GB911103A - Acid-stable proteolytic and amylolytic enzyme - Google Patents
Acid-stable proteolytic and amylolytic enzymeInfo
- Publication number
- GB911103A GB911103A GB38299/59A GB3829959A GB911103A GB 911103 A GB911103 A GB 911103A GB 38299/59 A GB38299/59 A GB 38299/59A GB 3829959 A GB3829959 A GB 3829959A GB 911103 A GB911103 A GB 911103A
- Authority
- GB
- United Kingdom
- Prior art keywords
- enzyme
- acid
- amylolytic enzyme
- stable proteolytic
- wheat bran
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired
Links
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
- C12N9/2411—Amylases
- C12N9/2414—Alpha-amylase (3.2.1.1.)
- C12N9/2417—Alpha-amylase (3.2.1.1.) from microbiological source
- C12N9/242—Fungal source
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/58—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from fungi
- C12N9/62—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from fungi from Aspergillus
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/96—Stabilising an enzyme by forming an adduct or a composition; Forming enzyme conjugates
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Genetics & Genomics (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Biotechnology (AREA)
- Medicinal Chemistry (AREA)
- Microbiology (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Mycology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Abstract
An acid stable proteolytic and amylolytic enzyme is obtained by cultivating Aspergillus oryzal var. microsporus TPR-18 on sterilised acidic wheat bran, extracting with water, adding zinc or cobalt chloride to stabilize the enzyme, concentrating the extract and then precipitating the enzyme by the addition of isopropanol. The wheat bran is treated with 20 to 50% by weight of 0.2 HCl and the cultivation is at 30 DEG C. for 40 to 50 hours. The zinc or cobalt chloride is used in quantities of 10-3 mol per litre of aqueous extract and then the pH is adjusted to 5 to 6 prior to concentration and precipitation.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB38299/59A GB911103A (en) | 1959-11-11 | 1959-11-11 | Acid-stable proteolytic and amylolytic enzyme |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB38299/59A GB911103A (en) | 1959-11-11 | 1959-11-11 | Acid-stable proteolytic and amylolytic enzyme |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| GB911103A true GB911103A (en) | 1962-11-21 |
Family
ID=10402544
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| GB38299/59A Expired GB911103A (en) | 1959-11-11 | 1959-11-11 | Acid-stable proteolytic and amylolytic enzyme |
Country Status (1)
| Country | Link |
|---|---|
| GB (1) | GB911103A (en) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE1271660B (en) * | 1964-05-26 | 1968-07-04 | Glaxo Lab Ltd | Process for the preparation of an enzyme complex |
-
1959
- 1959-11-11 GB GB38299/59A patent/GB911103A/en not_active Expired
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE1271660B (en) * | 1964-05-26 | 1968-07-04 | Glaxo Lab Ltd | Process for the preparation of an enzyme complex |
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