Purification and characterization of a biodegradable plastic-degrading enzyme from Aspergillus oryzae
Abstract We used biodegradable plastics as fermentation substrates for the filamentous fungus Aspergillus oryzae. This fungus could grow under culture conditions that contained emulsified poly-(butylene succinate) (PBS) and emulsified poly-(butylene succinate-co-adipate) (PBSA) as the sole carbon so...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Maeda, Hiroshi [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2005 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer-Verlag 2005 |
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| Übergeordnetes Werk: |
Enthalten in: Applied microbiology and biotechnology - Berlin : Springer, 1975, 67(2005), 6 vom: 27. Jan., Seite 778-788 |
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| Übergeordnetes Werk: |
volume:67 ; year:2005 ; number:6 ; day:27 ; month:01 ; pages:778-788 |
| Links: |
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| DOI / URN: |
10.1007/s00253-004-1853-6 |
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| Katalog-ID: |
SPR002937492 |
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| 100 | 1 | |a Maeda, Hiroshi |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Purification and characterization of a biodegradable plastic-degrading enzyme from Aspergillus oryzae |
| 264 | 1 | |c 2005 | |
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| 500 | |a © Springer-Verlag 2005 | ||
| 520 | |a Abstract We used biodegradable plastics as fermentation substrates for the filamentous fungus Aspergillus oryzae. This fungus could grow under culture conditions that contained emulsified poly-(butylene succinate) (PBS) and emulsified poly-(butylene succinate-co-adipate) (PBSA) as the sole carbon source, and could digest PBS and PBSA, as indicated by clearing of the culture supernatant. We purified the PBS-degrading enzyme from the culture supernatant, and its molecular mass was determined as 21.6 kDa. The enzyme was identified as cutinase based on internal amino acid sequences. Specific activities against PBS, PBSA and poly-(lactic acid) (PLA) were determined as 0.42 U/mg, 11 U/mg and 0.067 U/mg, respectively. To obtain a better understanding of how the enzyme recognizes and hydrolyzes PBS/PBSA, we investigated the environment of the catalytic pocket, which is divided into carboxylic acid and alcohol recognition sites. The affinities for different substrates depended on the carbon chain length of the carboxylic acid in the substrate. Competitive inhibition modes were exhibited by carboxylic acids and alcohols that consisted of $ C_{4} $-$ C_{6} $ and $ C_{3} $-$ C_{8} $ chain lengths, respectively. Determination of the affinities for different chemicals indicated that the most preferred substrate for the enzyme would consist of butyric acid and n-hexanol. | ||
| 650 | 4 | |a Succinic Acid |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Hexanoic Acid |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Biodegradable Plastic |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Inhibition Mode |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Butylene Succinate |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Yamagata, Youhei |4 aut | |
| 700 | 1 | |a Abe, Keietsu |4 aut | |
| 700 | 1 | |a Hasegawa, Fumihiko |4 aut | |
| 700 | 1 | |a Machida, Masayuki |4 aut | |
| 700 | 1 | |a Ishioka, Ryoji |4 aut | |
| 700 | 1 | |a Gomi, Katsuya |4 aut | |
| 700 | 1 | |a Nakajima, Tasuku |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Applied microbiology and biotechnology |d Berlin : Springer, 1975 |g 67(2005), 6 vom: 27. Jan., Seite 778-788 |w (DE-627)265509564 |w (DE-600)1464336-4 |x 1432-0614 |7 nnns |
| 773 | 1 | 8 | |g volume:67 |g year:2005 |g number:6 |g day:27 |g month:01 |g pages:778-788 |
| 856 | 4 | 0 | |u https://dx.doi.org/10.1007/s00253-004-1853-6 |z lizenzpflichtig |3 Volltext |
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10.1007/s00253-004-1853-6 doi (DE-627)SPR002937492 (SPR)s00253-004-1853-6-e DE-627 ger DE-627 rakwb eng Maeda, Hiroshi verfasserin aut Purification and characterization of a biodegradable plastic-degrading enzyme from Aspergillus oryzae 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2005 Abstract We used biodegradable plastics as fermentation substrates for the filamentous fungus Aspergillus oryzae. This fungus could grow under culture conditions that contained emulsified poly-(butylene succinate) (PBS) and emulsified poly-(butylene succinate-co-adipate) (PBSA) as the sole carbon source, and could digest PBS and PBSA, as indicated by clearing of the culture supernatant. We purified the PBS-degrading enzyme from the culture supernatant, and its molecular mass was determined as 21.6 kDa. The enzyme was identified as cutinase based on internal amino acid sequences. Specific activities against PBS, PBSA and poly-(lactic acid) (PLA) were determined as 0.42 U/mg, 11 U/mg and 0.067 U/mg, respectively. To obtain a better understanding of how the enzyme recognizes and hydrolyzes PBS/PBSA, we investigated the environment of the catalytic pocket, which is divided into carboxylic acid and alcohol recognition sites. The affinities for different substrates depended on the carbon chain length of the carboxylic acid in the substrate. Competitive inhibition modes were exhibited by carboxylic acids and alcohols that consisted of $ C_{4} $-$ C_{6} $ and $ C_{3} $-$ C_{8} $ chain lengths, respectively. Determination of the affinities for different chemicals indicated that the most preferred substrate for the enzyme would consist of butyric acid and n-hexanol. Succinic Acid (dpeaa)DE-He213 Hexanoic Acid (dpeaa)DE-He213 Biodegradable Plastic (dpeaa)DE-He213 Inhibition Mode (dpeaa)DE-He213 Butylene Succinate (dpeaa)DE-He213 Yamagata, Youhei aut Abe, Keietsu aut Hasegawa, Fumihiko aut Machida, Masayuki aut Ishioka, Ryoji aut Gomi, Katsuya aut Nakajima, Tasuku aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 67(2005), 6 vom: 27. Jan., Seite 778-788 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:67 year:2005 number:6 day:27 month:01 pages:778-788 https://dx.doi.org/10.1007/s00253-004-1853-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 67 2005 6 27 01 778-788 |
| spelling |
10.1007/s00253-004-1853-6 doi (DE-627)SPR002937492 (SPR)s00253-004-1853-6-e DE-627 ger DE-627 rakwb eng Maeda, Hiroshi verfasserin aut Purification and characterization of a biodegradable plastic-degrading enzyme from Aspergillus oryzae 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2005 Abstract We used biodegradable plastics as fermentation substrates for the filamentous fungus Aspergillus oryzae. This fungus could grow under culture conditions that contained emulsified poly-(butylene succinate) (PBS) and emulsified poly-(butylene succinate-co-adipate) (PBSA) as the sole carbon source, and could digest PBS and PBSA, as indicated by clearing of the culture supernatant. We purified the PBS-degrading enzyme from the culture supernatant, and its molecular mass was determined as 21.6 kDa. The enzyme was identified as cutinase based on internal amino acid sequences. Specific activities against PBS, PBSA and poly-(lactic acid) (PLA) were determined as 0.42 U/mg, 11 U/mg and 0.067 U/mg, respectively. To obtain a better understanding of how the enzyme recognizes and hydrolyzes PBS/PBSA, we investigated the environment of the catalytic pocket, which is divided into carboxylic acid and alcohol recognition sites. The affinities for different substrates depended on the carbon chain length of the carboxylic acid in the substrate. Competitive inhibition modes were exhibited by carboxylic acids and alcohols that consisted of $ C_{4} $-$ C_{6} $ and $ C_{3} $-$ C_{8} $ chain lengths, respectively. Determination of the affinities for different chemicals indicated that the most preferred substrate for the enzyme would consist of butyric acid and n-hexanol. Succinic Acid (dpeaa)DE-He213 Hexanoic Acid (dpeaa)DE-He213 Biodegradable Plastic (dpeaa)DE-He213 Inhibition Mode (dpeaa)DE-He213 Butylene Succinate (dpeaa)DE-He213 Yamagata, Youhei aut Abe, Keietsu aut Hasegawa, Fumihiko aut Machida, Masayuki aut Ishioka, Ryoji aut Gomi, Katsuya aut Nakajima, Tasuku aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 67(2005), 6 vom: 27. Jan., Seite 778-788 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:67 year:2005 number:6 day:27 month:01 pages:778-788 https://dx.doi.org/10.1007/s00253-004-1853-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 67 2005 6 27 01 778-788 |
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10.1007/s00253-004-1853-6 doi (DE-627)SPR002937492 (SPR)s00253-004-1853-6-e DE-627 ger DE-627 rakwb eng Maeda, Hiroshi verfasserin aut Purification and characterization of a biodegradable plastic-degrading enzyme from Aspergillus oryzae 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2005 Abstract We used biodegradable plastics as fermentation substrates for the filamentous fungus Aspergillus oryzae. This fungus could grow under culture conditions that contained emulsified poly-(butylene succinate) (PBS) and emulsified poly-(butylene succinate-co-adipate) (PBSA) as the sole carbon source, and could digest PBS and PBSA, as indicated by clearing of the culture supernatant. We purified the PBS-degrading enzyme from the culture supernatant, and its molecular mass was determined as 21.6 kDa. The enzyme was identified as cutinase based on internal amino acid sequences. Specific activities against PBS, PBSA and poly-(lactic acid) (PLA) were determined as 0.42 U/mg, 11 U/mg and 0.067 U/mg, respectively. To obtain a better understanding of how the enzyme recognizes and hydrolyzes PBS/PBSA, we investigated the environment of the catalytic pocket, which is divided into carboxylic acid and alcohol recognition sites. The affinities for different substrates depended on the carbon chain length of the carboxylic acid in the substrate. Competitive inhibition modes were exhibited by carboxylic acids and alcohols that consisted of $ C_{4} $-$ C_{6} $ and $ C_{3} $-$ C_{8} $ chain lengths, respectively. Determination of the affinities for different chemicals indicated that the most preferred substrate for the enzyme would consist of butyric acid and n-hexanol. Succinic Acid (dpeaa)DE-He213 Hexanoic Acid (dpeaa)DE-He213 Biodegradable Plastic (dpeaa)DE-He213 Inhibition Mode (dpeaa)DE-He213 Butylene Succinate (dpeaa)DE-He213 Yamagata, Youhei aut Abe, Keietsu aut Hasegawa, Fumihiko aut Machida, Masayuki aut Ishioka, Ryoji aut Gomi, Katsuya aut Nakajima, Tasuku aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 67(2005), 6 vom: 27. Jan., Seite 778-788 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:67 year:2005 number:6 day:27 month:01 pages:778-788 https://dx.doi.org/10.1007/s00253-004-1853-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 67 2005 6 27 01 778-788 |
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10.1007/s00253-004-1853-6 doi (DE-627)SPR002937492 (SPR)s00253-004-1853-6-e DE-627 ger DE-627 rakwb eng Maeda, Hiroshi verfasserin aut Purification and characterization of a biodegradable plastic-degrading enzyme from Aspergillus oryzae 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2005 Abstract We used biodegradable plastics as fermentation substrates for the filamentous fungus Aspergillus oryzae. This fungus could grow under culture conditions that contained emulsified poly-(butylene succinate) (PBS) and emulsified poly-(butylene succinate-co-adipate) (PBSA) as the sole carbon source, and could digest PBS and PBSA, as indicated by clearing of the culture supernatant. We purified the PBS-degrading enzyme from the culture supernatant, and its molecular mass was determined as 21.6 kDa. The enzyme was identified as cutinase based on internal amino acid sequences. Specific activities against PBS, PBSA and poly-(lactic acid) (PLA) were determined as 0.42 U/mg, 11 U/mg and 0.067 U/mg, respectively. To obtain a better understanding of how the enzyme recognizes and hydrolyzes PBS/PBSA, we investigated the environment of the catalytic pocket, which is divided into carboxylic acid and alcohol recognition sites. The affinities for different substrates depended on the carbon chain length of the carboxylic acid in the substrate. Competitive inhibition modes were exhibited by carboxylic acids and alcohols that consisted of $ C_{4} $-$ C_{6} $ and $ C_{3} $-$ C_{8} $ chain lengths, respectively. Determination of the affinities for different chemicals indicated that the most preferred substrate for the enzyme would consist of butyric acid and n-hexanol. Succinic Acid (dpeaa)DE-He213 Hexanoic Acid (dpeaa)DE-He213 Biodegradable Plastic (dpeaa)DE-He213 Inhibition Mode (dpeaa)DE-He213 Butylene Succinate (dpeaa)DE-He213 Yamagata, Youhei aut Abe, Keietsu aut Hasegawa, Fumihiko aut Machida, Masayuki aut Ishioka, Ryoji aut Gomi, Katsuya aut Nakajima, Tasuku aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 67(2005), 6 vom: 27. Jan., Seite 778-788 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:67 year:2005 number:6 day:27 month:01 pages:778-788 https://dx.doi.org/10.1007/s00253-004-1853-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 67 2005 6 27 01 778-788 |
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10.1007/s00253-004-1853-6 doi (DE-627)SPR002937492 (SPR)s00253-004-1853-6-e DE-627 ger DE-627 rakwb eng Maeda, Hiroshi verfasserin aut Purification and characterization of a biodegradable plastic-degrading enzyme from Aspergillus oryzae 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2005 Abstract We used biodegradable plastics as fermentation substrates for the filamentous fungus Aspergillus oryzae. This fungus could grow under culture conditions that contained emulsified poly-(butylene succinate) (PBS) and emulsified poly-(butylene succinate-co-adipate) (PBSA) as the sole carbon source, and could digest PBS and PBSA, as indicated by clearing of the culture supernatant. We purified the PBS-degrading enzyme from the culture supernatant, and its molecular mass was determined as 21.6 kDa. The enzyme was identified as cutinase based on internal amino acid sequences. Specific activities against PBS, PBSA and poly-(lactic acid) (PLA) were determined as 0.42 U/mg, 11 U/mg and 0.067 U/mg, respectively. To obtain a better understanding of how the enzyme recognizes and hydrolyzes PBS/PBSA, we investigated the environment of the catalytic pocket, which is divided into carboxylic acid and alcohol recognition sites. The affinities for different substrates depended on the carbon chain length of the carboxylic acid in the substrate. Competitive inhibition modes were exhibited by carboxylic acids and alcohols that consisted of $ C_{4} $-$ C_{6} $ and $ C_{3} $-$ C_{8} $ chain lengths, respectively. Determination of the affinities for different chemicals indicated that the most preferred substrate for the enzyme would consist of butyric acid and n-hexanol. Succinic Acid (dpeaa)DE-He213 Hexanoic Acid (dpeaa)DE-He213 Biodegradable Plastic (dpeaa)DE-He213 Inhibition Mode (dpeaa)DE-He213 Butylene Succinate (dpeaa)DE-He213 Yamagata, Youhei aut Abe, Keietsu aut Hasegawa, Fumihiko aut Machida, Masayuki aut Ishioka, Ryoji aut Gomi, Katsuya aut Nakajima, Tasuku aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 67(2005), 6 vom: 27. Jan., Seite 778-788 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:67 year:2005 number:6 day:27 month:01 pages:778-788 https://dx.doi.org/10.1007/s00253-004-1853-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 67 2005 6 27 01 778-788 |
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Enthalten in Applied microbiology and biotechnology 67(2005), 6 vom: 27. Jan., Seite 778-788 volume:67 year:2005 number:6 day:27 month:01 pages:778-788 |
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Enthalten in Applied microbiology and biotechnology 67(2005), 6 vom: 27. Jan., Seite 778-788 volume:67 year:2005 number:6 day:27 month:01 pages:778-788 |
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Succinic Acid Hexanoic Acid Biodegradable Plastic Inhibition Mode Butylene Succinate |
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Applied microbiology and biotechnology |
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Maeda, Hiroshi @@aut@@ Yamagata, Youhei @@aut@@ Abe, Keietsu @@aut@@ Hasegawa, Fumihiko @@aut@@ Machida, Masayuki @@aut@@ Ishioka, Ryoji @@aut@@ Gomi, Katsuya @@aut@@ Nakajima, Tasuku @@aut@@ |
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2005-01-27T00:00:00Z |
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This fungus could grow under culture conditions that contained emulsified poly-(butylene succinate) (PBS) and emulsified poly-(butylene succinate-co-adipate) (PBSA) as the sole carbon source, and could digest PBS and PBSA, as indicated by clearing of the culture supernatant. We purified the PBS-degrading enzyme from the culture supernatant, and its molecular mass was determined as 21.6 kDa. The enzyme was identified as cutinase based on internal amino acid sequences. Specific activities against PBS, PBSA and poly-(lactic acid) (PLA) were determined as 0.42 U/mg, 11 U/mg and 0.067 U/mg, respectively. To obtain a better understanding of how the enzyme recognizes and hydrolyzes PBS/PBSA, we investigated the environment of the catalytic pocket, which is divided into carboxylic acid and alcohol recognition sites. The affinities for different substrates depended on the carbon chain length of the carboxylic acid in the substrate. Competitive inhibition modes were exhibited by carboxylic acids and alcohols that consisted of $ C_{4} $-$ C_{6} $ and $ C_{3} $-$ C_{8} $ chain lengths, respectively. 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|
| author |
Maeda, Hiroshi |
| spellingShingle |
Maeda, Hiroshi misc Succinic Acid misc Hexanoic Acid misc Biodegradable Plastic misc Inhibition Mode misc Butylene Succinate Purification and characterization of a biodegradable plastic-degrading enzyme from Aspergillus oryzae |
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| topic_title |
Purification and characterization of a biodegradable plastic-degrading enzyme from Aspergillus oryzae Succinic Acid (dpeaa)DE-He213 Hexanoic Acid (dpeaa)DE-He213 Biodegradable Plastic (dpeaa)DE-He213 Inhibition Mode (dpeaa)DE-He213 Butylene Succinate (dpeaa)DE-He213 |
| topic |
misc Succinic Acid misc Hexanoic Acid misc Biodegradable Plastic misc Inhibition Mode misc Butylene Succinate |
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misc Succinic Acid misc Hexanoic Acid misc Biodegradable Plastic misc Inhibition Mode misc Butylene Succinate |
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Elektronische Aufsätze Aufsätze Elektronische Ressource |
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Purification and characterization of a biodegradable plastic-degrading enzyme from Aspergillus oryzae |
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| title_full |
Purification and characterization of a biodegradable plastic-degrading enzyme from Aspergillus oryzae |
| author_sort |
Maeda, Hiroshi |
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Applied microbiology and biotechnology |
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Applied microbiology and biotechnology |
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Maeda, Hiroshi Yamagata, Youhei Abe, Keietsu Hasegawa, Fumihiko Machida, Masayuki Ishioka, Ryoji Gomi, Katsuya Nakajima, Tasuku |
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Maeda, Hiroshi |
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10.1007/s00253-004-1853-6 |
| title_sort |
purification and characterization of a biodegradable plastic-degrading enzyme from aspergillus oryzae |
| title_auth |
Purification and characterization of a biodegradable plastic-degrading enzyme from Aspergillus oryzae |
| abstract |
Abstract We used biodegradable plastics as fermentation substrates for the filamentous fungus Aspergillus oryzae. This fungus could grow under culture conditions that contained emulsified poly-(butylene succinate) (PBS) and emulsified poly-(butylene succinate-co-adipate) (PBSA) as the sole carbon source, and could digest PBS and PBSA, as indicated by clearing of the culture supernatant. We purified the PBS-degrading enzyme from the culture supernatant, and its molecular mass was determined as 21.6 kDa. The enzyme was identified as cutinase based on internal amino acid sequences. Specific activities against PBS, PBSA and poly-(lactic acid) (PLA) were determined as 0.42 U/mg, 11 U/mg and 0.067 U/mg, respectively. To obtain a better understanding of how the enzyme recognizes and hydrolyzes PBS/PBSA, we investigated the environment of the catalytic pocket, which is divided into carboxylic acid and alcohol recognition sites. The affinities for different substrates depended on the carbon chain length of the carboxylic acid in the substrate. Competitive inhibition modes were exhibited by carboxylic acids and alcohols that consisted of $ C_{4} $-$ C_{6} $ and $ C_{3} $-$ C_{8} $ chain lengths, respectively. Determination of the affinities for different chemicals indicated that the most preferred substrate for the enzyme would consist of butyric acid and n-hexanol. © Springer-Verlag 2005 |
| abstractGer |
Abstract We used biodegradable plastics as fermentation substrates for the filamentous fungus Aspergillus oryzae. This fungus could grow under culture conditions that contained emulsified poly-(butylene succinate) (PBS) and emulsified poly-(butylene succinate-co-adipate) (PBSA) as the sole carbon source, and could digest PBS and PBSA, as indicated by clearing of the culture supernatant. We purified the PBS-degrading enzyme from the culture supernatant, and its molecular mass was determined as 21.6 kDa. The enzyme was identified as cutinase based on internal amino acid sequences. Specific activities against PBS, PBSA and poly-(lactic acid) (PLA) were determined as 0.42 U/mg, 11 U/mg and 0.067 U/mg, respectively. To obtain a better understanding of how the enzyme recognizes and hydrolyzes PBS/PBSA, we investigated the environment of the catalytic pocket, which is divided into carboxylic acid and alcohol recognition sites. The affinities for different substrates depended on the carbon chain length of the carboxylic acid in the substrate. Competitive inhibition modes were exhibited by carboxylic acids and alcohols that consisted of $ C_{4} $-$ C_{6} $ and $ C_{3} $-$ C_{8} $ chain lengths, respectively. Determination of the affinities for different chemicals indicated that the most preferred substrate for the enzyme would consist of butyric acid and n-hexanol. © Springer-Verlag 2005 |
| abstract_unstemmed |
Abstract We used biodegradable plastics as fermentation substrates for the filamentous fungus Aspergillus oryzae. This fungus could grow under culture conditions that contained emulsified poly-(butylene succinate) (PBS) and emulsified poly-(butylene succinate-co-adipate) (PBSA) as the sole carbon source, and could digest PBS and PBSA, as indicated by clearing of the culture supernatant. We purified the PBS-degrading enzyme from the culture supernatant, and its molecular mass was determined as 21.6 kDa. The enzyme was identified as cutinase based on internal amino acid sequences. Specific activities against PBS, PBSA and poly-(lactic acid) (PLA) were determined as 0.42 U/mg, 11 U/mg and 0.067 U/mg, respectively. To obtain a better understanding of how the enzyme recognizes and hydrolyzes PBS/PBSA, we investigated the environment of the catalytic pocket, which is divided into carboxylic acid and alcohol recognition sites. The affinities for different substrates depended on the carbon chain length of the carboxylic acid in the substrate. Competitive inhibition modes were exhibited by carboxylic acids and alcohols that consisted of $ C_{4} $-$ C_{6} $ and $ C_{3} $-$ C_{8} $ chain lengths, respectively. Determination of the affinities for different chemicals indicated that the most preferred substrate for the enzyme would consist of butyric acid and n-hexanol. © Springer-Verlag 2005 |
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| title_short |
Purification and characterization of a biodegradable plastic-degrading enzyme from Aspergillus oryzae |
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https://dx.doi.org/10.1007/s00253-004-1853-6 |
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Yamagata, Youhei Abe, Keietsu Hasegawa, Fumihiko Machida, Masayuki Ishioka, Ryoji Gomi, Katsuya Nakajima, Tasuku |
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Yamagata, Youhei Abe, Keietsu Hasegawa, Fumihiko Machida, Masayuki Ishioka, Ryoji Gomi, Katsuya Nakajima, Tasuku |
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| doi_str |
10.1007/s00253-004-1853-6 |
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2024-07-03T16:11:34.884Z |
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| score |
7.399351 |