Effective purification procedure of Aspergillus oryzae α-amylase from solid state fermentation cultures including Concanavalin A-Sepharose
Solid state fermentation cultures of Aspergillus oryzae NRRL 3485 on moistened wheat bran produced high levels of α-amylase as judged by the specific activity of water extracts (500-700 units/mg protein) and by the enzyme concentration (around 0.15 g/L ) in those extracts. The purification of α-amyl...
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1996
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| LEADER | 07680caa a22006377a 4500 | ||
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| 001 | PAPER-3404 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203252.0 | ||
| 008 | 140217s1996 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-0006647087 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 100 | 1 | |a Terebiznik, M.R. | |
| 245 | 1 | 0 | |a Effective purification procedure of Aspergillus oryzae α-amylase from solid state fermentation cultures including Concanavalin A-Sepharose |
| 260 | |c 1996 | ||
| 270 | 1 | 0 | |m Terebiznik, M.R.; Departamento de Industrias, Fac. de Ciencias Exactas y Naturales, Ciudad Universitaria, 1428 Buenos Aires, Argentina |
| 506 | |2 openaire |e Política editorial | ||
| 504 | |a Bergmeyer, H.U., Grassl, M., Reagents for enzymatic analysis: Enzymes α-glucosidase (1983) Methods of Enzymatic Analysis, 2, pp. 205-206. , 3rd ed. (H.U. Bergmeyer, ed.), Verlag Chemie GmbH, Weinheim | ||
| 504 | |a Bradford, M.M., A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding (1976) Anal. Biochem., 72, pp. 248-254 | ||
| 504 | |a Brandani, V., Di Giacomo, G., Spera, L., Extraction of protein α-amylase by reverse micelles (1993) Process Biochem., 28, pp. 411-414 | ||
| 504 | |a Cheng, C., Udaka, S., Efficient production of Taka-amylase by Trichoderma viride (1991) Agric. Biol. Chem., 55, pp. 1817-1822 | ||
| 504 | |a Ebisu, S., Mori, M., Takagi, H., Kadowaki, K., Yamagata, H., Tsukagoshi, N., Udaka, S., Production of a fungal protein. Taka-amylase, by protein producing Bacillus brevis HPD31 (1993) J. Indust. Microbiol., 11, pp. 83-88 | ||
| 504 | |a Errat, J.A., Douglas, P.E., Moranelli, F., Seligy, V.L., The induction of α-amylase by starch in Aspergillus oryzae: Evidence for controlled mRNA expression (1984) Can. J. Biochem. Cell Biol., 62, pp. 678-690 | ||
| 504 | |a Fogarty, M.W., Kelly, C.T., Amylases, amyloglucosidase and related glucanases (1980) Econ. Microbiol., 5. , (A.H. Rose, ed.), Academic Press, London | ||
| 504 | |a Hase, S., Fujimura, K., Kanoh, M., Ikenaka, T., Studies on heterogeneity of Taka-Amylase A: Isolation of an amylase having one N-acetylglucosamine residue as the sugar chain (1982) J. Biochem., 92, pp. 265-270 | ||
| 504 | |a Kalb, J., Levitzki, A., Metal-binding sites of concanavalin A and their role in binding of α-methyl D-glucopyranoside (1968) Biochem. J., 109, pp. 669-672 | ||
| 504 | |a Kong, X., Wang, Z., Cui, Y., Jiang, L., Purification and properties of alpha-amylase from Aspergillus oryzae 6-193 (1991) Acta Microbiol. Sinica, 31, pp. 274-280 | ||
| 504 | |a Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685 | ||
| 504 | |a Mckelvy, J., Lee, Y.C., Microheteroregeneity of the carbohydrate group of Aspergillus oryzae α-amylase (1969) Arch. Biochem. Biophys., 132, pp. 99-110 | ||
| 504 | |a Miranda, E.A., Berglund, K.A., Evaluation of column flotation in the downstream processing of fermentation products: Recovery of a genetically engineered α-amylase (1993) Biotechnol. Prog., 9, pp. 411-420 | ||
| 504 | |a Nelson, N., A photometric adaptation of the Somogyi method for the determination of glucose (1944) J. Biol. Chem., 153, pp. 375-380 | ||
| 504 | |a Oakley, B., Kirsh, O., Morris, N., A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide (1980) Anal. Biochem., 105, pp. 361-363 | ||
| 504 | |a Ono, K., Shigeta, S., Oka, S., Effective purification of glucoamylase in Koji, a solid culture of Aspergillus oryzae on steamed rice, by affinity chromatography using an immobilized acarbose (BAY G-5421) (1988) Agric. Biol. Chem., 52, pp. 1707-1714 | ||
| 504 | |a Ramana Murthy, M.V., Karanth, N.G., Raghava Rao, M.S., Biochemical engineering aspects of solid-state fermentation (1993) Adv. Appl. Microbiol., 38, pp. 99-147 | ||
| 504 | |a Randez-Gil, F., Sanz, P., Expression of Aspergillus oryzae α-amylase gene in Saccharomyces cerevisiae (1993) FEMS Microbiol. Lett., 112, pp. 119-123 | ||
| 504 | |a Rozie, H., Somers, W., Van't Riet, K., Rombouts, F.M., Visser, J., Crosslinked potato starch as an affinity adsorbent for bacterial α-amylase (1991) Carbohydr. Pol., 15, pp. 349-365 | ||
| 504 | |a Shibuya, I., Tamura, G., Ishikawa, T., Hara, S., Cloning of the alpha-amylase cDNA of Aspergillus shirousamii and its expression in Saccharomyces cerevisiae (1992) Biosci. Biotechnol. Biochem., 56, pp. 174-179 | ||
| 504 | |a Smith, B.W., Roe, J.H., A photometric method for the determination of α-amylase in blood and urine, with use of the starch-iodine color (1949) J. Biol. Chem., 179, pp. 53-58 | ||
| 504 | |a Turchi, S.L., Becker, T., Improved purification of α-amylase isolated from Rhizomucor pusillus by affinity chromatography (1987) Current Microbiol., 15, pp. 203-205 | ||
| 504 | |a Yamaguchi, H., Ikenaka, T., Matsushima, Y., The complete sequence of a glycopeptide obtained from Taka-amylase A (1971) J. Biochem., 70, pp. 587-594 | ||
| 504 | |a Yamakawa, Y., Okuyama, T., Heterogeneity of crystalline Takaamylase (1973) J. Biochem., 73, pp. 447-454 | ||
| 520 | 3 | |a Solid state fermentation cultures of Aspergillus oryzae NRRL 3485 on moistened wheat bran produced high levels of α-amylase as judged by the specific activity of water extracts (500-700 units/mg protein) and by the enzyme concentration (around 0.15 g/L ) in those extracts. The purification of α-amylase by affinity chromatography on Concanavalin A-Sepharose is described. A first DEAE-Sepharose chromatography step (binding of the enzyme contained in the water extract and further elution with 0.2 M NaCl, pH 5) was necessary in order to remove contaminants that hinder the binding of the glycoprotein α-amylase to the lectin. Elution was performed with 7.5 mM α-D-methylmannoside. The enzyme was obtained highly concentrated and purified with a specific activity of 2000 units/mg protein and a recovery of around 60%, free of α-glucosidase, amyloglucosidase and color contaminants. The purity of the enzyme preparation was assessed through nondenaturing gel electrophoresis and sucrose gradient centrifugation. An improvement of the performance of the purification procedure is presented in which the maximum capacities of both the anion exchanger and the lectin matrices were exploited. |l eng | |
| 593 | |a Departamento de Industrias, Ciudad Universitaria, 1428 Buenos Aires, Argentina | ||
| 593 | |a Depto. de Quim. Biológica, Fac. de Ciencias Exactas y Naturales, Ciudad Universitaria, 1428 Buenos Aires, Argentina | ||
| 593 | |a Departmento de Ing. Química, Facultad de Ingeniería, Ciudad Universitaria, 1428 Buenos Aires, Argentina | ||
| 593 | |a Departamento de Industrias, Fac. de Ciencias Exactas y Naturales, Ciudad Universitaria, 1428 Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a ASPERGILLUS ORYZAE |
| 690 | 1 | 0 | |a TRITICUM AESTIVUM |
| 700 | 1 | |a Pilosof, A.M.R. | |
| 700 | 1 | |a Moreno, S. | |
| 773 | 0 | |d 1996 |g v. 19 |h pp. 341-354 |k n. 5 |p J. Food Biochem. |x 01458884 |w (AR-BaUEN)CENRE-750 |t Journal of Food Biochemistry | |
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| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_01458884_v19_n5_p341_Terebiznik |y Handle |
| 856 | 4 | 0 | |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01458884_v19_n5_p341_Terebiznik |y Registro en la Biblioteca Digital |
| 961 | |a paper_01458884_v19_n5_p341_Terebiznik |b paper |c PE | ||
| 962 | |a info:eu-repo/semantics/article |a info:ar-repo/semantics/artículo |b info:eu-repo/semantics/publishedVersion | ||
| 999 | |c 64357 | ||