Abstract: Provided are a fructose-4-epimerase variant having tagatose conversion activity, and a method of preparing tagatose using the same.

Abstract: Provided are a tagatose-bisphosphate aldolase variant having tagatose conversion activity, and a method of preparing tagatose using the same.

Abstract: The present application relates to a fructose-4-epimerase variant exhibiting tagatose conversion activity and a method for preparing tagatose using the same.

Abstract: Provided are a fructose-4-epimerase variant having tagatose conversion activity, and a method of producing tagatose using the same.

Abstract: The present disclosure relates to a mixed sugar composition containing tagatose and sorbose.

Abstract: Provided are a fructose-4-epimerase variant having tagatose conversion activity, and a method of producing tagatose using the same.

Abstract: Provided are a tagatose-bisphosphate aldolase variant having tagatose conversion activity, and a method of preparing tagatose using the same.

Abstract: Provided are a fructose-4-epimerase variant having tagatose conversion activity, and a method of preparing tagatose using the same.

Abstract: Provided is an omega-transaminase mutant with improved activity using a point mutation in an active site of an omega-transaminase. Specifically, provided is a method for improving activity and extending a substrate spectrum of omega-transaminase by introducing a point mutation into a wild-type omega-transaminase rendered by replacing tryptophan at position 58 with the other amino acid.

Abstract: Disclosed are methods for producing optically active amino acids and amines. According to the methods, ?-keto acids are generated as reaction intermediates, and as a result, ?-transaminase-catalyzed kinetic resolution of racemic amino acids or amines as racemic amine compounds enables the production of optically active amine compounds without the need to use expensive ?-keto acids as starting materials. Therefore, the optically active amine compounds are produced at greatly reduced costs. In addition, the optically active amine compounds have high enantiomeric excess.

Abstract: Provided is an omega-transaminase mutant with improved activity using a point mutation in an active site of an omega-transaminase. Specifically, provided is a method for improving activity and extending a substrate spectrum of omega-transaminase by introducing a point mutation into a wild-type omega-transaminase rendered by replacing tryptophan at position 58 with the other amino acid.

Abstract: Disclosed are methods for producing optically active amino acids and amines. According to the methods, ?-keto acids are generated as reaction intermediates, and as a result, ?-transaminase-catalyzed kinetic resolution of racemic amino acids or amines as racemic amine compounds enables the production of optically active amine compounds without the need to use expensive ?-keto acids as starting materials. Therefore, the optically active amine compounds are produced at greatly reduced costs. In addition, the optically active amine compounds have high enantiomeric excess.

Abstract: The present disclosure relates to a method for preparing an optically active amino acid using cosubstrate shuttling of transaminase. The method includes coupling a reaction of converting a keto acid to an amino acid by ?-transaminase and a reaction of transferring an amino group of an amine substrate by ?-transaminase (TA) using an amino acid cosubstrate. The present disclosure allows production of various optically active amino acids with high purity and high efficiency by solving the low equilibrium constant problem of transaminase and is applicable to production of various optically active amino acids in industrial scale. Since the present disclosure allows easy production of various unnatural amino acids having high reactivity and stability, which are used as pharmaceutical precursors, it can be usefully employed in preparation of pharmaceuticals, food additives and various animal feeds.

Abstract: The present disclosure relates to a method for preparing an optically active amino acid using cosubstrate shuttling of transaminase. The method includes coupling a reaction of converting a keto acid to an amino acid by ?-transaminase and a reaction of transferring an amino group of an amine substrate by ?-transaminase (TA) using an amino acid cosubstrate. The present disclosure allows production of various optically active amino acids with high purity and high efficiency by solving the low equilibrium constant problem of transaminase and is applicable to production of various optically active amino acids in industrial scale. Since the present disclosure allows easy production of various unnatural amino acids having high reactivity and stability, which are used as pharmaceutical precursors, it can be usefully employed in preparation of pharmaceuticals, food additives and various animal feeds.