Polypeptide scaffolds comprising enzymatic proteins are provided. The enzymatic polypeptide scaffolds comprise heterologous enzymes to form a heterologous metabolic pathway, and can be targeted to a substrate through a surface anchoring domain. The enzymatic polypeptide scaffolds leverage the high specificity and affinity protein/protein interaction between the cohesins and dockerins of microorganismal cellulosomes to form custom enzymatic arrays.

An aspect of the present disclosure is a microbial cell that includes a genetic modification resulting in the expression of a deficient form of an endogenous dioxygenase, and a gene encoding an exogenous dioxygenase and a promoter sequence, where the endogenous dioxygenase includes PcaH and PcaG, the exogenous dioxygenase includes LigA and LigB, the microbial cell is capable of growth utilizing at least one of a cellulose decomposition molecule or a lignin decomposition molecule, and the microbial cell is capable of producing 2-hydroxy-2H-pyran-4,6-dicarboxylic acid.

Provided are nucleic acids and vectors that collectively encode various gene products related to converting styrene to polyhydroxybutyrate (PHB). In some embodiments, the nucleic acids and vectors collectively encode a styrene monooxygenase polypeptide, a flavin reductase polypeptide, a styrene-oxide isomerase polypeptide, and a phenylacetaldehyde dehydrogenase polypeptide, an acetyl-CoA C-acetyltransferase polypeptide, a 3-ketoacyl-ACP reductase polypeptide, a class I poly(R)-hydroxyalkanoic acid synthase polypeptide, and optionally an influx porin polypeptide. Also provided are systems and methods for producing PHB from styrene, methods and systems for remediating polystyrene waste. In some embodiments, the systems are in vivo systems.

Anti-peptide antibodies (APAs) are extremely important tools for biomedical research. Many important techniques, such as immunoblots, ELISA immunoassays, immunocytochemistry, and protein microarrays are intrinsically linked to APA function and completely dependent on APA quality. Unfortunately, not all commercially-available APAs have good antigen binding characteristics; as a result, researchers are often unable to perform high quality protein analysis experiments. This disclosure describes a new method for the scalable production of polyclonal APAs using recombinant antigens. These recombinant peptide antigens have several advantages over traditional peptide antigens which improve the ease and speed of antibody production. The recombinant antigens can be scalably produced and purified much faster than traditional synthetic peptide-conjugates. These recombinant antigen-carriers are designed to specifically aggregate in vivo after administration into the host; this aggregation greatly enhances immunogenicity and may eliminate the need for the use of chemical adjuvants which cause physical irritation and discomfort to the host.

This document describes biochemical pathways for producing 2-aminopimelate from 2,6-diaminopimelate, and methods for converting 2-aminopimelate to one or more of adipic acid, adipate semialdehyde, caprolactam, 6-aminohexanoic acid, 6-hexanoic acid, hexamethylenediamine, or 1,6-hexanediol by decarboxylating 2-aminopimelate into a six carbon chain aliphatic backbone and enzymatically forming one or two terminal functional groups, comprised of carboxyl, amine or hydroxyl group, in the backbone.

Provided are a recombinant yeast producing 3-hydroxypropionic acid (3-HP) and a method for producing 3-HP using the same, more particularly, a recombinant yeast producing 3-HP, comprising an exogenous AADH gene; an endogenous or exogenous ACC gene; an exogenous MCR gene; and an exogenous HPDH gene, and producing 3-HP through [Pyruvate Acetaldehyde.fwdarw.Acetyl-CoA Malonyl-CoA Malonate semialdehyde 3-HP] biosynthesis pathway, and a method for producing 3-HP using the same.

This invention provides microbial organisms, particularly yeasts such as Yarrowia lipolytica, that have one or more disrupted genes. The gene disruption(s) may yield improved production of fatty acyl-CoA derivatives.

This document describes biochemical pathways for producing 7-hydroxyheptanoate methyl ester and heptanoic acid heptyl ester using one or more of a fatty acid O-methyltransferase, an alcohol O-acetyltransferase, and a monooxygenase, as well as recombinant hosts expressing one or more of such exogenous enzymes. 7-hydroxyheptanoate methyl esters and heptanoic acid heptyl esters can be enzymatically converted to pimelic acid, 7-aminoheptanoate, 7-hydroxyheptanoate, heptamethylenediamine, or 1,7-heptanediol.

The invention relates to methods and compositions for modifying a characteristic of a plant without modifying the plant's genome using one or more cells comprising one or more phytohormone genes and at least one polynucleotide of interest, which one or more phytohormone genes and the at least one polynucleotide of interest are expressed in the one or more cells.

The invention relates to a whole-cell catalyst which expresses a recombinant α-dioxygenase or the combination of a recombinant fatty acid reductase and a phosphopantetheinyl transferase which phosphopantetheinylates the fatty acid reductase, and which expresses, in addition to the α-dioxygenase and/or the combination of fatty acid reductase and phosphopantetheinyl transferase, a transaminase, wherein the phosphopantetheinyl transferase and/or transaminase is preferably recombinant; and also to a process for converting a carboxylic acid or dicarboxylic acid or a monoester thereof to an amine or diamine, comprising the steps of contacting the carboxylic acid or dicarboxylic acid or the monoester thereof with a phosphopantetheinylated fatty acid reductase or an α-dioxygenase and contacting the product with a transaminase.