Aldolase, aldolase mutant, and method and composition for producing tagatose by using same

Patent metadata

Field	Value
Publication number	US-2016186162-A1
Application number	US-201414908469-A
Country	US
Kind code	A1
Filing date	Jul 25, 2014
Priority date	Jul 29, 2013
Publication date	Jun 30, 2016
Grant date	—

Abstract

This disclosure relates to aldolase, an aldolase mutant, and a method and a composition for producing tagatose by using the same. The feature of the disclosure is environment-friendly due to the use of an enzyme acquired from microorganisms, requires only a simple process of enzyme immobilization, uses a low-cost substrate in a substrate compared with a conventional method for producing tagatose and has a remarkably high yield, thereby greatly reducing production costs and maximizing production effects.

First claim

1 .- 2 . (canceled)

3 . A method of producing tagatose from fructose, the method comprising:
reacting fructose 6-phosphate with fructose 1,6-diphosphate aldolase or a mutant of fructose 1,6-bisphosphate aldolase.

4 . The method of claim 3 , wherein the fructose 1,6-diphosphate aldolase is selected from the group consisting of SEQ ID NOS: 1 to 4.

5 .- 11 . (canceled)

12 . The method of claim 3 , wherein the mutant includes a substitution at one or more residues at positions of 332, 314, 227, and 62 of fructose aldolased enzyme of SEQ ID NO: 1, wherein the residue at position 332 is substituted from arginine to glutamine, the residue at position 314 is substituted from glutamine to alanine, the residue at position 227 is substituted from histidine to alanine, and the residue at position 62 is substituted from serine to alanine.

13 .- 14 . (canceled)

15 . A mutant enzyme of fructose 1,6-bisphosphate aldolase, which is an enzyme selected from the group consisting of SEQ ID NOS: 1 to 4.

16 . The mutant enzyme of claim 15 , wherein the mutant enzyme includes a substitution at one or more residues at positions of 332, 314, 227, and 62 of fructose aldolased enzyme of SEQ ID NO: 1, wherein the residue at position 332 is substituted from arginine to glutamine, the residue at position 314 is substituted from glutamine to alanine, the residue at position 227 is substituted from histidine to alanine, and the residue at position 62 is substituted from serine to alanine.

17 . The mutant enzyme of claim 15 , wherein the fructose 1,6-diphosphate aldolase is SEQ ID NO: 1.

18 . The mutant enzyme of claim 15 , wherein the fructose 1,6-diphosphate aldolase is SEQ ID NO: 2.

19 . The mutant enzyme of claim 15 , wherein the fructose 1,6-diphosphate aldolase is SEQ ID NO: 3.

20 . The mutant enzyme of claim 15 , wherein the fructose 1,6-diphosphate aldolase is SEQ ID NO: 4.

21 . The method according to claim 4 , wherein the fructose 1,6-diphosphate aldolase is SEQ ID NO: 1.

22 . The method according to claim 4 , wherein the fructose 1,6-diphosphate aldolase is SEQ ID NO: 2.

23 . The method according to claim 4 , wherein the fructose 1,6-diphosphate aldolase is SEQ ID NO: 3.

24 . The method according to claim 4 , wherein the fructose 1,6-diphosphate aldolase is SEQ ID NO: 4.

Assignees

• Univ Konkuk Ind Coop Corp

Inventors

• Oh Deok-Kun
• Hong Seung-Hye
• Lee Seon-Hwa

Classifications

• C12P19/02

  Monosaccharides (2-ketogulonic acid C12P7/60) · CPC title

• C12Y401/02013

  Fructose-bisphosphate aldolase (4.1.2.13) · CPC title

• C12N9/88 Primary

  Lyases (4.) · CPC title

• C12P7/26

  Ketones · CPC title