Béguin, 1983 - Google Patents
Detection of cellulase activity in polyacrylamide gels using Congo red-stained agar replicasBéguin, 1983
- Document ID
- 17469091412591583543
- Author
- Béguin P
- Publication year
- Publication venue
- Analytical Biochemistry
External Links
Snippet
Bands that have cellulolytic activity are visualized after polyacrylamide gel electrophoresis by laying the slab gel on top of a thin sheet of 2% agar containing 0.1% carboxymethylcellulose. After a suitable incubation time, zones of carboxymethylcellulose …
- 239000000499 gel 0 title abstract description 29
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; 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.)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; 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
- C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
- C12N9/2437—Cellulases (3.2.1.4; 3.2.1.74; 3.2.1.91; 3.2.1.150)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
- C12N11/02—Enzymes or microbial cells being immobilised on or in an organic carrier
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Béguin | Detection of cellulase activity in polyacrylamide gels using Congo red-stained agar replicas | |
| Biely et al. | Remazol brilliant blue-xylan: a soluble chromogenic substrate for xylanases | |
| Ried et al. | Activity stain for rapid characterization of pectic enzymes in isoelectric focusing and sodium dodecyl sulfate-polyacrylamide gels | |
| Kwon et al. | Detection of β-glucosidase activity in polyacrylamide gels with esculin as substrate | |
| Wood et al. | Use of complex formation between Congo Red and polysaccharides in detection and assay of polysaccharide hydrolases | |
| Aiba et al. | Cloning and expression of thermostable α-amylase gene from Bacillus stearothermophilus in Bacillus stearothermophilus and Bacillus subtilis | |
| Workman et al. | Purification and properties of β-glucosidase from Aspergillus terreus | |
| JP2652871B2 (en) | Alkaline cellulase and method for producing the same | |
| Kluepfel | Screening of prokaryotes for cellulose-and hemicellulose-degrading enzymes | |
| Uchino et al. | A thermostable xylanase from a thermophilic acidophilic Bacillus sp. | |
| Yabuki et al. | Rapid induction of alpha-amylase by nongrowing mycelia of Aspergillus oryzae | |
| Klingeberg et al. | Properties of extremely thermostable proteases from anaerobic hyperthermophilic bacteria | |
| Kadowaki et al. | Xylanase production by Aspergillus tamarii | |
| Schmid et al. | Purification and partial characterization of a cellodextrin glucohydrolase (β‐glucosidase) from Trichoderma reesei strain QM 9414 | |
| Kluepfel et al. | Purification and characterization of a new xylanase (xylanase C) produced by Streptomyces lividans 66 | |
| Kerjan et al. | Characterization of a thermosensitive sporulation mutant of Bacillus subtilis affected in the structural gene of an intracellular protease | |
| Nevalainen | Induction, isolation, and characterization of Aspergillus niger mutant strains producing elevated levels of beta-galactosidase | |
| Matsuo et al. | Purification and some properties of β-xylosidase from Emericella nidulans | |
| Sanyal et al. | Extracellular cellulolytic enzyme system of Aspergillus japonicus: 2. Purification and characterization of an inducible extracellular β-glucosidase | |
| Cavedon et al. | Characterization of the extracellular cellulase from a mesophilic clostridium (strain C7) | |
| Ishihara et al. | Purification and some properties of a thermostable xylanase from thermophilic fungus strain HG-1 | |
| Sajedi et al. | Purification, characterization, and structural investigation of a new moderately thermophilic and partially calcium-independent extracellular α-amylase from Bacillus sp. TM1 | |
| Gilbert et al. | Characterization of the enzymes present in the cellulase system of Thielavia terrestris 255B | |
| Schmid et al. | Evidence for the lack of exo-cellobiohydrolase activity in the cellulase system of Trichoderma reesei QM 9414 | |
| Hiraoka et al. | Studies on Mold Dextranases: Some Physicochemical Properties and Substrate Specificity of Dextranases Obtained from Aspergillus carneus and Penicillium luteum |