Abstract: A2M polypeptide compositions containing a non-natural bait region are disclosed. Methods of producing wild-type and variant A2M polypeptides and polynucleotides containing a non-natural bait region are also disclosed. The bait regions of the variant A2M polypeptides demonstrate enhanced protease inhibitory characteristics compared to wild-type A2M. Variant A2M polypeptides that demonstrate longer half-lives upon administration to an organism compared to wild-type A2M are disclosed. The A2M compositions are useful in treating a number of diseases and conditions including inflammation, chronic wounds, and diseases with a pathology associated with proteases.

Abstract: The present invention provides for a genetically modified host cell and related methods and materials for the biocatalytic production of an ?,?-dicarboxylic acids (DCAs) and/or mono-methyl ester derivatives of dicarboxylic acids (DCAMMEs).

Abstract: Provided are methods and compositions relating to conjugation of nucleic acids and proteins of interest under conditions that maintain protein activity. The nucleic acid-protein conjugates may be used in nucleic acid nanostructures such as those generated using DNA origami methods.

Abstract: A method for producing an objective substance such as vanillin and vanillic acid is provided. An objective substance is produced from a carbon source or a precursor of the objective substance by using a microorganism having an objective substance-producing ability, which microorganism has been modified so that the activity of enolase is reduced.

Abstract: Multi-carbon compounds such as ethanol, n-butanol, sec-butanol, isobutanol, tert-butanol, fatty (or aliphatic long chain) alcohols, fatty acid methyl esters, 2,3-butanediol and the like, are important industrial commodity chemicals with a variety of applications. The present invention provides metabolically engineered host microorganisms which metabolize methane (CH4) as their sole carbon source to produce multi-carbon compounds for use in fuels (e.g., bio-fuel, bio-diesel) and bio-based chemicals. Furthermore, use of the metabolically engineered host microorganisms of the invention (which utilize methane as the sole carbon source) mitigate current industry practices and methods of producing multi-carbon compounds from petroleum or petroleum-derived feedstocks, and ameliorate much of the ongoing depletion of arable food source “farmland” currently being diverted to grow bio-fuel feedstocks, and as such, improve the environmental footprint of future bio-fuel, bio-diesel and bio-based chemical compositions.

Abstract: The present invention provides novel methods for reducing the serine protease and/or serine protease zymogen content of a plasma-derived protein composition. Also provided are methods for manufacturing plasma-derived protein compositions having reduced serine protease and\or serine protease zymogen content. Among yet other aspects, the present invention provides aqueous and lyophilized compositions of plasma-derived proteins having reduced serine protease and/or serine protease zymogen content. Yet other aspects include methods for treating, managing, and/or preventing a disease comprising the administration of a plasma-derived protein composition having a reduced serine protease or serine protease zymogen content.

Abstract: Disclosed herein are compositions and methods for treating celiac sprue.

Abstract: The present disclosure discloses an engineering strain and application thereof in joint production of Danshensu and alanine, and belongs to the technical field of bioengineering. The present disclosure constructs a three-enzyme co-expression genetic engineering strain, and realizes joint production of Danshensu and alanine. Further, the transport of a substrate is promoted and decomposition of products is reduced by knocking out or enhancing expression of related genes on E. coli genome. The genetic engineering strain provided by the present disclosure can produce optically pure D-danshensu and L-danshensu, and jointly produce pyruvic acid. The production process is simple, raw materials are easily available, impurities are fewer, and a good industrial application prospect is achieved.

Abstract: The invention relates to a process for the preparation of a sugar and/or fermentation product from lignocellulosic material.

Abstract: The invention concerns fusion proteins, wherein two endoglycosidases are fused, possibly via a linker. The fusion enzymes according to the invention have structure (1): EndoX-(L)p-EndoY (1), wherein EndoX is an endoglycosidase, EndoY is an endoglycosidase distinct from EndoX, L is a linker and p is 0 or 1. Such fusion enzymes capable of trimming glycoproteins comprising at least two distinct glycoforms in a single step. The invention further concerns the use of the fusion enzyme according to the invention for trimming glycoproteins. In another aspect, the invention relates to the process of production of the fusion enzyme. In a further aspect, the inventions concerns a process for trimming glycoproteins, comprising trimming the glycoprotein with a fusion enzyme according to the invention, to obtain a trimmed glycoprotein.

Abstract: Disclosed are methods and systems for the analysis activity of enzyme disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13 (ADAMTS13) in a sample. The methods and systems disclosed herein can be useful for diagnosis of thrombotic thrombocytopenic purpura in a patient.

Abstract: Provided is a method for producing a methacrylic acid ester using a biocatalyst, said method comprising a step for treating methacrylyl-CoA with an alcohol or phenol in the presence of an alcohol acyltransferase to synthesize the methacrylic acid ester. According to this production method, a methacrylic acid ester can be efficiently produced while largely reducing energy, resource and environmental load, compared with the conventional chemical production processes.

Abstract: Objects of the present invention are to provide a preparation method which makes it possible to obtain porous microcarriers having unique properties and a unique particle size distribution and to provide porous gelatin microcarriers having excellent cell growth properties. According to the present invention, there are provided a method for preparing porous recombinant gelatin microcarriers that includes an emulsification step in which an emulsifier having a specific HLB value is used in a specific amount, and provided porous gelatin microcarriers having specific voids.

Abstract: The present invention relates to a genetically engineered yeast (e.g., Crabtree negative) that express a heterologous xylose isomerase. In a fermentation method the engineered yeast are capable of producing a bioproduct, such as ethanol, in a fermentation medium that includes xylose. Desirable bioproduct titers can be achieved when materials such as acetate are present in the fermentation medium.

Abstract: A polynucleotide encoding a modified luciferase polypeptide. The modified luciferase polypeptide has at least 60% amino acid sequence identity to a wild-type Oplophorus luciferase and includes at least one amino acid substitution at a position corresponding to an amino acid in a wild-type Oplophorus luciferase of SEQ ID NO:1. The modified luciferase polypeptide has at least one of enhanced luminescence, enhanced signal stability, and enhanced protein stability relative to the wild-type Oplophorus luciferase.

Abstract: A filamentous fungus mutant strain showing improved secretory protein production and a method of producing a protein using the filamentous fungus are provided. The method of producing a protein comprises a step of culturing a filamentous fungus mutant strain in which a function of tubulin is reduced or lost and collecting a protein from a culture product.

Abstract: The present invention provides polypeptides related to Ralstonia proteins, nucleic acids encoding the same, compositions comprising the same, kits comprising the same, non-human transgenic animals comprising the same, and methods of using the same.

Abstract: Provided herein are methods for producing products containing strained carbocycles, such as cyclopropene moieties and/or bicyclobutane moieties. The methods include combining an alkyne and a carbene precursor in the presence of a heme protein, e.g., a cytochrome P450, under conditions sufficient to form the strained carbocycle. Reaction mixtures for producing strained carbocycles are also described, as well as whole-cell catalysts comprising heme proteins and variants thereof for forming cyclopropenes, bicyclobutanes, and related products.

Abstract: A protein crystal comprising a first protein crystal having available space in the lattice, wherein a second protein crystal and a moiety can be accommodated in the available space in the lattice. The first and second proteins are co-expressed from one or more nucleic acid constructs. In a preferred embodiment, the first protein is the p21-activated kinase PAK4, the second protein is the PAK4 kinase inhibitor Inka1, and the moiety comprises a reporter molecule such as fluorescent proteins or tags and is fused to the iBox or iBox-C or Inka1. Preferably the crystal is formed in cellulo. Also provided is a fusion protein comprising the first protein and the second protein, wherein upon crystallisation the second protein fits within the available space in the lattice of the first protein, along with the moiety. Methods for producing the protein crystal are also disclosed.

Abstract: The present invention relates to a lipase variant of a parent lipase, which variant has lipase activity, at least 75% but less than 100% sequence identity to SEQ ID NO: 3 and comprises a substitution at one or more positions corresponding to positions 1; 2; 3; 4; 5; 6; 7; 9; 10; 11; 12; 13; 14; 15; 17; 18; 29; 30; 33; 34; 36; 37; 38; 40; 41; 43; 44; 45; 46; 47; 49; 50; 5 51; 52; 54; 55; 57; 58; 59; 60; 69; 70; 71; 72; 81; 82; 85; 86; 87; 89; 90; 91; 92; 94; 95; 96; 97; 99; 100; 101; 102; 103; 105; 108; 111; 115; 116; 118; 119; 120; 122; 123; 124; 126; 127; 128; 129; 130; 131; 132; 133; 134; 136; 144; 152; 155; 157; 158; 159; 161; 162; 163; 177; 178; 181; 182; 184; 185; 187; 189; 191; 196; 197; 199; 203; 205; 206; 207; 208; 209; 211; 215; 220; 221; 222; 223; 224; 226; 229; 230; 232; 235; 236; 240; 242; 243; 244; 247; 248; 252; 254; 255; 257; 10 260; 261; 262 of SEQ ID NO: 3.