Characterization of a chimeric enzyme comprising feruloyl esterase and family 42 carbohydrate-binding module
Abstract We engineered a chimeric enzyme (AwFaeA-CBM42) comprising of type-A feruloyl esterase from Aspergillus awamori (AwFaeA) and family 42 carbohydrate-binding module (AkCBM42) from glycoside hydrolase family 54 α-l-arabinofuranosidase of Aspergillus kawachii. The chimeric enzyme was successfull...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Koseki, Takuya [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2009 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer-Verlag 2009 |
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| Übergeordnetes Werk: |
Enthalten in: Applied microbiology and biotechnology - Springer-Verlag, 1984, 86(2009), 1 vom: 16. Sept., Seite 155-161 |
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| Übergeordnetes Werk: |
volume:86 ; year:2009 ; number:1 ; day:16 ; month:09 ; pages:155-161 |
| Links: |
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| DOI / URN: |
10.1007/s00253-009-2224-0 |
|---|
| Katalog-ID: |
OLC2050726880 |
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| 245 | 1 | 0 | |a Characterization of a chimeric enzyme comprising feruloyl esterase and family 42 carbohydrate-binding module |
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| 520 | |a Abstract We engineered a chimeric enzyme (AwFaeA-CBM42) comprising of type-A feruloyl esterase from Aspergillus awamori (AwFaeA) and family 42 carbohydrate-binding module (AkCBM42) from glycoside hydrolase family 54 α-l-arabinofuranosidase of Aspergillus kawachii. The chimeric enzyme was successfully produced in Pichia pastoris and accumulated in the culture broth. The purified chimeric enzyme had an apparent relative molecular mass (Mr) of 53,000. The chimeric enzyme binds to arabinoxylan; this indicates that the AkCBM42 in AwFaeA-CBM42 binds to arabinofuranose side chain moiety of arabinoxylan. The thermostability of the chimeric enzyme was greater than that of AwFaeA. No significant difference of the specific activity toward methyl ferulate was observed between the AwFaeA and chimeric enzyme, but the release of ferulic acid from insoluble arabinoxylan by the chimeric enzyme was approximately 4-fold higher than that achieved by AwFaeA alone. In addition, the chimeric enzyme and xylanase acted synergistically for the degradation of arabinoxylan. In conclusion, the findings of our study demonstrated that the components of the AwFaeA-CBM42 chimeric enzyme act synergistically to bring about the degradation of complex substrates and that the family 42 carbohydrate-binding module has potential for application in the degradation of polysaccharides. | ||
| 650 | 4 | |a Chimeric enzyme | |
| 650 | 4 | |a Feruloyl esterase | |
| 650 | 4 | |a α- | |
| 650 | 4 | |a -arabinofuranosidase | |
| 650 | 4 | |a CBM42 | |
| 650 | 4 | |a Arabinoxylan | |
| 700 | 1 | |a Mochizuki, Keiji |4 aut | |
| 700 | 1 | |a Kisara, Hiroe |4 aut | |
| 700 | 1 | |a Miyanaga, Akimasa |4 aut | |
| 700 | 1 | |a Fushinobu, Shinya |4 aut | |
| 700 | 1 | |a Murayama, Tetsuya |4 aut | |
| 700 | 1 | |a Shiono, Yoshihito |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Applied microbiology and biotechnology |d Springer-Verlag, 1984 |g 86(2009), 1 vom: 16. Sept., Seite 155-161 |w (DE-627)129942634 |w (DE-600)392453-1 |w (DE-576)015507750 |x 0175-7598 |7 nnns |
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10.1007/s00253-009-2224-0 doi (DE-627)OLC2050726880 (DE-He213)s00253-009-2224-0-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Koseki, Takuya verfasserin aut Characterization of a chimeric enzyme comprising feruloyl esterase and family 42 carbohydrate-binding module 2009 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2009 Abstract We engineered a chimeric enzyme (AwFaeA-CBM42) comprising of type-A feruloyl esterase from Aspergillus awamori (AwFaeA) and family 42 carbohydrate-binding module (AkCBM42) from glycoside hydrolase family 54 α-l-arabinofuranosidase of Aspergillus kawachii. The chimeric enzyme was successfully produced in Pichia pastoris and accumulated in the culture broth. The purified chimeric enzyme had an apparent relative molecular mass (Mr) of 53,000. The chimeric enzyme binds to arabinoxylan; this indicates that the AkCBM42 in AwFaeA-CBM42 binds to arabinofuranose side chain moiety of arabinoxylan. The thermostability of the chimeric enzyme was greater than that of AwFaeA. No significant difference of the specific activity toward methyl ferulate was observed between the AwFaeA and chimeric enzyme, but the release of ferulic acid from insoluble arabinoxylan by the chimeric enzyme was approximately 4-fold higher than that achieved by AwFaeA alone. In addition, the chimeric enzyme and xylanase acted synergistically for the degradation of arabinoxylan. In conclusion, the findings of our study demonstrated that the components of the AwFaeA-CBM42 chimeric enzyme act synergistically to bring about the degradation of complex substrates and that the family 42 carbohydrate-binding module has potential for application in the degradation of polysaccharides. Chimeric enzyme Feruloyl esterase α- -arabinofuranosidase CBM42 Arabinoxylan Mochizuki, Keiji aut Kisara, Hiroe aut Miyanaga, Akimasa aut Fushinobu, Shinya aut Murayama, Tetsuya aut Shiono, Yoshihito aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 86(2009), 1 vom: 16. Sept., Seite 155-161 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:86 year:2009 number:1 day:16 month:09 pages:155-161 https://doi.org/10.1007/s00253-009-2224-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_23 GBV_ILN_40 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 86 2009 1 16 09 155-161 |
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10.1007/s00253-009-2224-0 doi (DE-627)OLC2050726880 (DE-He213)s00253-009-2224-0-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Koseki, Takuya verfasserin aut Characterization of a chimeric enzyme comprising feruloyl esterase and family 42 carbohydrate-binding module 2009 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2009 Abstract We engineered a chimeric enzyme (AwFaeA-CBM42) comprising of type-A feruloyl esterase from Aspergillus awamori (AwFaeA) and family 42 carbohydrate-binding module (AkCBM42) from glycoside hydrolase family 54 α-l-arabinofuranosidase of Aspergillus kawachii. The chimeric enzyme was successfully produced in Pichia pastoris and accumulated in the culture broth. The purified chimeric enzyme had an apparent relative molecular mass (Mr) of 53,000. The chimeric enzyme binds to arabinoxylan; this indicates that the AkCBM42 in AwFaeA-CBM42 binds to arabinofuranose side chain moiety of arabinoxylan. The thermostability of the chimeric enzyme was greater than that of AwFaeA. No significant difference of the specific activity toward methyl ferulate was observed between the AwFaeA and chimeric enzyme, but the release of ferulic acid from insoluble arabinoxylan by the chimeric enzyme was approximately 4-fold higher than that achieved by AwFaeA alone. In addition, the chimeric enzyme and xylanase acted synergistically for the degradation of arabinoxylan. In conclusion, the findings of our study demonstrated that the components of the AwFaeA-CBM42 chimeric enzyme act synergistically to bring about the degradation of complex substrates and that the family 42 carbohydrate-binding module has potential for application in the degradation of polysaccharides. Chimeric enzyme Feruloyl esterase α- -arabinofuranosidase CBM42 Arabinoxylan Mochizuki, Keiji aut Kisara, Hiroe aut Miyanaga, Akimasa aut Fushinobu, Shinya aut Murayama, Tetsuya aut Shiono, Yoshihito aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 86(2009), 1 vom: 16. Sept., Seite 155-161 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:86 year:2009 number:1 day:16 month:09 pages:155-161 https://doi.org/10.1007/s00253-009-2224-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_23 GBV_ILN_40 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 86 2009 1 16 09 155-161 |
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10.1007/s00253-009-2224-0 doi (DE-627)OLC2050726880 (DE-He213)s00253-009-2224-0-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Koseki, Takuya verfasserin aut Characterization of a chimeric enzyme comprising feruloyl esterase and family 42 carbohydrate-binding module 2009 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2009 Abstract We engineered a chimeric enzyme (AwFaeA-CBM42) comprising of type-A feruloyl esterase from Aspergillus awamori (AwFaeA) and family 42 carbohydrate-binding module (AkCBM42) from glycoside hydrolase family 54 α-l-arabinofuranosidase of Aspergillus kawachii. The chimeric enzyme was successfully produced in Pichia pastoris and accumulated in the culture broth. The purified chimeric enzyme had an apparent relative molecular mass (Mr) of 53,000. The chimeric enzyme binds to arabinoxylan; this indicates that the AkCBM42 in AwFaeA-CBM42 binds to arabinofuranose side chain moiety of arabinoxylan. The thermostability of the chimeric enzyme was greater than that of AwFaeA. No significant difference of the specific activity toward methyl ferulate was observed between the AwFaeA and chimeric enzyme, but the release of ferulic acid from insoluble arabinoxylan by the chimeric enzyme was approximately 4-fold higher than that achieved by AwFaeA alone. In addition, the chimeric enzyme and xylanase acted synergistically for the degradation of arabinoxylan. In conclusion, the findings of our study demonstrated that the components of the AwFaeA-CBM42 chimeric enzyme act synergistically to bring about the degradation of complex substrates and that the family 42 carbohydrate-binding module has potential for application in the degradation of polysaccharides. Chimeric enzyme Feruloyl esterase α- -arabinofuranosidase CBM42 Arabinoxylan Mochizuki, Keiji aut Kisara, Hiroe aut Miyanaga, Akimasa aut Fushinobu, Shinya aut Murayama, Tetsuya aut Shiono, Yoshihito aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 86(2009), 1 vom: 16. Sept., Seite 155-161 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:86 year:2009 number:1 day:16 month:09 pages:155-161 https://doi.org/10.1007/s00253-009-2224-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_23 GBV_ILN_40 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 86 2009 1 16 09 155-161 |
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10.1007/s00253-009-2224-0 doi (DE-627)OLC2050726880 (DE-He213)s00253-009-2224-0-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Koseki, Takuya verfasserin aut Characterization of a chimeric enzyme comprising feruloyl esterase and family 42 carbohydrate-binding module 2009 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2009 Abstract We engineered a chimeric enzyme (AwFaeA-CBM42) comprising of type-A feruloyl esterase from Aspergillus awamori (AwFaeA) and family 42 carbohydrate-binding module (AkCBM42) from glycoside hydrolase family 54 α-l-arabinofuranosidase of Aspergillus kawachii. The chimeric enzyme was successfully produced in Pichia pastoris and accumulated in the culture broth. The purified chimeric enzyme had an apparent relative molecular mass (Mr) of 53,000. The chimeric enzyme binds to arabinoxylan; this indicates that the AkCBM42 in AwFaeA-CBM42 binds to arabinofuranose side chain moiety of arabinoxylan. The thermostability of the chimeric enzyme was greater than that of AwFaeA. No significant difference of the specific activity toward methyl ferulate was observed between the AwFaeA and chimeric enzyme, but the release of ferulic acid from insoluble arabinoxylan by the chimeric enzyme was approximately 4-fold higher than that achieved by AwFaeA alone. In addition, the chimeric enzyme and xylanase acted synergistically for the degradation of arabinoxylan. In conclusion, the findings of our study demonstrated that the components of the AwFaeA-CBM42 chimeric enzyme act synergistically to bring about the degradation of complex substrates and that the family 42 carbohydrate-binding module has potential for application in the degradation of polysaccharides. Chimeric enzyme Feruloyl esterase α- -arabinofuranosidase CBM42 Arabinoxylan Mochizuki, Keiji aut Kisara, Hiroe aut Miyanaga, Akimasa aut Fushinobu, Shinya aut Murayama, Tetsuya aut Shiono, Yoshihito aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 86(2009), 1 vom: 16. Sept., Seite 155-161 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:86 year:2009 number:1 day:16 month:09 pages:155-161 https://doi.org/10.1007/s00253-009-2224-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_23 GBV_ILN_40 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 86 2009 1 16 09 155-161 |
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10.1007/s00253-009-2224-0 doi (DE-627)OLC2050726880 (DE-He213)s00253-009-2224-0-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Koseki, Takuya verfasserin aut Characterization of a chimeric enzyme comprising feruloyl esterase and family 42 carbohydrate-binding module 2009 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2009 Abstract We engineered a chimeric enzyme (AwFaeA-CBM42) comprising of type-A feruloyl esterase from Aspergillus awamori (AwFaeA) and family 42 carbohydrate-binding module (AkCBM42) from glycoside hydrolase family 54 α-l-arabinofuranosidase of Aspergillus kawachii. The chimeric enzyme was successfully produced in Pichia pastoris and accumulated in the culture broth. The purified chimeric enzyme had an apparent relative molecular mass (Mr) of 53,000. The chimeric enzyme binds to arabinoxylan; this indicates that the AkCBM42 in AwFaeA-CBM42 binds to arabinofuranose side chain moiety of arabinoxylan. The thermostability of the chimeric enzyme was greater than that of AwFaeA. No significant difference of the specific activity toward methyl ferulate was observed between the AwFaeA and chimeric enzyme, but the release of ferulic acid from insoluble arabinoxylan by the chimeric enzyme was approximately 4-fold higher than that achieved by AwFaeA alone. In addition, the chimeric enzyme and xylanase acted synergistically for the degradation of arabinoxylan. In conclusion, the findings of our study demonstrated that the components of the AwFaeA-CBM42 chimeric enzyme act synergistically to bring about the degradation of complex substrates and that the family 42 carbohydrate-binding module has potential for application in the degradation of polysaccharides. Chimeric enzyme Feruloyl esterase α- -arabinofuranosidase CBM42 Arabinoxylan Mochizuki, Keiji aut Kisara, Hiroe aut Miyanaga, Akimasa aut Fushinobu, Shinya aut Murayama, Tetsuya aut Shiono, Yoshihito aut Enthalten in Applied microbiology and biotechnology Springer-Verlag, 1984 86(2009), 1 vom: 16. Sept., Seite 155-161 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:86 year:2009 number:1 day:16 month:09 pages:155-161 https://doi.org/10.1007/s00253-009-2224-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_23 GBV_ILN_40 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 86 2009 1 16 09 155-161 |
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Enthalten in Applied microbiology and biotechnology 86(2009), 1 vom: 16. Sept., Seite 155-161 volume:86 year:2009 number:1 day:16 month:09 pages:155-161 |
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Enthalten in Applied microbiology and biotechnology 86(2009), 1 vom: 16. Sept., Seite 155-161 volume:86 year:2009 number:1 day:16 month:09 pages:155-161 |
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Koseki, Takuya @@aut@@ Mochizuki, Keiji @@aut@@ Kisara, Hiroe @@aut@@ Miyanaga, Akimasa @@aut@@ Fushinobu, Shinya @@aut@@ Murayama, Tetsuya @@aut@@ Shiono, Yoshihito @@aut@@ |
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Koseki, Takuya |
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Koseki, Takuya ddc 570 ssgn 12 fid BIODIV misc Chimeric enzyme misc Feruloyl esterase misc α- misc -arabinofuranosidase misc CBM42 misc Arabinoxylan Characterization of a chimeric enzyme comprising feruloyl esterase and family 42 carbohydrate-binding module |
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570 VZ 12 ssgn BIODIV DE-30 fid Characterization of a chimeric enzyme comprising feruloyl esterase and family 42 carbohydrate-binding module Chimeric enzyme Feruloyl esterase α- -arabinofuranosidase CBM42 Arabinoxylan |
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Koseki, Takuya Mochizuki, Keiji Kisara, Hiroe Miyanaga, Akimasa Fushinobu, Shinya Murayama, Tetsuya Shiono, Yoshihito |
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characterization of a chimeric enzyme comprising feruloyl esterase and family 42 carbohydrate-binding module |
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Characterization of a chimeric enzyme comprising feruloyl esterase and family 42 carbohydrate-binding module |
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Abstract We engineered a chimeric enzyme (AwFaeA-CBM42) comprising of type-A feruloyl esterase from Aspergillus awamori (AwFaeA) and family 42 carbohydrate-binding module (AkCBM42) from glycoside hydrolase family 54 α-l-arabinofuranosidase of Aspergillus kawachii. The chimeric enzyme was successfully produced in Pichia pastoris and accumulated in the culture broth. The purified chimeric enzyme had an apparent relative molecular mass (Mr) of 53,000. The chimeric enzyme binds to arabinoxylan; this indicates that the AkCBM42 in AwFaeA-CBM42 binds to arabinofuranose side chain moiety of arabinoxylan. The thermostability of the chimeric enzyme was greater than that of AwFaeA. No significant difference of the specific activity toward methyl ferulate was observed between the AwFaeA and chimeric enzyme, but the release of ferulic acid from insoluble arabinoxylan by the chimeric enzyme was approximately 4-fold higher than that achieved by AwFaeA alone. In addition, the chimeric enzyme and xylanase acted synergistically for the degradation of arabinoxylan. In conclusion, the findings of our study demonstrated that the components of the AwFaeA-CBM42 chimeric enzyme act synergistically to bring about the degradation of complex substrates and that the family 42 carbohydrate-binding module has potential for application in the degradation of polysaccharides. © Springer-Verlag 2009 |
| abstractGer |
Abstract We engineered a chimeric enzyme (AwFaeA-CBM42) comprising of type-A feruloyl esterase from Aspergillus awamori (AwFaeA) and family 42 carbohydrate-binding module (AkCBM42) from glycoside hydrolase family 54 α-l-arabinofuranosidase of Aspergillus kawachii. The chimeric enzyme was successfully produced in Pichia pastoris and accumulated in the culture broth. The purified chimeric enzyme had an apparent relative molecular mass (Mr) of 53,000. The chimeric enzyme binds to arabinoxylan; this indicates that the AkCBM42 in AwFaeA-CBM42 binds to arabinofuranose side chain moiety of arabinoxylan. The thermostability of the chimeric enzyme was greater than that of AwFaeA. No significant difference of the specific activity toward methyl ferulate was observed between the AwFaeA and chimeric enzyme, but the release of ferulic acid from insoluble arabinoxylan by the chimeric enzyme was approximately 4-fold higher than that achieved by AwFaeA alone. In addition, the chimeric enzyme and xylanase acted synergistically for the degradation of arabinoxylan. In conclusion, the findings of our study demonstrated that the components of the AwFaeA-CBM42 chimeric enzyme act synergistically to bring about the degradation of complex substrates and that the family 42 carbohydrate-binding module has potential for application in the degradation of polysaccharides. © Springer-Verlag 2009 |
| abstract_unstemmed |
Abstract We engineered a chimeric enzyme (AwFaeA-CBM42) comprising of type-A feruloyl esterase from Aspergillus awamori (AwFaeA) and family 42 carbohydrate-binding module (AkCBM42) from glycoside hydrolase family 54 α-l-arabinofuranosidase of Aspergillus kawachii. The chimeric enzyme was successfully produced in Pichia pastoris and accumulated in the culture broth. The purified chimeric enzyme had an apparent relative molecular mass (Mr) of 53,000. The chimeric enzyme binds to arabinoxylan; this indicates that the AkCBM42 in AwFaeA-CBM42 binds to arabinofuranose side chain moiety of arabinoxylan. The thermostability of the chimeric enzyme was greater than that of AwFaeA. No significant difference of the specific activity toward methyl ferulate was observed between the AwFaeA and chimeric enzyme, but the release of ferulic acid from insoluble arabinoxylan by the chimeric enzyme was approximately 4-fold higher than that achieved by AwFaeA alone. In addition, the chimeric enzyme and xylanase acted synergistically for the degradation of arabinoxylan. In conclusion, the findings of our study demonstrated that the components of the AwFaeA-CBM42 chimeric enzyme act synergistically to bring about the degradation of complex substrates and that the family 42 carbohydrate-binding module has potential for application in the degradation of polysaccharides. © Springer-Verlag 2009 |
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The chimeric enzyme was successfully produced in Pichia pastoris and accumulated in the culture broth. The purified chimeric enzyme had an apparent relative molecular mass (Mr) of 53,000. The chimeric enzyme binds to arabinoxylan; this indicates that the AkCBM42 in AwFaeA-CBM42 binds to arabinofuranose side chain moiety of arabinoxylan. The thermostability of the chimeric enzyme was greater than that of AwFaeA. No significant difference of the specific activity toward methyl ferulate was observed between the AwFaeA and chimeric enzyme, but the release of ferulic acid from insoluble arabinoxylan by the chimeric enzyme was approximately 4-fold higher than that achieved by AwFaeA alone. In addition, the chimeric enzyme and xylanase acted synergistically for the degradation of arabinoxylan. 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