Abstract: Provided herein are methods of production of recombinant E. coli asparaginase. Methods herein allow production of asparaginase in Pseudomonadales host cells at high expression levels and having activity comparable to commercially available asparaginase preparations.

Abstract: Provided herein are methods of production of recombinant E. coli asparaginase. Methods herein allow production of asparaginase in Pseudomonadales host cells at high expression levels and having activity comparable to commercially available asparaginase preparations.

Abstract: Compositions containing conjugates of heparosan polymer with at least one drug are disclosed, along with methods of production and use thereof.

Abstract: An asparaginase enzyme derived from the fungi Basidiomycete, in particular the Basidiomycete is Flammulina velutipes. A method for hydrolysing at least one of L-asparagine or L-glutamine. A method for reducing acrylamide formation in a substance comprising L-asparagine is also described.

Abstract: The disclosure relates to a Gram negative bacterial cell that is transformed with a nucleic acid molecule that encodes a Gram positive twin-arginine translocase and including methods for the production of polypeptides.

Abstract: The present invention relates to a composition for breaking down L-asparagine comprising L-asparaginase, and to a production method for L-asparaginase. The L-asparaginase of the present invention differs from existing L-asparaginase in that it has improved heat stability and exhibits high activity even at high temperatures, and thus it improves upon shortcomings of existing L-asparaginase and so can be used to advantage industrially.

Abstract: The present invention relates to newly identified asparaginase polypeptide variants of SEQ ID NO: 3 and to polynucleotide sequences that encode such novel asparaginase variants. Furthermore the invention relates to the use of these novel asparaginase variants in industrial processes.

Abstract: The present invention relates to a novel mutant of L-asparaginase enzyme characterized in having high thermostability, pH stability and no glutaminase activity useful for therapeutics and the process of preparing the same. The present invention specifically relates to mutant's MTCC 5580, MTCC 5581 and MTCC 5582 characterized in having higher stability, no glutaminase activity etc., to allow their usage in the form of improved protein therapeutics. A thermostable L-asparaginase from P. furiosus was cloned and expressed in E. coli host. The enzyme was engineered at its active site to create three different mutants based on structural and sequence analysis with a E. coli—derived enzyme homologue. The mutants MTCC 5580, MTCC 5581 and MTCC 5582 were tested for their stability, substrate affinity, optimum pH and temperature of activity and cytotoxicity. Based on the studies, all the three enzymes were found thermostable and with no glutaminase activity as compared to other available enzyme EcA II.

Abstract: An asparaginase enzyme derived from the fungi Basidiomycete, in particular the Basidiomycete is Flammulina velutipes. A method for hydrolysing at least one of L-asparagine or L-glutamine. A method for reducing acrylamide formation in a substance comprising L-asparagine is also described.

Abstract: The formation of acrylamide during heat treatment in the production of a food product is reduced by treating the raw material with an enzyme before the heat treatment. The enzyme is capable of reacting on asparagine or glutamine (optionally substituted) as a substrate or is a laccase or a peroxidase.

Abstract: A stable asparaginase solution is disclosed. In one aspect, drinking water is treated to reduce the level of chlorine to enhance the residual enzyme activity of asparaginase. The treatment can occur by removing chlorine constituents or by supplying additives that reduces the level of chlorine. Additives can include reducing agents and chlorine scavengers. Removal technologies can include use of activated carbon, ion exchange, and air stripping.

Abstract: Provided herein are methods for inducing and stabilizing an enzyme activity. Optionally, the enzyme is in a microorganism capable of producing the enzyme. In some embodiments, the enzyme can be nitrile hydratase, amidase, or asparaginase I. Provided are compositions comprising enzymes or microorganisms having induced and/or stabilized activity. Also provided are methods of delaying a plant development process by exposing a plant or plant part to the enzymes or microorganisms having induced and/or stabilized activity.

Abstract: The present invention relates to an asparaginase having the width of the pH activity profile which is at least 3.5. Furthermore the invention relates to newly identified asparaginase polypeptide according to any one of SEQ ID NO: 2 or SEQ ID NO: 4 and to variants thereof and to polynucleotide sequences that encode such novel asparaginase variants. Furthermore the invention relates to the use of these novel asparaginase variants in industrial processes.

Abstract: The invention relates to a method for the preparation of fried vegetable products. In particular, it relates to a method for the preparation of fried vegetable products which have been subjected to an asparagine-reducing enzyme. The method comprises reducing the amount of enzyme product formed on the surface of the enzyme-treated vegetable material due to the action of the asparagine-reducing enzyme. If the amount of enzyme product is reduced before frying, this will contribute to the colour and the quality of the frying oil and of products subsequently fried in the oil and, thus, will minimize the loss of quality of the frying oil. The invention also relates to use of an asparagine-reducing enzyme preparation for preserving the colour of the frying oil.

Abstract: The present invention provides methods and materials by which glycosylation of glycoproteins can be regulated. Methods include the monitoring and regulation of parameters such that a glycoprotein having a desired product quality is obtained.

Abstract: Process for the production of a food product involving at least one heating step, comprising adding one or more enzymes to an intermediate form of said food product in said production process whereby the enzyme is added prior to said heating step in an amount that is effective in reducing the level of amino acids that are present in said intermediate form of said food product which amino acids are involved in the formation of acrylamide during said heating step. The invention also relates to food products obtained from the process of the invention.

Abstract: The formation of acrylamide during heat treatment in the production of a food product is reduced by treating the raw material with an enzyme before the heat treatment. The enzyme is capable of reacting on asparagine or glutamine (optionally substituted) as a substrate or is a laccase or a peroxidase.

Abstract: The formation of acrylamide during heat treatment in the production of a food product is reduced by treating the raw material with an enzyme before the heat treatment. The enzyme is capable of reacting on asparagine or glutamine (optionally substituted) as a substrate or is a laccase or a peroxidase.

Abstract: The present invention relates to an asparaginase having the width of the pH activity profile which is at least 3.5. Furthermore the invention relates to newly identified asparaginase polypeptide according to any one of SEQ ID NO: 2 or SEQ ID NO: 4 and to variants thereof and to polynucleotide sequences that encode such novel asparaginase variants. Furthermore the invention relates to the use of these novel asparaginase variants in industrial processes.

Abstract: Process for the production of a food product involving at least one heating step, comprising adding one or more enzymes to an intermediate form of said food product in said production process whereby the enzyme is added prior to said heating step in an amount that is effective in reducing the level of amino acids that are present in said intermediate form of said food product which amino acids are involved in the formation of acrylamide during said heating step. The invention also relates to food products obtained from the process of the invention.

Abstract: The present invention relates to a novel enzyme composition comprising asparaginase and at least one hydrolysing enzyme, the use of such composition to reduce acrylamide levels in food products and a method to produce food products involving at least one heating step, comprising adding: a. asparaginase and b. at least one hydrolyzing enzyme to an intermediate form of said food product in said production process whereby the asparaginase and at least one hydrolyzing enzyme are added prior to said heating step in an amount that is effective in reducing the level of acrylamide of the food product in comparison to a food product whereto no asparaginase and hydrolyzing enzyme were added.

Abstract: A chemoenzymatic method for the preparation of a homogeneous glycoprotein or glycopeptide, including (a) providing an acceptor selected from the group consisting of GlcNAc-protein and GlcNAc-peptide; and (b) reacting the acceptor with a donor substrate including an activated oligosaccharide moiety, in the presence of a catalyst comprising endoglycosidase (ENGase), to transfer the oligosaccharide moiety to the acceptor and yield the homogeneous glycoprotein or glycopeptide. The donor substrate includes, in a specific implementation, a synthetic oligosaccharide oxazoline. A related method of glycoprotein or glycopeptide remodeling with a predetermined natural N-glycan or a tailor-made oligosaccharide moiety, and a method of remodeling an antibody including a heterogeneous sugar chain, are also described. The disclosed methodology enables glycoprotein drugs to be modified for prolonged half-life in vivo, reduced immunogenicity, and enhanced in vivo activity, and for targeting and drug delivery.

Abstract: The invention relates to new asparaginases having improved properties, preferably improved thermotolerance, such as improved activity at high temperatures and/or improved thermostability. The invention also relates to DNA sequences encoding such improved asparaginases, their production in a recombinant host cell, as well as methods of using the asparaginases, in particular for reduction of acrylamide in foods. The invention furthermore relates to methods of generating and preparing asparaginase variants having improved properties.

Abstract: Compositions for transporting L-asparaginase across the cellular membrane of erythrocytes, comprising a low molecular weight protamine peptide. Process of preparation of compositions comprising conjugates of L-asparaginase and a low molecular weight protamine peptide. Method of treatment comprising administration of adapted L-asparaginase is also described.

Abstract: The invention relates to new asparaginases having improved properties, preferably improved thermotolerance, such as improved activity at high temperatures and/or improved thermostability. The invention also relates to DNA sequences encoding such improved asparaginases, their production in a recombinant host cell, as well as methods of using the asparaginases, in particular for reduction of acrylamide in foods. The invention furthermore relates to methods of generating and preparing asparaginase variants having improved properties.

Abstract: The invention provides a recombinant Escherichia coli host cell for producing an Escherichia coli L-asparaginase II enzyme. The host cell includes an Escherichia coli chromosome and at least one copy of a recombinant extrachromosomal vector, wherein the recombinant extrachromosomal vector encodes the L-asparaginase II enzyme, wherein the host cell chromosome also encodes the same L-asparaginase II enzyme, and wherein the host chromosome does not encode any other isoform of L-asparaginase II.

Abstract: The invention provides a recombinant Escherichia coli host cell for producing an Escherichia coli-asparaginase II enzyme. The host cell includes an Escherichia coli chromosome and at least one copy of a recombinant extrachromosomal vector, wherein the recombinant extrachromosomal vector encodes the L-asparaginase II enzyme, wherein the host cell chromosome also encodes the same L-asparaginase II enzyme, and wherein the host chromosome does not encode any other isoform of L-asparaginase II.

Abstract: The invention relates to new asparaginases having improved properties, preferably improved thermotolerance, such as improved activity at high temperatures and/or improved thermostability. The invention also relates to DNA sequences encoding such improved asparaginases, their production in a recombinant host cell, as well as methods of using the asparaginases, in particular for reduction of acrylamide in foods. The invention furthermore relates to methods of generating and preparing asparaginase variants having improved properties.

Abstract: The present invention relates to an asparaginase having the width of the pH activity profile which is at least 3.5. Furthermore the invention relates to newly identified asparaginase polypeptide according to any one of SEQ ID NO: 2 or SEQ ID NO: 4 and to variants thereof and to polynucleotide sequences that encode such novel asparaginase variants. Furthermore the invention relates to the use of these novel asparaginase variants in industrial processes.

Abstract: The invention relates to new asparaginases having improved properties, preferably improved thermotolerance, such as improved activity at high temperatures and/or improved thermostability. The invention also relates to DNA sequences encoding such improved asparaginases, their production in a recombinant host cell, as well as methods of using the asparaginases, in particular for reduction of acrylamide in foods. The invention furthermore relates to methods of generating and preparing asparaginase variants having improved properties.

Abstract: The invention relates to new asparaginases having improved properties, preferably improved thermotolerance, such as improved activity at high temperatures and/or improved thermostability. The invention also relates to DNA sequences encoding such improved asparaginases, their production in a recombinant host cell, as well as methods of using the asparaginases, in particular for reduction of acrylamide in foods. The invention furthermore relates to methods of generating and preparing asparaginase variants having improved properties.

Abstract: This invention relates to a method of producing a modified (poly)peptide, said method comprising the step of modifying in an organic solvent a crown ether-bound (poly)peptide at one or more carboxylic groups by esterification or thioesterification and/or at the amino group of the N-terminal amino acid by amidation or alkylation. Furthermore provided are (poly)peptides and antibodies obtainable with the method of the invention as well as medical uses thereof.

Abstract: A stable asparaginase solution is disclosed. In one aspect, drinking water is treated to reduce the level of chlorine to enhance the residual enzyme activity of asparaginase. The treatment can occur by removing chlorine constituents or by supplying additives that reduces the level of chlorine. Additives can include reducing agents and chlorine scavengers. Removal technologies can include use of activated carbon, ion exchange, and air stripping.

Abstract: The formation of acrylamide during heat treatment in the production of a food product is reduced by treating the raw material with an enzyme before the heat treatment. The enzyme is capable of reacting on asparagine or glutamine (optionally substituted) as a substrate or is a laccase or a peroxidase.

Abstract: A novel gene (designated 184P1E2) and its encoded protein, and variants thereof, are described wherein 184P1E2 exhibits tissue specific expression in normal adult tissue, and is aberrantly expressed in the cancers listed in Table I. Consequently, 184P1E2 provides a diagnostic, prognostic, prophylactic and/or therapeutic target for cancer. The 184P1E2 gene or fragment thereof, or its encoded protein, or variants thereof, or a fragment thereof, can be used to elicit a humoral or cellular immune response; antibodies or T cells reactive with 184P1E2 can be used in active or passive immunization.

Abstract: Described herein are methods for producing recombinant forms of asparaginase derived from Wolinella succinogenes. In addition, methods for covalent modification of proteins, including asparaginases, by acylation are also provided. Certain embodiments provide for epitopic-labeling of the amino terminus of W. succinogenes asparaginase. Additional embodiments concern methods for the therapeutic utilization of the native, homotetrameric form of W. succinogenes asparaginase, as well as the use of epitopically-labeled or non-epitopically-labeled recombinant W. succinogenes asparaginase (or a covalently modified analog thereof) in the therapeutic treatment of malignant and non-malignant hematological disease and other diseases where asparagine depletion or deprivation would be efficacious or which respond to asparagine depletion or deprivation, as well as their potential utilization in the therapeutic treatment of autoimmune diseases such as rheumatoid arthritis, AIDS, and SLE.

Abstract: A novel alkaline protease VapK suitable for a laundry detergent is disclosed. The gene vapk coding for the protease VapK, the recombinant plasmids containing said gene, and the transformed V. metshnikovii KS1 (pSBCm) with said recombinant plasmid are also disclosed. In addition, a process for producing the protease VapK is disclosed.

Abstract: Genetically-encodable, environmentally-responsive fusion proteins comprising ELP peptides. Such fusion proteins exhibit unique physico-chemical and functional properties that can be modulated as a function of solution environment. The invention also provides methods for purifying the FPs, which take advantage of these unique properties, including high-throughput purification methods that produce high yields (e.g., milligram levels) of purified proteins, thereby yielding sufficient purified product for multiple assays and analyses. The high throughput purification technique is simpler and less expensive than current commercial high throughput purification methods, since it requires only one transfer of purification intermediates to a new multiwell plate.

Abstract: An alkaline protease having the following properties; a gene encoding the same; a microorganism producing the same; and washing compositions containing the same; (i) acting over a broad pH value range of 4 to 13 and achieving, at pH 6 to 12, 80% or more the activity at the optimum pH value; (ii) when treated at 40° C. for 30 minutes, being stable over a pH value range of 6 to 11; (iii) having an isoelectric point of about 8.9 to 9.1; and (iv) having casein digesting activity that is not inhibited by oleic acid. The alkaline protease of the present invention is highly stable to various surface active agents and fatty acids, and exhibits high stability to oxidizing agents, and is therefore useful as an enzyme to be used in detergents for automatic dishwashers and laundry detergents, both containing bleaching components.

Abstract: Disclosed are polypeptides which originate from mammal, having L-asparaginase activity. The polypeptides are easily prepared by applying recombinant DNA techniques to DNAs encoding the polypeptides and they exert satisfactory effects in the treatment and/or the prevention for diseases caused by tumor cells dependent on L-asparagine, and cause no substantial serious side effects even when administered to humans in relatively-high dose.

Abstract: Disclosed are polypeptides which originate from mammal, having L-asparaginase activity. The polypeptides are easily prepared by applying recombinant DNA techniques to DNAs encoding the polypeptides and they exert satisfactory effects in the treatment and/or the prevention for diseases caused by tumor cells dependent on L-asparagine, and cause no substantial serious side effects even when administered to humans in relatively-high dose.

Abstract: Disclosed are polypeptides which originate from mammal, having L-asparaginase activity. The polypeptides are easily prepared by applying recombinant DNA techniques to DNAs encoding the polypeptides and they exert satisfactory effects in the treatment and/or the prevention for diseases caused by tumor cells dependent on L-asparagine, and cause no substantial serious side effects even when administered to humans in relatively-high dose.

Abstract: Disclosed is a DNA coding for mammalian L-asparaginase. Transformants introduced with the DNA effectively produce desired amounts of mammalian L-asparaginase such as those from humans, guinea pigs, and mice. The DNA is also useful as a probe for screening a DNA coding for desired mammalian L-asparaginase.

Abstract: Described herein are methods for producing recombinant forms of asparaginase derived from Wolinella succinogenes. In addition, methods for covalent modification of proteins, including asparaginases, by acylation are also provided. Certain embodiments provide for epitopic-labeling of the amino terminus of W. succinogenes asparaginase. Additional embodiments concern methods for the therapeutic utilization of the native, homotetrameric form of W. succinogenes asparaginase, as well as the use of epitopically-labeled or non-epitopically-labeled recombinant W. succinogenes asparaginase (or a covalently modified analog thereof) in the therapeutic treatment of malignant and non-malignant hematological disease and other diseases where asparagine depletion or deprivation would be efficacious or which respond to asparagine depletion or deprivation, as well as their potential utilization in the therapeutic treatment of autoimmune diseases such as rheumatoid arthritis, AIDS, and SLE.

Abstract: Disclosed are polypeptides which originate from mammal, having L-asparaginase activity. The polypeptides are easily prepared by applying recombinant DNA techniques to DNAs encoding the polypeptides and they exert satisfactory effects in the treatment and/or the prevention for diseases caused by tumor cells dependent on L-asparagine, and cause no substantial serious side effects even when administered to humans in relatively-high dose.

Abstract: Disclosed is a DNA coding for mammalian L-asparaginase. Transformants introduced with the DNA effectively produce desired amounts of mammalian L-asparaginase such as those from humans, guinea pigs, and mice. The DNA is also useful as a probe for screening a DNA coding for desired mammalian L-asparaginase.

Abstract: The present invention relates to: parasitic helminth asparaginase proteins; parasitic helminth asparaginase nucleic acid molecules, including those that encode such asparaginase proteins; antibodies raised against such asparaginase proteins; and compounds that inhibit parasitic helminth asparaginase activity. The present invention also includes methods to obtain such proteins, nucleic acid molecules, antibodies, and inhibitory compounds. Also included in the present invention are therapeutic compositions comprising such proteins, nucleic acid molecules, antibodies and/or inhibitory compounds as well as the use of such therapeutic compositions to protect animals from diseases caused by parasitic helminths.

Abstract: The present invention relates to: parasitic helminth asparaginase proteins; parasitic helminth asparaginase nucleic acid molecules, including those that encode such asparaginase proteins; antibodies raised against such asparaginase proteins; and compounds that inhibit parasitic helminth asparaginase activity. The present invention also includes methods to obtain such proteins, nucleic acid molecules, antibodies, and inhibitory compounds. Also included in the present invention are therapeutic compositions comprising such proteins, nucleic acid molecules, antibodies and/or inhibitory compounds as well as the use of such therapeutic compositions to protect animals from diseases caused by parasitic helminths.

Abstract: A hapten is described which may be used to elicit antibodies that catalyze the deamidation of asparginyl-glycyl dipeptides to form two products, the isoaspartyl-glycyl dipeptide and the aspartyl-glycyl dipeptide. A general synthetic scheme is also presented which shows how to modify the hapten to provide specificity for a particular protein in the antibodies that are elicited by the (modified) hapten. Antibodies which catalyze the the deamidation reaction are also described.

Abstract: A process is provided for the purification of L-asparaginase by contacting a crude extract of L-asparaginase with a solid medium having cation exchange groups so as to adsorb L-asparaginase on the support and eluting adsorbed L-asparaginase from the support. The cation exchange groups comprise sulphonate groups and the elution step is carried out at a pH which is higher than the pH used in the contacting step.