US4237221A
Expired / Lapsed
US
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Process for obtaining maltose phosphorylase and β-phosphoglucomutase and method of determining α-amylase using same
Assignee: Roche Diagnostics GmbH
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Filing: 1978-10-20
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Granted: 1980-12-02
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Expires: 1998-10-20
Abstract
Abstract The present invention provides a process for obtaining maltose phosphorylase and/or β-phosphoglucomutase from micro-organisms, wherein the starting material used is selected from Lactobacillus brevis DSM 20054, NCIB 8836, 8561 and 8562, Lactobacillus plantarum DSM 20174 and 43, Lactobacillus reuteri DSM 20016, Lactobacillus fermentum DSM 20052, Streptococcus spec. DSM 1118, DSM 119, DSM 1120 and DSM 1121. The present invention also provides a composition and process for determining α-amylase, wherein maltose phosphorylase and β-phosphoglucomutase obtained by such a process is used, as a crude extract or in an enriched form, optionally with the addition of α-glucose-1,6-diphosphate and of divalent manganese ions.
Inventors
- 👤 Helmgard Gauhl
- 👤 Hans Seidel
Bibliographic Details
Application Number
—
Jurisdiction
US
Data Source
google_patents
Last Synchronized
2026-10-28 10:44
CPC Classifications
C; C12; C12N; C12N9/00; C12N9/10; C12N9/1048; C12N9/1051; C12N9/12; C12Q; C12Q1/00; C12Q1/34; C12Q1/40
Claims Analysis
Total Claims: 13
Claim 1
Independent Claim
73 words
Process for obtaining an enzyme preparation comprising at least one member selected from the group consisting of maltose phosphorylase and β-phosphoglucomutase from micro-organisms, which process comprises extracting said enzyme preparation from a micro-organism selected from the group consisting of Lactobacillus brevis DSM 20054, NCIB 8836, 8561 and 8562, Lactobacillus plantarum DSM 20174 and 43, Lactobacillus reuteri DSM 20016, Lactobacillus fermentum DSM 20052, Streptococcus spec. DSM 1118, DSM 1119, DSM 1120 and DSM 1121.
Claim 2
Dependent Claim
73 words
Process for obtaining an enzyme preparation comprising at least one member selected from the group consisting of maltose phosphorylase and β-phosphoglucomutase from micro-organisms, which process comprises extracting said enzyme preparation from a micro-organism selected from the group consisting of Lactobacillus brevis DSM 20054, NCIB 8836, 8561 and 8562, Lactobacillus plantarum DSM 20174 and 43, Lactobacillus reuteri DSM 20016, Lactobacillus fermentum DSM 20052, Streptococcus spec. DSM 1118, DSM 1119, DSM 1120 and DSM 1121.
Claim 3
Dependent Claim
12 words
Process as claimed in claim 1, wherein said enzyme is maltose phosphorylase.
Claim 4
Dependent Claim
11 words
Process as claimed in claim 1, wherein said enzyme is β-phosphoglucomutase.
Claim 5
Dependent Claim
121 words
Process for determining α-amylase which comprises contacting a sample suspected of containing α-amylase with starch and an enzyme preparation comprising maltose phosphorylase and β-phosphoglucomutase from a micro-organism selected from the group consisting of Lactobacillus brevis DSM 20054, NCIB 8836, 8561 and 8562, Lactobacillus plantarum DSM 20174 and 43, Lactobacillus reuteri DSM 20016, Lactobacillus fermentum DSM 20052, Streptococcus spec. DSM 1117, DSM 1119, DSM 1120 or DSM 1121, splitting the maltose formed by means of said maltose phosphorylase, in the presence of phosphate, into glucose and β-glucose-1-phosphate, converting the latter into α-glucose-6-phosphate by means of said β-phosphoglucomutase, using said α-glucose-6-phosphate, in the presence of glucose-6-phosphodehydrogenase, to reduce nicotinamideadenine dinucleotide and determining the NADH formed as a measure of the initial α-amylase activity.
Claim 6
Dependent Claim
121 words
Process for determining α-amylase which comprises contacting a sample suspected of containing α-amylase with starch and an enzyme preparation comprising maltose phosphorylase and β-phosphoglucomutase from a micro-organism selected from the group consisting of Lactobacillus brevis DSM 20054, NCIB 8836, 8561 and 8562, Lactobacillus plantarum DSM 20174 and 43, Lactobacillus reuteri DSM 20016, Lactobacillus fermentum DSM 20052, Streptococcus spec. DSM 1117, DSM 1119, DSM 1120 or DSM 1121, splitting the maltose formed by means of said maltose phosphorylase, in the presence of phosphate, into glucose and β-glucose-1-phosphate, converting the latter into α-glucose-6-phosphate by means of said β-phosphoglucomutase, using said α-glucose-6-phosphate, in the presence of glucose-6-phosphodehydrogenase, to reduce nicotinamideadenine dinucleotide and determining the NADH formed as a measure of the initial α-amylase activity.
Claim 7
Dependent Claim
15 words
Process as claimed in claim 4, wherein the said enzyme is activated by adding α-glucose-1,6-diphosphate.
Claim 8
Dependent Claim
17 words
Process as claimed in claim 4, wherein the said enzyme is activated by adding divalent manganese ions.
Claim 9
Dependent Claim
16 words
Process as claimed in claim 4, wherein said enzyme comprises a crude extract from said micro-organisms.
Claim 10
Dependent Claim
68 words
Reagent composition for determining α-amylase which reagent composition comprises an enzyme preparation comprising maltose phosphorylase and β-phosphoglucomutase from a micro-organism selected from the group consisting of Lactobacillus brevis DSM 20054, NCIB 8836, 8561 and 8562, Lactobacillus plantarum DSM 20174 and 43, Lactobacillus reuteri DSM 20016, Lactobacillus fermentum DSM 20052, Streptococcus spec. DSM 1118, DSM 1119, DSM 1120 and DSM 1121; soluble starch; phosphate buffer; glucose-6-phosphatedehydrogenase; and nicotinamide-adenine dinucleotide.
Claim 11
Dependent Claim
68 words
Reagent composition for determining α-amylase which reagent composition comprises an enzyme preparation comprising maltose phosphorylase and β-phosphoglucomutase from a micro-organism selected from the group consisting of Lactobacillus brevis DSM 20054, NCIB 8836, 8561 and 8562, Lactobacillus plantarum DSM 20174 and 43, Lactobacillus reuteri DSM 20016, Lactobacillus fermentum DSM 20052, Streptococcus spec. DSM 1118, DSM 1119, DSM 1120 and DSM 1121; soluble starch; phosphate buffer; glucose-6-phosphatedehydrogenase; and nicotinamide-adenine dinucleotide.
Claim 12
Dependent Claim
22 words
Reagent composition as claimed in claim 8, also comprising at least one of α-glucose-1,6-diphosphate and divalent manganese ions to activate said enzyme.
Claim 13
Dependent Claim
17 words
Reagent composition as claimed in claim 8, wherein said enzyme comprises a crude extract from said micro-organisms.
References Cited (Backward Citations)
US4036697A
Cited
US4162194A
Cited
USPTO Annuity & Maintenance Windows
| Annuity Stage | Window Opens | Payment Deadline | Surcharge Period Until | Estimated Fee | Status |
|---|---|---|---|---|---|
| 3.5 Years (Year 4) | 1983-12-02 | 1984-06-02 | 1984-12-02 | $2000.00 | Window Closed / Lapsed |
| 7.5 Years (Year 8) | 1987-12-02 | 1988-06-02 | 1988-12-02 | $3760.00 | Window Closed / Lapsed |
| 11.5 Years (Year 12) | 1991-12-02 | 1992-06-02 | 1992-12-02 | $7700.00 | Window Closed / Lapsed |