A biopolymer composition can be formed based, at least in part, on a recombinantly expressed protein, expressed from a DNA coding sequence of a source protein, and the recombinantly expressed protein can optionally comprise one or more tags that enhance the crosslinking capacity of the protein. It was determined that such biopolymer composition can be suitable for use to obtain, for example, a biodegradable textile that exhibits a functional characteristic associated with the recombinantly expressed protein.

The purpose of the present invention is to provide a processing technology for enhancing the crosslinkage effect of a protein. A processed protein obtained by a method of producing a processed protein, said method comprising a crosslinkage step for treating a protein with laccase and transglutaminase, has an enhanced crosslinkage effect.

The present disclosure relates generally to biomarkers and peptide arrays, and, more particularly, to a method of using a peptide array to identify biomarkers for an autoimmune disease such as, e.g., Celiac disease. Furthermore, a set of novel biomarkers for Celiac disease, having high sensitivity and specificity, are disclosed in addition to method of treatment using the novel biomarkers.

Lipase enzymes, methods of making lipase enzymes, methods of using lipase enzymes in food, feed, personal care, detergents, grain processing, pulp and paper processing, biofuels, ethanol production, textiles, dairy processing, cocoa butter processing, cocoa extraction, dietary supplements, coffee processing, coatings, water treatment, and oil processing.

Compositions for a phage particle are disclosed. The phage particle is non-replicating and includes at least one heterologous nucleic acid sequence that is capable of being expressed in a target bacteria. The expressed heterologous nucleic acid sequence is non-lethal to the target bacteria.

Provided herein are conjugated immunoglobulins and methods for generating conjugated immunoglobulins using a microbial transglutaminase.

The invention relates to an aqueous binder composition for mineral fibers comprising at least one polyelectrolytic hydrocolloid.

The present invention describes a biomaterial made from a collagen composition comprising (i) partially hydrolyzed collagen and (ii) collagen and/or fully hydrolyzed collagen. The biomaterial is useful in producing a processed biomaterial which may be a leather-like material.

Cheese that shows a suppressed decrease in texture and/or stretchability of cheese due to heating, may be produced by allowing glucose oxidase, α-glucosidase, transglutaminase, or a combination of such enzymes to act on raw cheese. Cheese analogues improved in meltability and/or stretchability during heating, may be produced by allowing α-glucosidase to act on a mixture containing plant-derived oil and starch, or starch before mixing with plant-derived oil.

Site-specific modification of proteins with microbial transglutaminase (MTG) is a powerful and versatile strategy for a controlled modification of proteins under physiological conditions. We present evidence that solid-phase microbead-immobilization can be used to site-specifically and efficiently attach different functional molecules important for further downstream applications to proteins of therapeutic relevance including scFV, Fab-fragment and antibodies. We demonstrate that MTG remained firmly immobilized with no detectable column bleeding and that enzyme activity was sustained during continuous operation, which allowed for a convenient recycling of the enzyme, thus going beyond solution-phase MTG conjugation. In addition it is showed that immobilized MTG shows enhanced selectivity towards a certain residue in the presence of several reactive residues which are all targeted if the conjugation was carried out in solution. It is also reported on the site-specific lysine conjugation of antibodies using potent glutamine containing peptides with immobilized and MTG in solution. In addition, the generation of dual site-specifically conjugated IgG1 with immobilized and MTG in solution is reported, i.e. site-specific conjugation to glutamine and lysine residues of IgG1 antibody. Site-specific glutamine conjugation with small peptides containing a lysine residue and a functional moiety is also described.