Butamax Advanced Biofuels LLC

Butamax (tm) Advanced Biofuels LLC

E.i. Dupont De Nemours and Company

Daniel P Okeefe

Mark Scott Payne

Yougen Li

Mark J Nelson

Der-Ing Liao

Lori Ann Maggio-Hall

Hongxian He

Larry Cameron Anthony

Arthur Leo Kruckeberg

Steven Cary Rothman

Ranjan Patnaik

Lixuan Lisa Huang

Jessica McElvain

Pierre E Rouviere

Stephen R Fahnestock

Jean-Francois Tomb

Tanja Maria Gruber

Brian James Paul

Laura Anne Bedzyk

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

Methods for the evolution of NADPH specific ketol-acid reductoisomerase enzymes to acquire NADH specificity are provided. Specific mutant ketol-acid reductoisomerase enzymes isolated fromthat have undergone co-factor switching to utilize NADH are described.

Ketol-acid reductoisomerase using NADH

Methods for the evolution of NADPH specific ketol-add reductoisomerase enzymes to acquire NADH specificity are provided. Specific mutant ketol-acid reductoisomerase enzymes isolated fromthat have undergone co-factor switching to utilize NADH are described.

Methods for the evolution of NADPH binding ketol-acid reductoisomerase enzymes to acquire NADH binding functionality are provided. Specific mutant ketol-acid reductoisomerase enzymes isolated fromthat have undergone co-factor switching to bind NADH are described.

An acid-cleavable peptide linker comprising aspartic acid and proline residues is disclosed. The acid-cleavable peptide linker provides an altered sensitivity to acid-hydrolytic release of peptides of interest from fusion peptides of the formula PEP1-L-PEP2. The inventive linker, L, is described in various embodiments, each of which provides substantially more rapid acid-release of peptides of interest than does a single aspartic acid-proline pair. In an additional aspect, a method of increasing the stability of an acid cleavable linkage to acid hydrolysis is also provided.

Acid-cleavable linkers exhibiting altered rates of acid hydrolysis

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Ridley Park, PA, United States of America

Daniel P Okeefe