An isolated and/or purified α-glucanotransferase from Exiguobacterium acetylicum, recombinantly engineered variants thereof, active fragments thereof, synthetic nucleic acids encoding the α-glucanotransferase and variants thereof, host cells comprising the synthetic nucleic acids, and compositions comprising the α-glucanotransferase are provided. Methods of using the compositions include the manufacture of oligosaccharides.

Adding (A) an amylomaltase derived from a bacterium of the genus Thermus to a starch-containing material, and further adding (B) a protein or lipid modification enzyme, or (C) a starch degradation product or (D) a starch degradation enzyme is useful for modifying a starch-containing food.

The present disclosure relates to a composition for producing tagatose, comprising fructose-6-phosphate-4-epimerase, and a method of producing tagatose using the same.

The present invention relates to a mini-GDE for the treatment of glycogen storage disease III.

An isolated and/or purified α-glucanotransferase from Exiguobacterium Acetylicum, recombinantly engineered variants thereof, active fragments thereof, synthetic nucleic acids encoding the α-glucanotransferase and variants thereof, host cells comprising the synthetic nucleic acids, and compositions comprising the α-glucanotransferase are provided. Methods of using the compositions include the manufacture of oligosaccharides.

The present invention relates to high intensity sweetener glycosides which have been modified using a glycosyltransferase so as to reduce off-flavours. The invention also relates to uses of the modified high intensity sweetener glycosides and methods of production thereof.

A starch-containing food with improved properties may be obtained by reacting an actinomycete-derived amylomaltase with starch in the raw material.

The present disclosure discloses a maltooligosyl trehalose synthase mutant with improved thermal stability, and belongs to the technical fields of enzyme engineering and protein engineering. The residual enzyme activities of the MTSase mutants S361R, S444E, S361R/S444E, S361K/S444E, G415P/S361R/S444E and G415P consistent with the present disclosure after treatment at 60 C. for 10 min are respectively 70.3%, 50.1%, 83.5%, 65.9%, 100% and 80.7%, which are respectively 1.6, 1.1, 1.9, 1.5, 2.3 and 1.9 times of that of the wild type. The half-lives of the S361R/S444E and G415P/S361R/S444E at 60 C. are respectively 14.9 min and 90.8 min which are respectively 3.2 and 19.7 times of that of the wild type, indicating that the thermal stability of the MTSase mutant consistent with the present disclosure is significantly improved than that of the wild type.

This invention provides a range of translatable messenger UNA (mUNA) molecules. The mUNA molecules can be translated in vitro and in vivo to provide an active polypeptide or protein, or to provide an immunization agent or vaccine component. The mUNA molecules can be used as an active agent to express an active polypeptide or protein in cells or subjects. Among other things, the mUNA molecules are useful in methods for treating rare diseases.

This invention provides a range of translatable polynucleotide and oligomer molecules for expressing a human amylo-alpha-1, 6-glucosidase, 4-alpha-glucanotransferase (AGL), or a fragment thereof having AGL activity. The polynucleotide and oligomer molecules are expressible to provide the human AGL or a fragment thereof having AGL activity. The molecules can be used as active agents to express an active polypeptide or protein in cells or subjects. The agents can be used in methods for ameliorating, preventing, delaying onset, or treating a disease or condition associated with reduced activity of amylo-alpha-1, 6-glucosidase, 4-alpha-glucanotransferase (AGL) in a subject.