variant alpha-amylases are useful, for example, for starch liquefaction and saccharification, for cleaning starchy stains in laundry, dishwashing, and other applications, for textile processing (e.g., desizing), in animal feed for improving digestibility, and for baking and brewing.

Alpha-amylase combinatorial variants

Alpha-amylases from(AmyE), variants thereof, nucleic acids encoding the same, and host cells comprising the nucleic acids are provided. Methods of using AmyE or variants thereof are disclosed, including liquefaction and/or saccharification of starch. Such methods may yield sugars useful for ethanol production or high fructose corn syrup production. In some cases, the amylases can be used at low pH, in the absence of calcium, and/or in the absence of a glucoamylase.

[object Object]

An &#x3b1;-amylase from(AmyE) produces significant amounts of glucose from various carbohydrate substrates, including vegetable starch, maltoheptaose, and maltotriose. Among other things, this advantageous property allows AmyE or variants thereof to be used in a saccharification reaction having a reduced or eliminated requirement for glucoamylase. The reduction or elimination of the glucoamylase requirement significantly improves the efficiency of the production of ethanol or high fructose corn syrup, for example.

Embodiments of the present disclosure relate to a process for producing isoprenoid precursor molecules and/or isoprenoids from a starch substrate by saccharification and/or fermentation. The saccharification is effectively catalyzed by a glucoamylase at a pH in the range of 5.0 to 8.0. At a pH of 6.0 or above, the glucoamylase possesses at least 50% activity relative to its maximum activity. The saccharification and fermentation may be performed as a simultaneous saccharification and fermentation (SSF) process.

Production of isoprenoids under neutral pH conditions

Described are variants of a parent &#x3b1;-amylase that exhibits an alteration in at least one of the following properties relative to said parent &#x3b1;-amylase: specific activity, substrate specificity, substrate binding, substrate cleavage, thermal stability, pH-dependent activity, pH-dependent stability, oxidative stability, Ca2+ dependency, pI, and wash performance. The variants are suitable for starch conversion, ethanol production, laundry washing, dish washing, hard surface cleaning, textile desizing, and/or sweetener production.

A personal care composition is provided and includes an effective amount of a repeat sequence protein polymer. The personal care composition may be a hair care composition, a skin care composition, a nail care composition, a cosmetic composition, or an over-the-counter pharmaceutical composition.

Use of repeat sequence protein polymers in personal care compositions

Biomolecular conjugates are provided which comprise the conjugation product of a repeat sequence protein polymer and at least one active agent. Additional aspects provide methods for their manufacture and various industrial and consumer applications.

Repeat sequence protein polymer active agent congjugates, methods and uses

Methods for forming peptide derivatives using functional moieties and peptide derivatives are provided. Further, methods for using peptide derivatives to form silicon-based composite materials and silicon-based composite materials formed thereby are provided. The silicon-based composite materials may have features on the nanoscale, and the materials may exhibit characteristics derived from the functional moieties on the peptide derivatives. It is emphasized that this abstract is provided to comply with the rules requiring an abstract which will allow a searcher or other reader to quickly ascertain the subject matter of the technical disclosure. It is submitted with the understanding that is will not be used to interpret or limit the scope or meaning of the claims.

Peptide derivatives, and their use for the synthesis of silicon-based composite materials

Thermostable xylanases from Microtetraspora flexuosa as a feed additive

The present invention relates to novel xylanases purified from the microorganism, Microtetraspora flexuosa. Each biochemically unique xylanase is thermostable and has optimal activity in alkaline conditions. The present invention is also directed to methods that utilize either the whole enzyme system or one or more of the above purified thermostable xylanases obtained from Microtetraspora flexuosa. These enzymes are excellent candidates for enhancing the delignification and bleaching of pulp. Furthermore, treating the pulp with the above enzymes prior to bleaching may reduce the amount of chlorine containing and/or peroxide chemicals required in the bleaching process.

Method of enhancing the delignification and/or bleaching of pulp

Five xylanases are purified from the microorganism, Microtetraspora flexuosa,preferably strain ATCC 35864. Each biochemically unique xylanase is thermostable and has optimal activity in alkaline conditions. These enzymes are excellent candidates for enhancing the delignification and bleaching of pulp. Furthermore, treating the pulp with the above enzymes prior to bleaching may reduce the amount of chlorine containing and/or peroxide chemicals required in the bleaching process.

Five thermostable xylanases from microtetraspora flexuosa for use in

Growing community of inventors

San Francisco, CA, United States of America

William Albert Cuevas