CA2124758A1 - Trehalose-releasing enzyme, and its preparation and uses - Google Patents

Trehalose-releasing enzyme, and its preparation and uses

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Publication number
CA2124758A1
CA2124758A1 CA002124758A CA2124758A CA2124758A1 CA 2124758 A1 CA2124758 A1 CA 2124758A1 CA 002124758 A CA002124758 A CA 002124758A CA 2124758 A CA2124758 A CA 2124758A CA 2124758 A1 CA2124758 A1 CA 2124758A1
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CA
Canada
Prior art keywords
accordance
trehalose
enzyme
microorganism
alanine
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Granted
Application number
CA002124758A
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French (fr)
Other versions
CA2124758C (en
Inventor
Kazuhiko Maruta
Michio Kubota
Toshiyuki Sugimoto
Toshio Miyake
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Hayashibara Seibutsu Kagaku Kenkyujo KK
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Hayashibara Seibutsu Kagaku Kenkyujo KK
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Publication of CA2124758A1 publication Critical patent/CA2124758A1/en
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Publication of CA2124758C publication Critical patent/CA2124758C/en
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    • C13KSACCHARIDES OBTAINED FROM NATURAL SOURCES OR BY HYDROLYSIS OF NATURALLY OCCURRING DISACCHARIDES, OLIGOSACCHARIDES OR POLYSACCHARIDES
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    • C12N9/14Hydrolases (3)
    • C12N9/24Hydrolases (3) acting on glycosyl compounds (3.2)
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    • C12N9/2405Glucanases
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Abstract

Abstract of the Disclosure Disclosed is a trehalose-releasing enzyme which specifically hydrolyzes the linkage between a trehalose moiety and the remaining glycosyl moiety in a non-reducing saccharide having a trehalose structure as an end unit and having a degree of glucose polymerization of 3 or higher. The molecular weight of the enzyme is about 57,000 to 68,000 daltons on SDS-PAGE, and the isoelectric point is about 3.3 to 4.6 on isoelectrophoresis. The enzyme is useful in an industrial-scale preparation of trehalose, and the trehalose prepared therewith can be readily incorporated into food products, as well as cosmetic- and pharmaceutical-compositions.

Claims (58)

1. A trehalose-releasing enzyme which specifically hydrolyzes the linkage between a trehalose moiety and the remaining glycosyl moiety in a non-reducing saccharide having a trehalose structure as an end unit and having a degree of glucose polymerization of 3 or higher.
2. The enzyme in accordance with claim 1, wherein said glycosyl moiety consists of one or more glucose residues.
3. The enzyme in accordance with claim 1, which has the following physicochemical properties:
(1) Action Specifically hydrolyzing the linkage between a trehalose moiety and the remaining glycosyl moiety in a non-reducing saccharide having a trehalose structure as an end unit and having a degree of glucose polymerization of 3 or higher;
(2) Molecular weight About 57,000 to 68,000 daltons on sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE);
(3) Isoelectric point (pI) About 3.3 to 4.6 on isoelectrophoresis using ampholyte;
(4) Optimum temperature About 35-45°C when incubated at pH 7.0 for 30 min;
(5) Optimum pH
About 6.0-7.5 when incubated at 40°C for 30 min;
(6) Thermal stability Stable up to a temperature of about 30-45°C when incubated at pH 7.0 for 60 min;
and (7) pH Stability Stable at a pH of about 5.0-10.0 when incubated at 25°C for 16 hours.
4. The enzyme in accordance with claim 1, which has one or more partial amino acid sequences selected from the group consisting of:
(1) leucine-aspartic acid-tryptophan-alanine-glutamic acid-alanine-X1-X2-glycine-aspartic acid (where X1 means serine or alanine, and X2 means alanine or glutamic acid);
(2) aspartic acid-glutamic acid-arginine-alanine-valine-histidine-isoleucine-leucine-glutamic acid-X3 (where X3 means glutamic acid or aspartic acid); and (3) X4-glycine-glutamic acid-glycine-asparagine-threonine-tryptophan-glycine-aspartic acid-serine (where X4 means histidine or glutamine).
5. The enzyme in accordance with claim 1, which is an enzyme derived from a microorganism.
6. The enzyme in accordance with claim 5, wherein said microorganism is a microorganism selected from the group consisting of those of the genera Rhizobium, Arthrobacter, Brevibacterium and Micrococcus.
7. The enzyme in accordance with claim 6, wherein said microorganism of the genus Rhizobium is Rhizobium sp. M-11 (FERM BP-4130).
8. The enzyme in accordance with claim 6, wherein said microorganism of the genus Arthrobacter is Arthrobacter sp. Q36 (FERM BP-4316).
9. A process for preparing a trehalose-releasing enzyme which specifically hydrolyzes the linkage between a trehalose moiety and the remaining glycosyl moiety in a non-reducing saccharide having a trehalose structure as an end unit and having a degree of glucose polymerization of 3 or higher, said process comprising culturing a microorganism capable of producing said enzyme in a nutrient culture medium to form said enzyme, and recovering the resultant enzyme.
10. The enzyme in accordance with claim 9, wherein said glycosyl moiety consists of one or more glucose residues.
11. The process in accordance with claim 9, which has the following physicochemical properties:
(1) Action Specifically hydrolyzing the linkage between a trehalose moiety and the remaining glycosyl moiety in a non-reducing saccharide having a trehalose structure as an end unit and having a degree of glucose polymerization of 3 or higher;
(2) Molecular weight About 57,000 to 68,000 daltons on sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE);
(3) Isoelectric point (pI) About 3.3 to 4.6 on isoelectrophoresis using ampholyte;
(4) Optimum temperature About 35-45°C when incubated at pH 7.0 for 30 min;
(5) Optimum pH
About 6.0-7.5 when incubated at 40°C for 30 min;
(6) Thermal stability Stable up to a temperature of about 30-45°C when incubated at pH 7.0 for 60 min;
and (7) pH Stability Stable at a pH of about 5.0-10.0 when incubated at 25°C for 16 hours.
12. The enzyme in accordance with claim 9, which has one or more partial amino acid sequences selected from the group consisting of:
(1) leucine-aspartic acid-tryptophan-alanine-glutamic acid-alanine-X1-X2-glycine-aspartic acid (where X1 means serine or alanine, and X2 means alanine or glutamic acid);
(2) aspartic acid-glutamic acid-arginine-alanine-valine-histidine-isoleucine-leucine-glutamic acid-X3 (where X3 means glutamic acid or aspartic acid); and (3) X4-glycine-glutamic acid-glycine-asparagine-threonine-tryptophan-glycine-aspartic acid-serine (where X4 means histidine or glutamine).
13. The process in accordance with claim 9, which is an enzyme derived from a microorganism.
14. The process in accordance with claim 13, wherein said microorganism is a microorganism selected from the group consisting of those of the genera Rhizobium, Arthrobacter, Brevibacterium and Micrococcus.
15. The process in accordance with claim 14, wherein said microorganism of the genus Rhizobium is Rhizobium sp. M-11 (FERM BP-4130).
16. The process in accordance with claim 14, wherein said microorganism of the genus Arthrobacter is Arthrobacter sp. Q36 (FERM BP-4316).
17. A process for preparing trehalose, comprising:
(a) allowing an enzyme to act on a solution containing a non-reducing saccharide having a trehalose structure as an end unit and having a degree of glucose polymerization of 3 or higher to form trehalose, said enzyme being capable of specifically hydrolyzing the linkage between a trehalose moiety and the remaining glycosyl moiety in said non-reducing saccharide;
(b) purifying the resultant trehalose; and (c) recovering the purified trehalose.
18. The process in accordance with claim 17, wherein said enzyme in the step (a) is used together with a non-reducing saccharide-forming enzyme capable of forming one or more non-reducing saccharides having a trehalose structure as an end unit and having a degree of glucose polymerization of 3 or higher.
19. The process in accordance with claim 17, wherein the step (a) further contains a step of allowing glucoamylase to act on the resultant solution in the step (a).
20. The process in accordance with claim 17, wherein the step (b) contains a step of subjecting the resultant solution containing trehalose in the step (a) to column chromatography using a column packed with a strong-acid cation-exchange resin to purify the trehalose.
21. The process in accordance with claim 17, wherein the step (b) further contains a step of crystallizing trehalose in the resultant solution in the step (b) into hydrous- or anhydrous-crystalline trehalose.
22. The process in accordance with claim 17, wherein said glycosyl moiety consists of one or more glucose residues.
23. The process in accordance with claim 17, wherein said enzyme has the following physicochemical properties:
(1) Action Specifically hydrolyzing the linkage between a trehalose moiety and the remaining glycosyl moiety in a non-reducing saccharide having a trehalose structure as an end unit and having a degree of glucose polymerization of 3 or higher;
(2) Molecular weight About 57,000 to 68,000 daltons on sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE);
(3) Isoelectric point (pI) About 3.3 to 4.6 on isoelectrophoresis using ampholyte;
(4) Optimum temperature About 35-45°C when incubated at pH 7.0 for 30 min;
(5) Optimum pH
About 6.0-7.5 when incubated at 40°C for 30 min;
(6) Thermal stability Stable up to a temperature of about 30-45°C when incubated at pH 7.0 for 60 min;

and (7) pH Stability Stable at a pH of about 5.0-10.0 when incubated at 25°C for 16 hours.
24. The process in accordance with claim 17, wherein said enzyme has one or more partial amino acid sequences selected from the group consisting of:
(1) leucine-aspartic acid-tryptophan-alanine-glutamic acid-alanine-X1-X2-glycine-aspartic acid (where X1 means serine or alanine, and X2 Means alanine or glutamic acid);
(2) aspartic acid-glutamic acid-arginine-alanine-valine-histidine-isoleucine-leucine-glutamic acid-X3 (where X3 means glutamic acid or aspartic acid); and (3) X4-glycine-glutamic acid-glycine-asparagine-threonine-tryptophan-glycine-aspartic acid-serine (where X4 means histidine or glutamine).
25. The process in accordance with claim 17, wherein said enzyme is derived from a microorganism.
26. The process in accordance with claim 25, wherein said microorganism is a microorganism selected from the group consisting of those of the genera Rhizobium, Arthrobacter, Brevibacterium and Micrococcus.
27. The process in accordance with claim 26, wherein said microorganism of the genus Rhizobium is Rhizobium sp. M-11 (FERM BP-4130).
28. The process in accordance with claim 26, wherein said microorganism of the genus Arthrobacter is Arthrobacter sp. Q36 (FERM BP-4316).
29. A process for preparing saccharide composition containing trehalose, comprising:
(a) allowing an enzyme to act on a solution containing a non-reducing saccharide having a trehalose structure as an end unit and having a degree of glucose polymerization of 3 or higher to form trehalose, said enzyme being capable of specifically hydrolyzing the linkage between a trehalose moiety and the remaining glycosyl moiety in said non-reducing saccharide; and (b) recovering the resultant saccharide composition containing trehalose and other saccharide(s).
30. The process in accordance with claim 29, wherein said enzyme in the step (a) is used together with a non-reducing saccharide-forming enzyme capable of forming one or more non-reducing saccharides having a trehalose structure as an end unit and having a degree of glucose polymerization of 3 or higher.
31. The process in accordance with claim 29, wherein the step (a) further contains a step of allowing glucoamylase to act on the resultant solution in the step (a).
32. The process in accordance with claim 29, wherein the step (a) further contains a step of crystallizing trehalose in the resultant solution in the step (a) into hydrous- or anhydrous-crystalline trehalose.
33. The process in accordance with claim 29, wherein said glycosyl moiety consists of one or more glucose residues.
34. The process in accordance with claim 29, wherein said enzyme has the following physicochemical properties:
(1) Action Specifically hydrolyzing the linkage between a trehalose moiety and the remaining glycosyl moiety in a non-reducing saccharide having a trehalose structure as an end unit and having a degree of glucose polymerization of 3 or higher;
(2) Molecular weight About 57,000 to 68,000 daltons on sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE);
(3) Isoelectric point (pI) About 3.3 to 4.6 on isoelectrophoresis using ampholyte;
(4) Optimum temperature About 35-45°C when incubated at pH 7.0 for 30 min;
(5) Optimum pH
About 6.0-7.5 when incubated at 40°C for 30 min;
(6) Thermal stability Stable up to a temperature of about 30-45°C when incubated at pH 7.0 for 60 min;
and (7) pH Stability Stable at a pH of about 5.0-10.0 when incubated at 25°C for 16 hours.
35. The process in accordance with claim 29, wherein said enzyme has one or more partial amino acid sequences selected from the group consisting of:
(1) leucine-aspartic acid-tryptophan-alanine-glutamic acid-alanine-X1-X2-glycine-aspartic acid (where X1 means serine or alanine, and X2 means alanine or glutamic acid);
(2) aspartic acid-glutamic acid-arginine-alanine-valine-histidine-isoleucine-leucine-glutamic acid-X3 (where X3 means glutamic acid or aspartic acid); and (3) X4-glycine-glutamic acid-glycine-asparagine-threonine-tryptophan-glycine-aspartic acid-serine (where X4 means histidine or glutamine).
36. The process in accordance with claim 29, wherein said enzyme is derived from a microorganism.
37. The process in accordance with claim 36, wherein said microorganism is a microorganism selected from the group consisting of those of the genera Rhizobium, Arthrobacter, Brevibacterium and Micrococcus.
38. The process in accordance with claim 37, wherein said microorganism of the genus Rhizobium is Rhizobium sp. M-11 (FERM BP-4130).
39. The process in accordance with claim 37, wherein said microorganism of the genus Arthrobacter is Arthrobacter sp. Q36 (FERM BP-4316).
40. A process for preparing composition containing trehalose, comprising:
(a) allowing a non-reducing saccharide-forming enzyme (I) together with a trehalose-releasing enzyme (II) to act on a solution containing one or more reducing partial starch hydrolysates having a degree of glucose polymerization of 3 or higher to form trehalose, said enzyme (I) being capable of forming a non-reducing saccharide having a trehalose structure as an end unit and having a degree of glucose polymerization of 3 or higher, and said enzyme (II) being capable of specifically hydrolyzing the linkage between a trehalose moiety and the remaining glycosyl moiety in said non-reducing saccharide;
(b) recovering the resultant trehalose together with or without other saccharide(s); and (c) incorporating the trehalose together with or without other saccharide(s) into a material for composition.
41. The process in accordance with claim 40, which is a food product.
42. The process in accordance with claim 40, which is a cosmetic composition.
43. The process in accordance with claim 40, which is a pharmaceutical composition.
44. The process in accordance with claim 40, wherein said glycosyl moiety consists of one or more glucose residues.
45. The process in accordance with claim 40, wherein said enzyme has the following physicochemical properties:
(1) Action Specifically hydrolyzing the linkage between a trehalose moiety and the remaining glycosyl moiety in a non-reducing saccharide having a trehalose structure as an end unit and having a degree of glucose polymerization of 3 or higher;
(2) Molecular weight About 57,000 to 68,000 daltons on sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE);
(3) Isoelectric point (pI) About 3.3 to 4.6 on isoelectrophoresis using ampholyte;
(4) Optimum temperature About 35-45°C when incubated at pH 7.0 for 30 min;
(5) Optimum pH
About 6.0-7.5 when incubated at 40°C for 30 min;
(6) Thermal stability Stable up to a temperature of about 30-45°C when incubated at pH 7.0 for 60 min;
and (7) pH Stability Stable at a pH of about 5.0-10.0 when incubated at 25°C for 16 hours.
46. The process in accordance with claim 40, wherein said enzyme has one or more partial amino acid sequences selected from the group consisting of:
(1) leucine-aspartic acid-tryptophan-alanine-glutamic acid-alanine-X1-X2-glycine-aspartic acid (where X1 means serine or alanine, and X2 means alanine or glutamic acid);
(2) aspartic acid-glutamic acid-arginine-alanine-valine-histidine-isoleucine-leucine-glutamic acid-X3 (where X3 means glutamic acid or aspartic acid); and (3) X4-glycine-glutamic acid-glycine-asparagine-threonine-tryptophan-glycine-aspartic acid-serine (where X4 means histidine or glutamine).
47. The process in accordance with claim 40, wherein said enzyme is derived from a microorganism.
48. The process in accordance with claim 47, wherein said microorganism is a microorganism selected from the group consisting of those of the genera Rhizobium, Arthrobacter, Brevibacterium and Micrococcus.
49. The process in accordance with claim 48, wherein said microorganism of the genus Rhizobium is Rhizobium sp. M-11 (FERM BP-4130).
50. The process in accordance with claim 48, wherein said microorganism of the genus Arthrobacter is Arthrobacter sp. Q36 (FERM BP-4316).
51. A method to lower the degree of glucose polymerization of a reducing partial starch hydrolysate without increasing its reducing power, which contains a step of allowing a non-reducing saccharide-forming enzyme (I) together with a trehalose-releasing enzyme (II) to act on a solution containing one or more reducing partial starch hydrolysates having a degree of glucose polymerization of 3 or higher, said enzyme (I) being capable of forming one or more non-reducing saccharides having a trehalose structure as an end unit and having a degree of glucose polymerization of 3 or higher, and said enzyme (II) being capable of specifically hydrolyzing the linkage between a trehalose moiety and the remaining glycosyl moiety in said non-reducing saccharide.
52. The method in accordance with claim 51, wherein said glycosyl moiety consists of one or more glucose residues.
53. The method in accordance with claim 51, wherein said enzyme has the following physicochemical properties:
(1) Action Specifically hydrolyzing the linkage between a trehalose moiety and the remaining glycosyl moiety in a non-reducing saccharide having a trehalose structure as an end unit and having a degree of glucose polymerization of 3 or higher;
(2) Molecular weight About 57,000 to 68,000 daltons on sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE);
(3) Isoelectric point (pI) About 3.3 to 4.6 on isoelectrophoresis using ampholyte;
(4) Optimum temperature About 35-45°C when incubated at pH 7.0 for 30 min;
(5) Optimum pH
About 6.0-7.5 when incubated at 40°C for 30 min;
(6) Thermal stability Stable up to a temperature of about 30-45°C when incubated at pH 7.0 for 60 min;
and (7) pH Stability Stable at a pH of about 5.0-10.0 when incubated at 25°C for 16 hours.
54. The method in accordance with claim 51, wherein said enzyme has one or more partial amino acid sequences selected from the group consisting of:
(1) leucine-aspartic acid-tryptophan-alanine-glutamic acid-alanine-X1-X2-glycine-aspartic acid (where X1 means serine or alanine, and X2 means alanine or glutamic acid);
(2) aspartic acid-glutamic acid-arginine-alanine-valine-histidine-isoleucine-leucine-glutamic acid-X3 (where X3 means glutamic acid or aspartic acid); and (3) X4-glycine-glutamic acid-glycine-asparagine-threonine-tryptophan-glycine-aspartic acid-serine (where X4 means histidine or glutamine).
55. The method in accordance with claim 51, wherein said enzyme is derived from a microorganism.
56. The method in accordance with claim 55, wherein said microorganism is a microorganism selected from the group consisting of those of the genera Rhizobium, Arthrobacter, Brevibacterium and Micrococcus.
57. The method in accordance with claim 56, wherein said microorganism of the genus Rhizobium is Rhizobium sp. M-11 (FERM BP-4130).
58. The method in accordance with claim 56, wherein said microorganism of the genus Arthrobacter is Arthrobacter sp. Q36 (FERM BP-4316).
CA2124758A 1993-06-03 1994-05-31 Trehalose-releasing enzyme, and its preparation and uses Expired - Lifetime CA2124758C (en)

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