Patent US4861718A successfully refreshed from Google Patents.
US4861718A
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Gene coding for thermostable beta-galactosidase, bacillus subtilis having the gene, enzyme coded by the gene and a process for the production thereof
Assignee: Wakamoto Pharmaceutical Co Ltd
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Filing: 1985-09-27
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Granted: 1989-08-29
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Expires: 2005-09-27
Abstract
Abstract A novel gene coding for thermostable beta -galactosidase, novel recombinant DNA in which a DNA fragment containing the above gene is inserted, novel Bacillus subtilis in which the above recombinant DNA is introduced, and novel thermostable beta -galactosidase obtained by cultivating the above Bacillus subtilis.
Inventors
- 👤 Haruhisa Hirata
- 👤 Hirosuke Okada
- 👤 Seiji Negoro
Bibliographic Details
Application Number
—
Jurisdiction
US
Data Source
google_patents
Last Synchronized
2026-11-09 03:51
CPC Classifications
C; C12; C12Y; C12Y302/00; C12Y302/01; C12Y302/01023; C12N; C12N15/00; C12N15/09; C12N15/63; C12N15/74; C12N15/75; C12N9/00; C12N9/14; C12N9/24; C12N9/2402; C12N9/2468; C12N9/2471; Y; Y10; Y10S; Y10S435/00; Y10S435/8215; Y10S435/822; Y10S435/832; Y10S435/839
Claims Analysis
Total Claims: 3
Claim 1
Independent Claim
158 words
Thermostable β-galactosidase having the following physicochemical properties: a. action and substrate specificity: to hydrolyse substrates having a β-D-galactosidic linkage to release D-galactose, b. optimal pH and pH range for stability: optimal pH 5.5 pH range for stability 5.5 to 9.0 c. temperature range appropriate for activity: optimal temperature for activity about 70° C. d. temperature range for stability: half periods of the β-galactosidase activity at 55° C., 60° C. and 65° C. are about 620, 150 and 55 hours, respectively, e. influences of metal ions: Mg ++ , Ca ++ , Cu ++ , Fe ++ , Co ++ and Li + at a level of 1 mM do not inhibit the enzyme activity but Ag + inhibits the activity by about 80% or more, and Hg ++ by about 90% or more, f. molecular weight: (a) about 67,000 (measured by SDS-polyacrylamide electrophoresis) (b) 78,051 (calculated from amino acid sequence) g. Michaelis constant to lactose (Km): 2.4 mM.
Claim 2
Dependent Claim
158 words
Thermostable β-galactosidase having the following physicochemical properties: a. action and substrate specificity: to hydrolyse substrates having a β-D-galactosidic linkage to release D-galactose, b. optimal pH and pH range for stability: optimal pH 5.5 pH range for stability 5.5 to 9.0 c. temperature range appropriate for activity: optimal temperature for activity about 70° C. d. temperature range for stability: half periods of the β-galactosidase activity at 55° C., 60° C. and 65° C. are about 620, 150 and 55 hours, respectively, e. influences of metal ions: Mg ++ , Ca ++ , Cu ++ , Fe ++ , Co ++ and Li + at a level of 1 mM do not inhibit the enzyme activity but Ag + inhibits the activity by about 80% or more, and Hg ++ by about 90% or more, f. molecular weight: (a) about 67,000 (measured by SDS-polyacrylamide electrophoresis) (b) 78,051 (calculated from amino acid sequence) g. Michaelis constant to lactose (Km): 2.4 mM.
Claim 3
Dependent Claim
15 words
Thermostable β-galactosidase according to claim 1, characterized by having amino acid sequence of FIG. 4.
References Cited (Backward Citations)
No citation records indexed.
USPTO Annuity & Maintenance Windows
| Annuity Stage | Window Opens | Payment Deadline | Surcharge Period Until | Estimated Fee | Status |
|---|---|---|---|---|---|
| 3.5 Years (Year 4) | 1992-08-28 | 1993-02-27 | 1993-08-29 | $2000.00 | Window Closed / Lapsed |
| 7.5 Years (Year 8) | 1996-08-28 | 1997-02-27 | 1997-08-29 | $3760.00 | Window Closed / Lapsed |
| 11.5 Years (Year 12) | 2000-08-28 | 2001-02-27 | 2001-08-29 | $7700.00 | Window Closed / Lapsed |