The present invention describes a intracellular produced lactase, which comprises less than 40 units arylsulfatase activity per NLU of lactase activity. The invention also provides a process comprising treating a substrate with an enzyme preparation, wherein the enzyme preparation is substantially free from arylsulfatase.

The present invention describes a intracellular produced lactase, which comprises less than 40 units arylsulfatase activity per NLU of lactase activity. The invention also provides a process comprising treating a substrate with an enzyme preparation, wherein the enzyme preparation is substantially free from arylsulfatase.

The present invention relates to an immobilized capping enzyme, preferably an immobilized Vaccinia virus capping enzyme. Furthermore, the present invention relates to an immobilized cap-specific nucleoside 2′-O-methyltransferase, preferably an immobilized Vaccinia virus cap-specific nucleoside 2′-O-methyltransferase. Moreover, the present invention relates to a method for immobilizing said enzymes and to a method of using said enzymes for the addition of a 5′-cap structure to RNAs. Moreover, the present invention relates to an enzyme reactor for performing the capping reaction using said immobilized enzymes and the subsequent separation of the 5′-capped RNA product. In addition, the present invention relates to a kit comprising the capping enzyme and/or the cap-specific nucleoside 2′-O-methyltransferase.

The present invention relates to an immobilized capping enzyme, preferably an immobilized Vaccinia virus capping enzyme. Furthermore, the present invention relates to an immobilized cap-specific nucleoside 2′-O-methyltransferase, preferably an immobilized Vaccinia virus cap-specific nucleoside 2′-O-methyltransferase. Moreover, the present invention relates to a method for immobilizing said enzymes and to a method of using said enzymes for the addition of a 5′-cap structure to RNAs. Moreover, the present invention relates to an enzyme reactor for performing the capping reaction using said immobilized enzymes and the subsequent separation of the 5′-capped RNA product. In addition, the present invention relates to a kit comprising the capping enzyme and/or the cap-specific nucleoside 2′-O-methyltransferase.

A method for enhancing the enzymatic efficiency of an enzyme added to poultry feed for a living subject, comprises adding a cellulose-degrading enzyme to a mobile enzyme sequestration platform (MESP) so as to form an enzyme-MESP complex; adding the enzyme-MESP complex to poultry feed for a living subject; the enzyme efficiency of the cellulose-degrading enzyme of the enzyme-MESP complex after being exposed to a first adverse environment for a first period of time is at least 50% higher than the enzyme efficacy of the cellulose-degrading enzyme independent of the MESP being exposed to the first adverse environment for the first period of time.

A method for enhancing the enzymatic efficiency of an enzyme added to poultry feed for a living subject, comprises adding a cellulose-degrading enzyme to a mobile enzyme sequestration platform (MESP) so as to form an enzyme-MESP complex; adding the enzyme-MESP complex to poultry feed for a living subject; the enzyme efficiency of the cellulose-degrading enzyme of the enzyme-MESP complex after being exposed to a first adverse environment for a first period of time is at least 50% higher than the enzyme efficacy of the cellulose-degrading enzyme independent of the MESP being exposed to the first adverse environment for the first period of time.

Compositions and methods relating to DNase fusion polypeptides are disclosed. The fusion polypeptides include a biologically active DNase joined to the amino-terminus of an immunoglobulin Fc region via a flexible polypeptide linker (e.g., a linker containing at least 26 amino acid residues). Typically, the DNase is a hyperactive and/or actin-resistant DNase1 variant (e.g., a variant of human DNase1 having one or more amino acid substitutions selected from substitutions at Asp-53, Tyr-65, Glu-69, Arg-74, Gly-105, and Ala-114 according to amino acid position numbering of mature wild-type human DNase1) or a DNase1L3 variant (e.g., a variant of human DNase1L3 in which the native nuclear localization signals are removed). In some embodiments, the fusion polypeptide includes a polypeptide segment located carboxyl-terminal to the Fc region and which may be, e.g., a biologically active paraoxonase. Also disclosed are dimeric proteins comprising first and second DNase fusion polypeptides as disclosed herein. The fusion polypeptides and dimeric proteins are useful in methods for therapy, including methods for treating diseases and disorders characterized by NETosis.

An improved strain of E. coli for autoinduction of protein expression but also of autolytic enzymes thereby enabling combined autolysis and auto DNA/RNA hydrolysis. This combination of these two mechanisms improves cellular lysis and DNA removal and expounds the benefits of two stage production of a protein product. This system enables greater than 95% lysis and hydrolysis due to tightly controlled expression the genes. The autolytic genes may encode a lysozyme and a benzonase.

An improved strain of E. coli for autoinduction of protein expression but also of autolytic enzymes thereby enabling combined autolysis and auto DNA/RNA hydrolysis. This combination of these two mechanisms improves cellular lysis and DNA removal and expounds the benefits of two stage production of a protein product. This system enables greater than 95% lysis and hydrolysis due to tightly controlled expression the genes. The autolytic genes may encode a lysozyme and a benzonase.

Compositions comprise statistically random heteropolymers complexed with active proteins, and are formulated and used in stimuli-responsive materials and nanoreactors composed of proteins and synthetic materials.