GB1293563A - Enzymes and methods for their preparation, isolation and purification - Google Patents
Enzymes and methods for their preparation, isolation and purificationInfo
- Publication number
- GB1293563A GB1293563A GB917970A GB917970A GB1293563A GB 1293563 A GB1293563 A GB 1293563A GB 917970 A GB917970 A GB 917970A GB 917970 A GB917970 A GB 917970A GB 1293563 A GB1293563 A GB 1293563A
- Authority
- GB
- United Kingdom
- Prior art keywords
- mixture
- enzyme
- proteolytic
- enzyme mixture
- proteins
- 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)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/52—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/43—Enzymes; Proenzymes; Derivatives thereof
- A61K38/46—Hydrolases (3)
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Animal Behavior & Ethology (AREA)
- Gastroenterology & Hepatology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Immunology (AREA)
- Microbiology (AREA)
- Epidemiology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- Pharmacology & Pharmacy (AREA)
- Detergent Compositions (AREA)
- Peptides Or Proteins (AREA)
Abstract
1293563 Hydrolytic enzyme mixture ASTRA LAKEMEDEL AB 6 April 1970 [10 April 1969 25 Feb 1970] 18582/69 and 9179/70 Heading C3H A stable hydrolytic enzyme mixture which is a mixture of proteins is characterized in that it (a) has a U.V. spectrum characteristic of proteins containing aromatic amino acids, (b) is proteolytically active against casein, haemoglobin and gelatine, with a proteolytic optimum at pH 9-10 with casein, (c) hydrolyses N-α- tosyl-L-arginine ethyl ester, (d) contains proteolytic activity inducable by heating, (e) also contains esterases, lipases and amylases, (f) precipitates a heat stable enzyme with organic solvents (e.g. acetone) or ammonium sulphate, and (g) has stability and activity independent of Ca<SP>++</SP> ion concentration in solution. The mixture may be formed by fermenting Streptomyces globisporus variant NRRL 3762 under submerged aerobic conditions in a nutrient medium at, e.g. 26-30‹ C. and an initial pH of 6À0-7À5. A proteolytic enzyme fraction may be obtained from the enzyme mixture by subjecting it to gel filtration using a modified dextran having a fractionation range for peptides and globular proteins of molecular weight 1500-30,000 and eluting the dextran with water, or by contacting a solution of the enzymes with diethylaminoethyl cellulose and eluting the cellulose with ammonium acetate at pH 7À4, or by subjecting the enzyme mixture to isoelectric separation and recovering the fraction eluted at pH 4-6.
Priority Applications (8)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
FI700770A FI47779C (en) | 1969-04-10 | 1970-03-19 | Method for preparing a hydrolytic enzyme mixture. |
FI00770/70A FI47779B (en) | 1969-04-10 | 1970-03-19 | |
SE04417/70A SE362252B (en) | 1969-04-10 | 1970-03-31 | |
BE748297D BE748297A (en) | 1969-04-10 | 1970-04-01 | ENZYMES AND METHOD FOR THE PREPARATION, ISOLATION AND PURIFICATION OF THESE ENZYMES |
US25454A US3684658A (en) | 1969-04-10 | 1970-04-03 | Enzymes and process for their preparation |
AU13462/70A AU1346270A (en) | 1969-04-10 | 1970-04-06 | Enzymes and methods for their preparation, isolation and purification |
DE19702016822 DE2016822A1 (en) | 1969-04-10 | 1970-04-09 | Enzyme mixture and process for its preparation |
NL7005169A NL7005169A (en) | 1969-04-10 | 1970-04-10 |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
GB1858269 | 1969-04-10 |
Publications (1)
Publication Number | Publication Date |
---|---|
GB1293563A true GB1293563A (en) | 1972-10-18 |
Family
ID=10114925
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
GB917970A Expired GB1293563A (en) | 1969-04-10 | 1970-02-25 | Enzymes and methods for their preparation, isolation and purification |
Country Status (2)
Country | Link |
---|---|
FR (1) | FR2054547A1 (en) |
GB (1) | GB1293563A (en) |
Families Citing this family (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS56106593A (en) * | 1980-01-24 | 1981-08-24 | Dainippon Pharmaceut Co Ltd | Alkali protease m3 |
-
1970
- 1970-02-25 GB GB917970A patent/GB1293563A/en not_active Expired
- 1970-04-09 FR FR7012868A patent/FR2054547A1/en active Granted
Also Published As
Publication number | Publication date |
---|---|
FR2054547B1 (en) | 1973-03-16 |
FR2054547A1 (en) | 1971-04-23 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Horikoshi | Production of alkaline enzymes by alkalophilic microorganisms: part i. alkaline protease produced by Bacillus no. 221 | |
Moldave | [103] The preparation of C14-amino acyl soluble-RNA | |
KR940005795A (en) | Novel phospholipase Al, preparation method and use thereof | |
GB1463513A (en) | Enzymes | |
Hayashida et al. | Formation of active derivatives of glucoamylase I during the digestion with fungal acid protease and α-mannosidase | |
EP0204284A2 (en) | A novel lipase | |
Erlanger et al. | Studies on aging in nematodes: II. Studies of the activities of several enzymes as a function of age | |
Uesaka et al. | Alpha-l-arabinofuranosidase from Rhodotorula flava | |
Hashimoto et al. | Studies on Xylanase from Trichoderma viride Part I. Isolation and Some Properties of Crystalline Xylanase | |
Yokoyama et al. | Submerged production, purification, and crystallization of acid carboxypeptidase from Penicillium janthinellum IFO-8070 | |
Bernier et al. | The turnip lysozyme | |
DOI et al. | Joint action of two glucanases produced by Arthrobacter in spheroplast formation from baker's yeast | |
Barrabin et al. | Isolation and characterization of gyroxin from Crotalus durissus terrificus venom | |
Murao et al. | Enzymes lytic against Pseudomonas aeruginosa produced by Bacillus subtilis YT-25 | |
GB1293563A (en) | Enzymes and methods for their preparation, isolation and purification | |
Hiramatsu | A Neutral Proteinase from Streptomycea naraensis: I. Purification and Some Properties | |
GB1498461A (en) | Quantitative determination of cholesterol | |
Tucci et al. | Preparation and properties of porcine parotid butyrylcholinesterase | |
Tanaka et al. | Specificity Studies of 4-L-Aspartylglycosylamine amido hydrolase | |
Ozaki et al. | Purification and properties of elastolytic enzyme from Flavobacterium immotum | |
Shimoi et al. | Purification of the enzymes responsible for the lysis of yeast cells by Rarobacter faecitabidus | |
Ichishima et al. | 1, 2-α-D-Mannosidase from a wood-rotting basidiomycete, Pycnoporus sanguineus | |
KAMEI et al. | Cholesterol esterase produced by Streptomyces lavendulae. II. Purification and properties as a lipolytic enzyme | |
Weil et al. | Studies on the proteolytic enzyme system of the pancreas | |
Tani et al. | Purification and characterization of the cholinesterase of Pseudomonas aeruginosa A-16 |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
PS | Patent sealed | ||
PLNP | Patent lapsed through nonpayment of renewal fees |