A protein scaffold includes a plurality of EutM subunits and a multi-enzyme cascade. The multi-enzyme cascade includes a first enzyme attached to the first EutM subunit and a second enzyme attached to the second EutM subunit. The scaffold may be formed by a method that generally includes incubating a plurality of EutM subunits under conditions allowing the EutM subunits to self-assemble into a protein scaffold, attaching a first enzyme of a multi-enzyme cascade to a first EutM subunit, and attaching a second enzyme of the multi-enzyme cascade to a second EutM subunit. The scaffold may be self-assembled in vivo or in vitro. Each enzyme may be, independently of any other enzyme, attached to its EutM subunit in vivo or in vitro. Each enzyme may be, independently of any other enzyme, attached to its EutM subunit before or after the scaffold is assembled.

The present invention provides a unit and a method useful for more precise phenylalanine measurement. More specifically, the present invention provides a modified phenylalanine dehydrogenase that includes a mutation of at least one amino acid residue so as to improve the characteristics (for example, substrate specificity, solubility, and phenylalanine dehydrogenase activity) of a phenylalanine dehydrogenase related to measurement of phenylalanine, a method for analyzing phenylalanine by measuring phenylalanine contained in a test sample using the modified phenylalanine dehydrogenase, and others.

Microorganisms and methods are provided for producing biomass that includes PHB and protein in weight ratios and polymer lengths that are beneficial in feed and nutritional supplement compositions. The compositions also may be used for improvement in feed compositions that improve survivability of livestock and aquaculture species.

A protein scaffold includes a plurality of EutM subunits and a multi-enzyme cascade. The multi-enzyme cascade includes a first enzyme attached to the first EutM subunit and a second enzyme attached to the second EutM subunit. The scaffold may be formed by a method that generally includes incubating a plurality of EutM subunits under conditions allowing the EutM subunits to self-assemble into a protein scaffold, attaching a first enzyme of a multi-enzyme cascade to a first EutM subunit, and attaching a second enzyme of the multi-enzyme cascade to a second EutM subunit. The scaffold may be self-assembled in vivo or in vitro. Each enzyme may be, independently of any other enzyme, attached to its EutM subunit in vivo or in vitro. Each enzyme may be, independently of any other enzyme, attached to its EutM subunit before or after the scaffold is assembled.

The present invention relates to a biosensor capable of measuring the total concentration of one or a plurality of amino acids with the use of a reagentless system comprising an electrode modified by hydrogel that comprises at least one enzyme that oxidizes at least one substrate that is at least one amino acid. In some embodiments, the biosensor comprises a hydrogel comprising alginate. In some embodiments, the biosensor comprises use of a thermophilic bacterial metabolic enzyme immobilized or attached to the hydrogel.

The application provides an enzyme immobilization carrier and a preparation method thereof, an immobilized enzyme and a preparation method thereof. The above enzyme immobilization carrier is obtained by an amino modification or a cyanuric chloride modification of super-crosslinked polyvinyl alcohol. The use of the enzyme immobilization carrier provided by the application may effectively improve the stability and reusability of the immobilized enzyme. Moreover, due to the use of the form of enzyme covalent linkage, compared with an embedding method, the preparation method is no need for chemical reagent immersion and the like, it is beneficial to maintain the own activity of the enzyme, and promote the immobilized enzyme to have the better activity while the stability and reusability are kept.

The present invention relates to a novel biocatalytic method for the production of primary and secondary amines, comprising coupled enzymatic oxidation and reduction processes simultaneously regenerating the required cofactor; making use of two enzymesi.e. an alcohol dehydrogenase and an amine dehydrogenaseoperating simultaneously in a one pot process (i.e. biocatalytic cascade). Furthermore, the overall process is redox neutral, since the hydride generated from the first oxidative step is internally recycled in the second reductive step. The invention also relates to recombinant expression systems and microorganisms procuring the required enzyme activities; and bioreactors for performing such methods.

An engineered microorganism, which comprises one or more of a gene encoding an aromatic amino acid transaminase, a gene encoding phenylalanine dehydrogenase, a gene encoding phenylpyruvate decarboxylase, a gene encoding an aldehyde reductase, a gene encoding glutamate dehydrogenase, and a gene encoding a phenylalanine transport protein, or a functional equivalent thereof. The present invention also relates to a composition comprising the engineered microorganism; a method for using the engineered microorganism or the composition to alleviate and/or treat diseases and/or conditions associated with hyperphenylalaninemia; and use of the engineered microorganism or the composition in the preparation of medicaments or health products for treating diseases and/or conditions associated with hyperphenylalaninemia.

Microorganisms and methods are provided for producing biomass that includes PHB and protein in weight ratios and polymer lengths that are beneficial in feed and nutritional supplement compositions. The compositions also may be used for improvement in feed compositions that improve survivability of livestock and aquaculture species.

The present invention provides a method for efficiently producing L-homophenylalanine and a strain producing L-homophenylalanine. In the present invention, a new route for the synthesis of L-homophenylalanine by a cascade enzymatic method using cheap benzaldehyde and pyruvic acid as raw materials is designed. By constructing the pathway-related enzymes into the same E. coli strain, a recombinant E. coli is obtained, with which L-homophenylalanine is catalytically produced through reaction in a 5 L reactor, with a yield of 100.9 g/L, a conversion rate of 94%, and ee>99%. Compared with the existing main methods for producing L-HPA, the production cost of L-homophenylalanine is greatly reduced. Thus, the present invention has good application prospects.