Isolation and properties of major components of Penicillium canescens extracellular enzyme complex
The composition of the enzyme complex secreted by Penicillium canescens was investigated. A scheme for purification of the main components of the complex by chromatofocusing on a Mono P column was developed. It was found that along with beta-galactosidase, the major components of the complex were en...
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| Veröffentlicht in: | Biochemistry (Moscow) 2003-11, Vol.68 (11), p.1200-1209 |
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| container_title | Biochemistry (Moscow) |
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| creator | Sinitsyna, O A Bukhtoyarov, F E Gusakov, A V Okunev, O N Bekkarevitch, A O Vinetsky, Yu P Sinitsyn, A P |
| description | The composition of the enzyme complex secreted by Penicillium canescens was investigated. A scheme for purification of the main components of the complex by chromatofocusing on a Mono P column was developed. It was found that along with beta-galactosidase, the major components of the complex were endo-beta-1,4-xylanase (31 kD, pI 8.2-9.3), alpha-L-arabinofuranosidase (60 kD, pI 7.6), arabinoxylan-arabinofuranohydrolase (70 kD, pI 3.8-4.0), and endo-beta-1,3/1,4-glucanase (40 kD, pI 4.4). The substrate specificity, pH and temperature activity optima, adsorbability, thermal stability, and ability for synergic interaction of the isolated enzymes were studied. |
| doi_str_mv | 10.1023/b:biry.0000009134.48246.7e |
| format | Article |
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A scheme for purification of the main components of the complex by chromatofocusing on a Mono P column was developed. It was found that along with beta-galactosidase, the major components of the complex were endo-beta-1,4-xylanase (31 kD, pI 8.2-9.3), alpha-L-arabinofuranosidase (60 kD, pI 7.6), arabinoxylan-arabinofuranohydrolase (70 kD, pI 3.8-4.0), and endo-beta-1,3/1,4-glucanase (40 kD, pI 4.4). 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A scheme for purification of the main components of the complex by chromatofocusing on a Mono P column was developed. It was found that along with beta-galactosidase, the major components of the complex were endo-beta-1,4-xylanase (31 kD, pI 8.2-9.3), alpha-L-arabinofuranosidase (60 kD, pI 7.6), arabinoxylan-arabinofuranohydrolase (70 kD, pI 3.8-4.0), and endo-beta-1,3/1,4-glucanase (40 kD, pI 4.4). The substrate specificity, pH and temperature activity optima, adsorbability, thermal stability, and ability for synergic interaction of the isolated enzymes were studied.</description><subject>beta-Galactosidase - chemistry</subject><subject>beta-Galactosidase - isolation & purification</subject><subject>Chromatography, Liquid</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Endo-1,3-beta-Glucanase - chemistry</subject><subject>Endo-1,3-beta-Glucanase - isolation & purification</subject><subject>Enzymes</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - isolation & purification</subject><subject>Glycoside Hydrolases - chemistry</subject><subject>Glycoside Hydrolases - isolation & purification</subject><subject>Penicillium - enzymology</subject><subject>Substrate Specificity</subject><issn>0006-2979</issn><issn>1608-3040</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNpdkV9LwzAUxYMoOqdfQcoefOtM0jRp96bDPwNBEX3wKSTpLXS0yUxa2Pz0ZnUgmJeQ3N-5OTcHoRnBc4JpdqMXuvG7OR5XSTI2ZwVlfC7gCE0Ix0WaYYaP0SSWeUpLUZ6h8xDW8UhxmZ2iM8I4wyWnE6RXwbWqb5xNlK2SjXcb8H0DIXF10qm184lx3cZZsP149wq2MU3bNkOXGGUhGLAhgW3vlYG2HVrlE7Dfuw5GYQvbC3RSqzbA5WGfoo-H-_flU_r88rha3j6nhuGiTwuuBc2EZsoUBErQeU6YItzoipVZDpmOQE4Uqcq64qxgUBUCG1WTHAsekSm6_u0bh_gaIPSya8LeU3TphiAFYZgXjEZw9g9cu8Hb6E0KSjlnZOy2-IWMdyF4qOXGN53yO0mw3Mcg7-Td6u1T_sUgxxikgCi-Orww6A6qP-nh37MfhNGGPg</recordid><startdate>20031101</startdate><enddate>20031101</enddate><creator>Sinitsyna, O A</creator><creator>Bukhtoyarov, F E</creator><creator>Gusakov, A V</creator><creator>Okunev, O N</creator><creator>Bekkarevitch, A O</creator><creator>Vinetsky, Yu P</creator><creator>Sinitsyn, A P</creator><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8C1</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20031101</creationdate><title>Isolation and properties of major components of Penicillium canescens extracellular enzyme complex</title><author>Sinitsyna, O A ; 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| subjects | beta-Galactosidase - chemistry beta-Galactosidase - isolation & purification Chromatography, Liquid Electrophoresis, Polyacrylamide Gel Endo-1,3-beta-Glucanase - chemistry Endo-1,3-beta-Glucanase - isolation & purification Enzymes Fungal Proteins - chemistry Fungal Proteins - isolation & purification Glycoside Hydrolases - chemistry Glycoside Hydrolases - isolation & purification Penicillium - enzymology Substrate Specificity |
| title | Isolation and properties of major components of Penicillium canescens extracellular enzyme complex |
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