Abstract: Disclosed are mammalian cells and mammalian cell lines that have a reduced load of remnants of past viral/retroviral infections and methods of producing and using the same.

Abstract: The disclosure provides a modified UDP-GlcNAc:Lysosomal Enzyme GlcNAc phosphotransferase with enhanced ability to phosphorylate lysosomal enzymes and methods of use thereof.

Abstract: The present disclosure provides improved genome editing compositions and methods for editing a CBLB gene. The disclosure further provides genome edited cells for the prevention, treatment, or amelioration of at least one symptom of, a cancer, an infectious disease, an autoimmune disease, an inflammatory disease, or an immunodeficiency.

Abstract: The present invention provides assays and methods for studying DNA topology and topoisomerases. The assays and methods utilize a circular plasmid DNA comprising one or more hairpin structures and the ability of T5 exonuclease (T5E) to digest the circular plasmid DNA in a specific configuration. The assays and methods can be used as a high throughput screening for inhibitors of, for example, DNA gyrases and DNA topoisomerases I for anticancer drug and antibiotics discovery.

Abstract: The technology provided herein pertains to methods for the modification of a target nucleic acid in vitro, ex vivo or in vivo in the genome of a cell by using a pre-assembled complex comprising a nucleic acid and a metal nanocluster and exposing the complex bound to a target nucleic acid to electromagnetic radiation.

Abstract: The present invention relates to a method for the production of in vitro glycoengineered erythropoiesis stimulating protein, comprising the steps of providing sialic acid free erythropoiesis stimulating protein, treating the erythropoiesis stimulating protein with N-Acetyl-Glucosamin-transferase B3GNT2, treating the erythropoiesis stimulating protein with galactosyltransferase, and treating the erythropoiesis stimulating protein with sialyltransferase.

Abstract: Recombinant DP04-type DNA polymerase variants with amino acid substitutions that confer modified properties upon the polymerase for improved single molecule sequencing applications are provided. Such properties may include enhanced binding and incorporation of bulky nucleotide analog substrates into daughter strands and the like. Also provided are compositions comprising such DP04 variants and nucleotide analogs, as well as nucleic acids which encode the polymerases with the aforementioned phenotypes.

Abstract: The present invention relates to a cell comprising a chimeric antigen receptor (CAR) and a constitutively active or inducible Signal Transducer and Activator of Transcription (STAT) molecule.

Abstract: The present invention relates to a process for forming a functionalised dietary fibre comprising admixing an enzyme and an aqueous suspension of dietary fibre, wherein said dietary fibre is at a D50 particle size distribution of less than 30 microns after degradation by the enzyme and comprises less than 25 wt. % soluble fibres and at least 40% wt. % cellulose; denaturing said enzyme to form a functionalised, amphiphilic dietary fibre with adsorbed enzyme. The present invention further relates to a Pickering particle comprising a functionalised dietary fibre and denatured enzyme and the use of the functionalised dietary fibre and denatured enzyme according to present invention or the Pickering particle according to the present invention to stabilize an emulsion.

Abstract: A transformant obtained by introducing a DNA of (a1), (a2), or (a3) below, and (b) an alcohol dehydrogenase gene, into a bacterium of the genus Hydrogenophilus, can efficiently produce isobutanol utilizing carbon dioxide as a sole carbon source. (a1) DNA which consists of a base sequence of SEQ ID NO: 1; (a2) DNA which consists of a base sequence having 90% or more identity with SEQ ID NO: 1, the DNA encoding a polypeptide having 2-keto-acid decarboxylase activity; (a3) DNA which hybridizes with a DNA consisting of a base sequence complementary to SEQ ID NO: 1 under stringent conditions, and which encodes a polypeptide having 2-keto-acid decarboxylase activity.

Abstract: The present disclosure pertains to methods of growing bacterial host cells in a low-density polyethylene (LDPE) bag to produce plasmid DNA or express recombinant protein. The LDPE bag is filled with media, an antibiotic, and host bacterial cells that have been transformed with plasmid DNA encoding a protein of interest. The LDPE bag is sealable to the external environment and incubated at a growth temperature until a desired concentration of bacteria is achieved. When plasmid DNA is desired, host cells are harvested and plasmid DNA is separated from host cell components. When recombinant protein is desired, expression is induced while host cells are in the LDPE bag, followed by the harvest and separation of the recombinant protein. The LDPE bags are sterile and conducive to bacterial growth equal to or greater than that afforded by conventional shake flasks under similar growth conditions.

Abstract: The present invention relates to novel nucleic acid sequences encoding bacterial xylose isomerases that upon transformation of a eukaryotic microbial host cell, such as yeast, to confer to the host cell the ability of isomerising xylose to xylulose. The nucleic acid sequences encode xylose isomerases that originate from bacteria such as Eubacterium sp., Clostridium cellulosi and others. The invention further relates to fermentation processes wherein the transformed host cells ferment a xylose-containing medium to produce ethanol or other fermentation products.

Abstract: The present disclosure describes a variant polypeptide having lipolytic activity, wherein the variant has an amino acid sequence which, when aligned with the amino acid sequence as set out in SEQ ID NO: 2, comprises at least one substitution of an amino acid residue at a position corresponding to any of the positions 113, 122, 138, 141, 179, 282, 284, 286, 295, said positions being defined with reference to SEQ ID NO: 2, and wherein said variant has at least 70% identity with the mature polypeptide having lipolytic activity as set out in SEQ ID NO: 2. Such a variant polypeptide may be used in the preparation of a baked product.

Abstract: Some aspects of this disclosure provide a fusion protein comprising a guide nucleotide sequence-programmable DNA binding protein domain (e.g., a nuclease-inactive variant of Cas9 such as dCas9), an optional linker, and a recombinase catalytic domain (e.g., a tyrosine recombinase catalytic domain or a serine recombinase catalytic domain such as a Gin recombinase catalytic domain). This fusion protein can recombine DNA sites containing a minimal recombinase core site flanked by guide RNA-specified sequences. The instant disclosure represents a step toward programmable, scarless genome editing in unmodified cells that is independent of endogenous cellular machinery or cell state.

Abstract: The present invention relates to sensors and methods for detecting carbohydrates, such as lactose, in a sample. The sensors and methods may also be used to determine the amount of carbohydrate in the sample.

Abstract: The invention relates to a process for the production of ethanol comprising fermenting a (optionally liquefied) corn slurry under anaerobic conditions in the presence of a recombinant yeast; and recovering the ethanol, wherein said recombinant yeast functionally expresses a heterologous nucleic acid sequence encoding a glucoamylase having an amino acid sequence according to SEQ ID NO: 1 or which glucoamylase is a functional homologue thereof having a sequence identity of at least 80%, or which glucoamylase is a functional homologue which is derived, by way of one or more amino acid substitutions, deletions or insertions, from the amino acid sequence of SEQ ID NO: 1, and wherein the process comprises dosing a glucoamylase at a concentration of 0.05 g/L or less.

Abstract: A modified endoinulinase is provided, comprising modified wild-type T. purpuregenus endoinulinase, or a functional fragment thereof, in which an amino acid residue at each one of one or more positions corresponding to 128, 316, 344, 350 or 504 of wild-type T. purpuregenus endoinulinase is substituted, wherein: (i) a tyrosine residue corresponding to Y128 is substituted with H, K or R; a glutamate residue corresponding to E344 is substituted with K, H or R; and a threonine residue corresponding to T504 is substituted with M, S or Y; and optionally an alanine residue corresponding to A316 is substituted with T, S, C or M; (ii) a tyrosine residue corresponding to Y128 is substituted with H, K or R; a glutamate residue corresponding to E344 is substituted with K, H or R; a threonine residue corresponding to T504 is substituted with M, S or Y; and a glutamine residue corresponding to Q350 is substituted with L, G, A, V or I; or (iii) a tyrosine residue corresponding to Y128 is substituted with H, K or R.

Abstract: The present disclosure provides activated formylglycine-generating enzymes (FGE), methods of producing activated FGE, and their use in methods of producing a protein comprising a formylglycine (FGly) residue. The methods of producing activated FGE, as well as methods of use of activated FGE in producing FGly-containing proteins, include both cell-based and cell-free methods. Compositions and kits that find use, e.g., in practicing the methods of the present disclosure are also provided.

Abstract: The disclosure discloses a genetically engineered strain for producing porcine myoglobin and fermentation and purification thereof, and belongs to the technical field of genetic engineering. The disclosure realizes efficient secretion and expression of porcine myoglobin by integrating the gene of porcine myoglobin in P. pastoris. On this basis, optimization of the medium and culture conditions of recombinant P. pastoris can significantly increase the titer of porcine myoglobin, so that the titer can reach 285.42 mg/L under fermenter conditions. In addition, by creatively adding different concentrations of ammonium sulfate to fermentation broth step by step, the purity of myoglobin obtained by final concentration is up to 88.0%, and the purification rate is up to 66.1%.

Abstract: Provided herein are deglycosylating enzymes that remove a broad range of N-glycans from N-glycosylated proteins. Further provided are methods of recombinantly producing and expressing the deglycosylating enzymes. The presently described deglycosylating enzymes can be used to produce free glycans for characterization, and for prebiotic and immunostimulatory uses. In addition, the presently described deglycosylating enzymes can be used to produce deglycosylated proteins for characterization, to improve digestion, and to reduce immunogenicity.