Immobilization and Stabilization of Xylanase by Multipoint Covalent Attachment on Agarose and on Chitosan Supports
Xylanases have important applications in industry. Immobilization and stabilization of enzymes may allow their reuse in many cycles of the reaction, decreasing the process costs. This work proposes the use of a rational approach to obtain immobilized commercial xylanase biocatalysts with optimized f...
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| Veröffentlicht in: | Applied biochemistry and biotechnology 2010-05, Vol.161 (1-8), p.455-467 |
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| creator | Manrich, Anny Komesu, Andrea Adriano, Wellington Sabino Tardioli, Paulo Waldir Giordano, Raquel Lima Camargo |
| description | Xylanases have important applications in industry. Immobilization and stabilization of enzymes may allow their reuse in many cycles of the reaction, decreasing the process costs. This work proposes the use of a rational approach to obtain immobilized commercial xylanase biocatalysts with optimized features. Xylanase NS50014 from Novozymes was characterized and immobilized on glyoxyl-agarose, agarose-glutaraldehyde, and agarose-amino-epoxy support and on differently activated chitosan supports: glutaraldehyde-chitosan, glyoxyl-chitosan, and epoxy-chitosan. Two different chitosan matrices were tested. The best chitosan derivative was epoxy-chitosan-xylanase, which presented 100% of immobilization yield and 64% of recovered activity. No significant increase on the thermal stability was observed for all the chitosan-enzyme derivatives. Immobilization on glyoxyl-agarose showed low yield immobilization and stabilization degrees of the obtained derivative. The low concentration of lysine groups in the enzyme molecule could explain these poor results. The protein was then chemically modified with ethylenediamine and immobilized on glyoxyl-agarose. The new enzyme derivatives were 40-fold more stable than the soluble, aminated, and dialyzed enzyme (70 °C, pH 7), with 100% of immobilization yield. Therefore, the increase of the number of amine groups in the enzyme surface was confirmed to be a good strategy to improve the properties of immobilized xylanase. |
| doi_str_mv | 10.1007/s12010-009-8897-0 |
| format | Article |
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Immobilization and stabilization of enzymes may allow their reuse in many cycles of the reaction, decreasing the process costs. This work proposes the use of a rational approach to obtain immobilized commercial xylanase biocatalysts with optimized features. Xylanase NS50014 from Novozymes was characterized and immobilized on glyoxyl-agarose, agarose-glutaraldehyde, and agarose-amino-epoxy support and on differently activated chitosan supports: glutaraldehyde-chitosan, glyoxyl-chitosan, and epoxy-chitosan. Two different chitosan matrices were tested. The best chitosan derivative was epoxy-chitosan-xylanase, which presented 100% of immobilization yield and 64% of recovered activity. No significant increase on the thermal stability was observed for all the chitosan-enzyme derivatives. Immobilization on glyoxyl-agarose showed low yield immobilization and stabilization degrees of the obtained derivative. The low concentration of lysine groups in the enzyme molecule could explain these poor results. The protein was then chemically modified with ethylenediamine and immobilized on glyoxyl-agarose. The new enzyme derivatives were 40-fold more stable than the soluble, aminated, and dialyzed enzyme (70 °C, pH 7), with 100% of immobilization yield. Therefore, the increase of the number of amine groups in the enzyme surface was confirmed to be a good strategy to improve the properties of immobilized xylanase.</description><identifier>ISSN: 0273-2289</identifier><identifier>EISSN: 1559-0291</identifier><identifier>DOI: 10.1007/s12010-009-8897-0</identifier><identifier>PMID: 20119636</identifier><identifier>CODEN: ABIBDL</identifier><language>eng</language><publisher>New York: Humana Press Inc</publisher><subject>Animals ; Biochemistry ; Biological and medical sciences ; Biotechnology ; Catalysts ; Chemical reactions ; Chemistry ; Chemistry and Materials Science ; Chitosan - chemistry ; Comparative studies ; Endo-1,4-beta Xylanases - chemistry ; Endo-1,4-beta Xylanases - metabolism ; Enzyme Stability ; Enzymes ; Enzymes, Immobilized - chemistry ; Enzymes, Immobilized - metabolism ; Fundamental and applied biological sciences. Psychology ; Gels - chemistry ; General aspects ; Hydrogen-Ion Concentration ; Immobilization techniques ; Methods. Procedures. 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Immobilization and stabilization of enzymes may allow their reuse in many cycles of the reaction, decreasing the process costs. This work proposes the use of a rational approach to obtain immobilized commercial xylanase biocatalysts with optimized features. Xylanase NS50014 from Novozymes was characterized and immobilized on glyoxyl-agarose, agarose-glutaraldehyde, and agarose-amino-epoxy support and on differently activated chitosan supports: glutaraldehyde-chitosan, glyoxyl-chitosan, and epoxy-chitosan. Two different chitosan matrices were tested. The best chitosan derivative was epoxy-chitosan-xylanase, which presented 100% of immobilization yield and 64% of recovered activity. No significant increase on the thermal stability was observed for all the chitosan-enzyme derivatives. Immobilization on glyoxyl-agarose showed low yield immobilization and stabilization degrees of the obtained derivative. The low concentration of lysine groups in the enzyme molecule could explain these poor results. The protein was then chemically modified with ethylenediamine and immobilized on glyoxyl-agarose. The new enzyme derivatives were 40-fold more stable than the soluble, aminated, and dialyzed enzyme (70 °C, pH 7), with 100% of immobilization yield. Therefore, the increase of the number of amine groups in the enzyme surface was confirmed to be a good strategy to improve the properties of immobilized xylanase.</description><subject>Animals</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Catalysts</subject><subject>Chemical reactions</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chitosan - chemistry</subject><subject>Comparative studies</subject><subject>Endo-1,4-beta Xylanases - chemistry</subject><subject>Endo-1,4-beta Xylanases - metabolism</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Enzymes, Immobilized - chemistry</subject><subject>Enzymes, Immobilized - metabolism</subject><subject>Fundamental and applied biological sciences. 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Immobilization and stabilization of enzymes may allow their reuse in many cycles of the reaction, decreasing the process costs. This work proposes the use of a rational approach to obtain immobilized commercial xylanase biocatalysts with optimized features. Xylanase NS50014 from Novozymes was characterized and immobilized on glyoxyl-agarose, agarose-glutaraldehyde, and agarose-amino-epoxy support and on differently activated chitosan supports: glutaraldehyde-chitosan, glyoxyl-chitosan, and epoxy-chitosan. Two different chitosan matrices were tested. The best chitosan derivative was epoxy-chitosan-xylanase, which presented 100% of immobilization yield and 64% of recovered activity. No significant increase on the thermal stability was observed for all the chitosan-enzyme derivatives. Immobilization on glyoxyl-agarose showed low yield immobilization and stabilization degrees of the obtained derivative. The low concentration of lysine groups in the enzyme molecule could explain these poor results. The protein was then chemically modified with ethylenediamine and immobilized on glyoxyl-agarose. The new enzyme derivatives were 40-fold more stable than the soluble, aminated, and dialyzed enzyme (70 °C, pH 7), with 100% of immobilization yield. Therefore, the increase of the number of amine groups in the enzyme surface was confirmed to be a good strategy to improve the properties of immobilized xylanase.</abstract><cop>New York</cop><pub>Humana Press Inc</pub><pmid>20119636</pmid><doi>10.1007/s12010-009-8897-0</doi><tpages>13</tpages></addata></record> |
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| subjects | Animals Biochemistry Biological and medical sciences Biotechnology Catalysts Chemical reactions Chemistry Chemistry and Materials Science Chitosan - chemistry Comparative studies Endo-1,4-beta Xylanases - chemistry Endo-1,4-beta Xylanases - metabolism Enzyme Stability Enzymes Enzymes, Immobilized - chemistry Enzymes, Immobilized - metabolism Fundamental and applied biological sciences. Psychology Gels - chemistry General aspects Hydrogen-Ion Concentration Immobilization techniques Methods. Procedures. Technologies Sepharose - chemistry Temperature |
| title | Immobilization and Stabilization of Xylanase by Multipoint Covalent Attachment on Agarose and on Chitosan Supports |
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