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 purpose of the present invention is to provide a novel feature by which the strength of tofu can be increased with a method for producing tofu using an enzyme. Tofu obtained by a tofu production method that includes a crosslinking step in which laccase is acted on soy milk exhibits increased strength, and when the tofu production method thereof further includes a boiling step after the crosslinking step, the strength of the obtained tofu is dramatically improved.

The current invention discloses enzyme-based compositions for converting raw natural fibres from plant derived biomass into high quality textile grade fibres. The invention discloses at least one multi-component enzymatic formulation, and the optimal conditions for using these enzymatic formulations, which result in production of textile grade fibres from raw natural fibres. These textile grade fibres can be used in any industry, because of their high-quality parameters, and high spinnability index.

The present invention relates to laccase variants and uses thereof as eco-friendly biocatalysts in various industrial processes. More in particular, the invention relates to a polypeptide with laccase activity comprising an amino acid sequence that is at least 90% identical to the amino acid sequence according to SEQ ID NO: 1, wherein the polypeptide comprises at least one amino acid selected from the group consisting of Alanine, Proline, Aspartic acid, Isoleucine, Proline, Proline, Threonine and Proline at a position corresponding to of positions 253, 128, 384, 364, 292, 450, 33 and 322 in SEQ ID NO: 1 respectively.

Devices, systems, and compositions of matter involving enzyme-mediated bioelectrocatalysis are disclosed and described. An enzyme electrode can include an electrode, a bioelectric material coupled to the electrode, the bioelectric material further including a water-permeable polymer matrix, a planar linker covalently coupled to the water-permeable polymer matrix and noncovalently coupled to the electrode, and electrochemically active oxidoreductase enzyme molecules functionally embedded in the water-permeable polymer matrix.

Provided is a method of modifying a first cannabinoid into a second cannabinoid or a non-cannabinoid. The method comprises combining the first cannabinoid with an enzyme that can modify the first cannabinoid into the second cannabinoid or non-cannabinoid under conditions where the first cannabinoid is modified into the second cannabinoid or non-cannabinoid. Also provided is a non-naturally occurring enzyme that can modify a first cannabinoid into a second cannabinoid or a non-cannabinoid. A nucleic acid encoding that enzyme is additionally provided. Further provided is a non-naturally occurring nucleic acid that encodes an enzyme having the enzymatic activity of the above non-naturally occurring enzyme. An expression cassette comprising that nucleic acid is additionally provided. A cell comprising the above expression cassette is further provided. Also provided is a plant expression cassette comprising the above-identified nucleic acid.

The present invention relates to methods and engineered microbial hosts useful for treating lignin or a derivative thereof. In some embodiments, the host has one or more exogenous nucleic acid sequences that encode a ligninase (e.g., a laccase and/or a peroxidase).

The invention relates to a polypeptide comprising an exoglucanase catalytic domain comprising a sequence selected from the group consisting of SEQ ID NO: 1, SEQ ID NO: 2 and SEQ ID NO: 3, and to a polypeptide having beta-glucosidase activity comprising a sequence selected from the group consisting of SEQ ID NO: 6, SEQ ID NO: 7 and SEQ ID NO: 8, and to functionally equivalent variants thereof that maintain or improve their catalytic activity. Additionally, the invention relates to an enzyme cocktail comprising said polypeptide(s) and an endoglucanase. Further, the invention also relates to methods for hydrolysing cellulose to cellobiose and/or cellotetraose, cellobiose and/or cellotetraose to glucose and cellulose to glucose, and to produce bioethanol, using the polypeptides or enzyme cocktails of the invention, and to the uses of the polypeptides and enzyme cocktails of the invention for hydrolysing cellulose to cellobiose and/or cellotetraose, cellobiose and/or cellotetraose to glucose and cellulose to glucose, and to produce bioethanol.

The invention relates to obtaining lignin preparations of desirable molecular size and properties. It describes a method of de-polymerizing lignin of high molecular weight into low molecular weight lignin. More in particular, the invention provides a method for producing lignin with a low molecular weight wherein high molecular weight lignin is contacted with an alkaline laccase at alkaline pH in a reaction vessel and wherein the lignin with a molecular weight below 2 kDa is selectively removed from the reaction vessel during the reaction.

The technical field of enzyme immobilization, and particularly, an organic-inorganic hybrid nanoflower and a preparation method thereof. The organic-inorganic hybrid nanoflower is a flower-like immobilized enzyme formed by self-assembly of a layered rare earth compound as an inorganic carrier and a biological enzyme as an organic component. The layered rare earth compound is Ln.sub.2(OH).sub.5NO.sub.3.nH.sub.2O, where Ln is one or more of La, Ce, Pr, Nd, Sm, Eu, Gd, Tb, Dy, Ho, Er, Tm, Yb, or Y, and n=1.1-2.5. The biological enzyme is one or more of α-amylase, horseradish peroxidase, or laccase. A layered rare earth compound is used as the inorganic carrier for the organic biological enzyme to form the flower-like immobilized enzyme. The immobilized enzyme has better stability and higher catalytic performance when compared with a free enzyme.