Butamax Advanced Biofuels LLC

Butamax (tm) Advanced Biofuels LLC

University of California

Amyris Biotechnologies, Inc.

Butamax (tm) Advanced Biofules LLC

Larry Cameron Anthony

Lori Ann Maggio-Hall

Steven Cary Rothman

Mark J Nelson

Arthur Leo Kruckeberg

Lixuan Lisa Huang

Hongxian He

Yougen Li

Ranjan Patnaik

Daniel P Okeefe

Jessica McElvain

Rick Weizhang Ye

Jean-Francois Tomb

Keith H Burlew

Tyler T Ames

Jay D Keasling

Caroline M Peres

Dennis Flint

Daniel P O'Keefe

Jack Newman

Brian James Paul

Douglas J Pitera

Michael Dauner

Wonchul Suh

Lisa L Huang

Farnaz F Nowroozi

Robert Balcarcel

Jennifer Anthony

Jessica Mcelvain

Katharine J Gibson

Daniel P O'keefe

Jack D Newman

Farnaz Nowroozi

Provided herein are processes and microorganisms which utilize both protein hydrolysates and carbohydrates from biomass feedstocks to produce renewable hydrocarbon compositions. Advantages of the disclosed methods may be recognized in fuel blends comprising such hydrocarbon compositions.

Production of renewable hydrocarbon compositions

The invention relates to the fields of industrial microbiology and alcohol production including production of yeast products with features suitable for transport, storage, and utilization in fermentation.

Method for the production of yeast

The invention relates to recombinant host cells having at least one integrated polynucleotide encoding a polypeptide that catalyzes a step in a pyruvate-utilizing biosynthetic pathway, e.g., pyruvate to acetolactate conversion. The invention also relates to methods of increasing the biosynthetic production of isobutanol, 2,3-butanediol, 2-butanol or 2-butanone using such host cells.

Integration of a polynucleotide encoding a polypeptide that catalyzes pyruvate to acetolactate conversion

Provided herein are recombinant yeast host cells and methods for their use for production of isobutanol. Yeast host cells provided comprise an isobutanol biosynthetic pathway and at least one of reduced or eliminated aldehyde dehydrogenase activity, reduced or eliminated acetolactate reductase activity; or a heterologous polynucleotide encoding a polypeptide having ketol-acid reductoisomerase activity.

Host cells and methods for production of isobutanol

Provided herein are recombinant yeast host cells and methods for their use for production of fermentation products. Host cells provided herein comprise a pyruvate-utilizing pathway and a competitive growth advantage over other microorganisms in solution.

Competitive growth and/or production advantage for butanologen microorganism

Yeast cells with reduced activity of certain enzymes involved in branched chain amino acid biosynthesis in yeast mitochondria are described. Target enzymes include threonine deaminase, isopropylmalate synthase, and optionally branched chain amino acid transaminase.

Increased production of isobutanol in yeast with reduced mitochondrial amino acid biosynthesis

Butanol strain improvement with integration of a polynucleotide encoding a polypeptide that catalyzes pyruvate to acetolactate conversion

Crabtree positive yeast cells that have endogenous expressed pyruvate decarboxylase genes inactivated and an engineered biosynthetic pathway utilizing pyruvate were found to have improved growth and product yield when glucose repression was reduced. These cells were able to grow in media containing a high glucose concentration.

Yeast production host cells

Yeast strains were engineered that have increased activity of heterologous proteins that require binding of an Fe&#x2014;S cluster for their activity. The yeast strains have reduced activity of an endogenous Fe&#x2014;S protein. Activities of heterologous fungal or plant 2Fe-2S dihydroxy-acid dehydratases and Fe&#x2014;S propanediol dehydratase reactivase were increased for increased production of products made using biosynthetic pathways including these enzymes, such as valine, isoleucine, leucine, pantothenic acid (vitamin B5), isobutanol, 2-butanone and 2-butanol.

Recombinant yeast host cells comprising FE-S cluster proteins

A high flux in conversion of pyruvate to acetolactate was achieved in yeast through expression of acetolactate synthase in the cytosol in conjunction with reduction in pyruvate decarboxylase activity. Additional manipulations to improve flux to acetolactate are reduced pyruvate dehydrogenase activity and reduced glycerol-3-phosphate dehydrogenase activity. Production of compounds having acetolactate as an upstream intermediate benefit from the increased conversion of pruvate to acetolactate in the described strains.

Enhanced pyruvate to acetolactate conversion in yeast

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Aston, PA, United States of America

Larry Cameron Anthony