New immobilization method for enzyme stabilization involving a mesoporous material and an organic/inorganic hybrid gel
Abstract Horseradish peroxidase (HRP) was immobilized in a mesoporous material (folded sheets mesoporous materials, FSM-16) and then entrapped in organic/inorganic hybrid gel comprising various molar ratios of dimethyldimethoxysilane (DMDMOS)/tetramethoxysilane (TMOS). When pore size of FSM-16 mater...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
2000 |
|---|
| Umfang: |
6 |
|---|
| Reproduktion: |
Springer Online Journal Archives 1860-2002 |
|---|---|
| Übergeordnetes Werk: |
in: Biotechnology letters - 1979, 22(2000) vom: Winter, Seite 1953-1958 |
| Übergeordnetes Werk: |
volume:22 ; year:2000 ; month:24 ; pages:1953-1958 ; extent:6 |
| Links: |
|---|
| Katalog-ID: |
NLEJ193174928 |
|---|
| LEADER | 01000caa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLEJ193174928 | ||
| 003 | DE-627 | ||
| 005 | 20230506153058.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 070526s2000 xx |||||o 00| ||eng c | ||
| 035 | |a (DE-627)NLEJ193174928 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 245 | 1 | 0 | |a New immobilization method for enzyme stabilization involving a mesoporous material and an organic/inorganic hybrid gel |
| 264 | 1 | |c 2000 | |
| 300 | |a 6 | ||
| 336 | |a nicht spezifiziert |b zzz |2 rdacontent | ||
| 337 | |a nicht spezifiziert |b z |2 rdamedia | ||
| 338 | |a nicht spezifiziert |b zu |2 rdacarrier | ||
| 520 | |a Abstract Horseradish peroxidase (HRP) was immobilized in a mesoporous material (folded sheets mesoporous materials, FSM-16) and then entrapped in organic/inorganic hybrid gel comprising various molar ratios of dimethyldimethoxysilane (DMDMOS)/tetramethoxysilane (TMOS). When pore size of FSM-16 materials is much larger than the diameters of horseradish peroxidase (HRP), the residual enzymatic activity after thermal treatment (70 °C, 60 min) increased from 73 to 99%, and the oxidative conversion yield of 1,2-diaminobenzene in an organic solvent increased from 59 to 79% after 4 h and the level of leakage of immobilized HRP decreased from 6 to 1.5% on washing by secondary hybrid gel entrapment comprising a molar ratio of DMDMOS/TMOS=1:3. When pore size of FSM-16 materials just matches the diameter of the enzyme, the conversion yield in an organic solvent and the level of leakage of immobilized HRP did not change so much. | ||
| 533 | |f Springer Online Journal Archives 1860-2002 | ||
| 700 | 1 | |a Li, Bo |4 oth | |
| 700 | 1 | |a Takahashi, Haruo |4 oth | |
| 773 | 0 | 8 | |i in |t Biotechnology letters |d 1979 |g 22(2000) vom: Winter, Seite 1953-1958 |w (DE-627)NLEJ188984178 |w (DE-600)2012203-2 |x 1573-6776 |7 nnns |
| 773 | 1 | 8 | |g volume:22 |g year:2000 |g month:24 |g pages:1953-1958 |g extent:6 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1023/A:1026702025928 |
| 912 | |a GBV_USEFLAG_U | ||
| 912 | |a ZDB-1-SOJ | ||
| 912 | |a GBV_NL_ARTICLE | ||
| 951 | |a AR | ||
| 952 | |d 22 |j 2000 |c 24 |h 1953-1958 |g 6 | ||
| matchkey_str |
article:15736776:2000----::eimblztomtofrnyetblztoivligmsprumtraa |
|---|---|
| hierarchy_sort_str |
2000 |
| publishDate |
2000 |
| allfields |
(DE-627)NLEJ193174928 DE-627 ger DE-627 rakwb eng New immobilization method for enzyme stabilization involving a mesoporous material and an organic/inorganic hybrid gel 2000 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract Horseradish peroxidase (HRP) was immobilized in a mesoporous material (folded sheets mesoporous materials, FSM-16) and then entrapped in organic/inorganic hybrid gel comprising various molar ratios of dimethyldimethoxysilane (DMDMOS)/tetramethoxysilane (TMOS). When pore size of FSM-16 materials is much larger than the diameters of horseradish peroxidase (HRP), the residual enzymatic activity after thermal treatment (70 °C, 60 min) increased from 73 to 99%, and the oxidative conversion yield of 1,2-diaminobenzene in an organic solvent increased from 59 to 79% after 4 h and the level of leakage of immobilized HRP decreased from 6 to 1.5% on washing by secondary hybrid gel entrapment comprising a molar ratio of DMDMOS/TMOS=1:3. When pore size of FSM-16 materials just matches the diameter of the enzyme, the conversion yield in an organic solvent and the level of leakage of immobilized HRP did not change so much. Springer Online Journal Archives 1860-2002 Li, Bo oth Takahashi, Haruo oth in Biotechnology letters 1979 22(2000) vom: Winter, Seite 1953-1958 (DE-627)NLEJ188984178 (DE-600)2012203-2 1573-6776 nnns volume:22 year:2000 month:24 pages:1953-1958 extent:6 http://dx.doi.org/10.1023/A:1026702025928 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 22 2000 24 1953-1958 6 |
| spelling |
(DE-627)NLEJ193174928 DE-627 ger DE-627 rakwb eng New immobilization method for enzyme stabilization involving a mesoporous material and an organic/inorganic hybrid gel 2000 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract Horseradish peroxidase (HRP) was immobilized in a mesoporous material (folded sheets mesoporous materials, FSM-16) and then entrapped in organic/inorganic hybrid gel comprising various molar ratios of dimethyldimethoxysilane (DMDMOS)/tetramethoxysilane (TMOS). When pore size of FSM-16 materials is much larger than the diameters of horseradish peroxidase (HRP), the residual enzymatic activity after thermal treatment (70 °C, 60 min) increased from 73 to 99%, and the oxidative conversion yield of 1,2-diaminobenzene in an organic solvent increased from 59 to 79% after 4 h and the level of leakage of immobilized HRP decreased from 6 to 1.5% on washing by secondary hybrid gel entrapment comprising a molar ratio of DMDMOS/TMOS=1:3. When pore size of FSM-16 materials just matches the diameter of the enzyme, the conversion yield in an organic solvent and the level of leakage of immobilized HRP did not change so much. Springer Online Journal Archives 1860-2002 Li, Bo oth Takahashi, Haruo oth in Biotechnology letters 1979 22(2000) vom: Winter, Seite 1953-1958 (DE-627)NLEJ188984178 (DE-600)2012203-2 1573-6776 nnns volume:22 year:2000 month:24 pages:1953-1958 extent:6 http://dx.doi.org/10.1023/A:1026702025928 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 22 2000 24 1953-1958 6 |
| allfields_unstemmed |
(DE-627)NLEJ193174928 DE-627 ger DE-627 rakwb eng New immobilization method for enzyme stabilization involving a mesoporous material and an organic/inorganic hybrid gel 2000 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract Horseradish peroxidase (HRP) was immobilized in a mesoporous material (folded sheets mesoporous materials, FSM-16) and then entrapped in organic/inorganic hybrid gel comprising various molar ratios of dimethyldimethoxysilane (DMDMOS)/tetramethoxysilane (TMOS). When pore size of FSM-16 materials is much larger than the diameters of horseradish peroxidase (HRP), the residual enzymatic activity after thermal treatment (70 °C, 60 min) increased from 73 to 99%, and the oxidative conversion yield of 1,2-diaminobenzene in an organic solvent increased from 59 to 79% after 4 h and the level of leakage of immobilized HRP decreased from 6 to 1.5% on washing by secondary hybrid gel entrapment comprising a molar ratio of DMDMOS/TMOS=1:3. When pore size of FSM-16 materials just matches the diameter of the enzyme, the conversion yield in an organic solvent and the level of leakage of immobilized HRP did not change so much. Springer Online Journal Archives 1860-2002 Li, Bo oth Takahashi, Haruo oth in Biotechnology letters 1979 22(2000) vom: Winter, Seite 1953-1958 (DE-627)NLEJ188984178 (DE-600)2012203-2 1573-6776 nnns volume:22 year:2000 month:24 pages:1953-1958 extent:6 http://dx.doi.org/10.1023/A:1026702025928 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 22 2000 24 1953-1958 6 |
| allfieldsGer |
(DE-627)NLEJ193174928 DE-627 ger DE-627 rakwb eng New immobilization method for enzyme stabilization involving a mesoporous material and an organic/inorganic hybrid gel 2000 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract Horseradish peroxidase (HRP) was immobilized in a mesoporous material (folded sheets mesoporous materials, FSM-16) and then entrapped in organic/inorganic hybrid gel comprising various molar ratios of dimethyldimethoxysilane (DMDMOS)/tetramethoxysilane (TMOS). When pore size of FSM-16 materials is much larger than the diameters of horseradish peroxidase (HRP), the residual enzymatic activity after thermal treatment (70 °C, 60 min) increased from 73 to 99%, and the oxidative conversion yield of 1,2-diaminobenzene in an organic solvent increased from 59 to 79% after 4 h and the level of leakage of immobilized HRP decreased from 6 to 1.5% on washing by secondary hybrid gel entrapment comprising a molar ratio of DMDMOS/TMOS=1:3. When pore size of FSM-16 materials just matches the diameter of the enzyme, the conversion yield in an organic solvent and the level of leakage of immobilized HRP did not change so much. Springer Online Journal Archives 1860-2002 Li, Bo oth Takahashi, Haruo oth in Biotechnology letters 1979 22(2000) vom: Winter, Seite 1953-1958 (DE-627)NLEJ188984178 (DE-600)2012203-2 1573-6776 nnns volume:22 year:2000 month:24 pages:1953-1958 extent:6 http://dx.doi.org/10.1023/A:1026702025928 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 22 2000 24 1953-1958 6 |
| allfieldsSound |
(DE-627)NLEJ193174928 DE-627 ger DE-627 rakwb eng New immobilization method for enzyme stabilization involving a mesoporous material and an organic/inorganic hybrid gel 2000 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract Horseradish peroxidase (HRP) was immobilized in a mesoporous material (folded sheets mesoporous materials, FSM-16) and then entrapped in organic/inorganic hybrid gel comprising various molar ratios of dimethyldimethoxysilane (DMDMOS)/tetramethoxysilane (TMOS). When pore size of FSM-16 materials is much larger than the diameters of horseradish peroxidase (HRP), the residual enzymatic activity after thermal treatment (70 °C, 60 min) increased from 73 to 99%, and the oxidative conversion yield of 1,2-diaminobenzene in an organic solvent increased from 59 to 79% after 4 h and the level of leakage of immobilized HRP decreased from 6 to 1.5% on washing by secondary hybrid gel entrapment comprising a molar ratio of DMDMOS/TMOS=1:3. When pore size of FSM-16 materials just matches the diameter of the enzyme, the conversion yield in an organic solvent and the level of leakage of immobilized HRP did not change so much. Springer Online Journal Archives 1860-2002 Li, Bo oth Takahashi, Haruo oth in Biotechnology letters 1979 22(2000) vom: Winter, Seite 1953-1958 (DE-627)NLEJ188984178 (DE-600)2012203-2 1573-6776 nnns volume:22 year:2000 month:24 pages:1953-1958 extent:6 http://dx.doi.org/10.1023/A:1026702025928 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 22 2000 24 1953-1958 6 |
| language |
English |
| source |
in Biotechnology letters 22(2000) vom: Winter, Seite 1953-1958 volume:22 year:2000 month:24 pages:1953-1958 extent:6 |
| sourceStr |
in Biotechnology letters 22(2000) vom: Winter, Seite 1953-1958 volume:22 year:2000 month:24 pages:1953-1958 extent:6 |
| format_phy_str_mv |
Article |
| institution |
findex.gbv.de |
| isfreeaccess_bool |
false |
| container_title |
Biotechnology letters |
| authorswithroles_txt_mv |
Li, Bo @@oth@@ Takahashi, Haruo @@oth@@ |
| publishDateDaySort_date |
2000-01-01T00:00:00Z |
| hierarchy_top_id |
NLEJ188984178 |
| id |
NLEJ193174928 |
| language_de |
englisch |
| fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ193174928</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230506153058.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070526s2000 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ193174928</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">New immobilization method for enzyme stabilization involving a mesoporous material and an organic/inorganic hybrid gel</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2000</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">6</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Horseradish peroxidase (HRP) was immobilized in a mesoporous material (folded sheets mesoporous materials, FSM-16) and then entrapped in organic/inorganic hybrid gel comprising various molar ratios of dimethyldimethoxysilane (DMDMOS)/tetramethoxysilane (TMOS). When pore size of FSM-16 materials is much larger than the diameters of horseradish peroxidase (HRP), the residual enzymatic activity after thermal treatment (70 °C, 60 min) increased from 73 to 99%, and the oxidative conversion yield of 1,2-diaminobenzene in an organic solvent increased from 59 to 79% after 4 h and the level of leakage of immobilized HRP decreased from 6 to 1.5% on washing by secondary hybrid gel entrapment comprising a molar ratio of DMDMOS/TMOS=1:3. When pore size of FSM-16 materials just matches the diameter of the enzyme, the conversion yield in an organic solvent and the level of leakage of immobilized HRP did not change so much.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Springer Online Journal Archives 1860-2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Li, Bo</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Takahashi, Haruo</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Biotechnology letters</subfield><subfield code="d">1979</subfield><subfield code="g">22(2000) vom: Winter, Seite 1953-1958</subfield><subfield code="w">(DE-627)NLEJ188984178</subfield><subfield code="w">(DE-600)2012203-2</subfield><subfield code="x">1573-6776</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:22</subfield><subfield code="g">year:2000</subfield><subfield code="g">month:24</subfield><subfield code="g">pages:1953-1958</subfield><subfield code="g">extent:6</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1023/A:1026702025928</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SOJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">22</subfield><subfield code="j">2000</subfield><subfield code="c">24</subfield><subfield code="h">1953-1958</subfield><subfield code="g">6</subfield></datafield></record></collection>
|
| series2 |
Springer Online Journal Archives 1860-2002 |
| ppnlink_with_tag_str_mv |
@@773@@(DE-627)NLEJ188984178 |
| format |
electronic Article |
| delete_txt_mv |
keep |
| collection |
NL |
| remote_str |
true |
| illustrated |
Not Illustrated |
| issn |
1573-6776 |
| topic_title |
New immobilization method for enzyme stabilization involving a mesoporous material and an organic/inorganic hybrid gel |
| format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
| format_main_str_mv |
Text Zeitschrift/Artikel |
| carriertype_str_mv |
zu |
| author2_variant |
b l bl h t ht |
| hierarchy_parent_title |
Biotechnology letters |
| hierarchy_parent_id |
NLEJ188984178 |
| hierarchy_top_title |
Biotechnology letters |
| isfreeaccess_txt |
false |
| familylinks_str_mv |
(DE-627)NLEJ188984178 (DE-600)2012203-2 |
| title |
New immobilization method for enzyme stabilization involving a mesoporous material and an organic/inorganic hybrid gel |
| spellingShingle |
New immobilization method for enzyme stabilization involving a mesoporous material and an organic/inorganic hybrid gel |
| ctrlnum |
(DE-627)NLEJ193174928 |
| title_full |
New immobilization method for enzyme stabilization involving a mesoporous material and an organic/inorganic hybrid gel |
| journal |
Biotechnology letters |
| journalStr |
Biotechnology letters |
| lang_code |
eng |
| isOA_bool |
false |
| recordtype |
marc |
| publishDateSort |
2000 |
| contenttype_str_mv |
zzz |
| container_start_page |
1953 |
| container_volume |
22 |
| physical |
6 |
| format_se |
Elektronische Aufsätze |
| title_sort |
new immobilization method for enzyme stabilization involving a mesoporous material and an organic/inorganic hybrid gel |
| title_auth |
New immobilization method for enzyme stabilization involving a mesoporous material and an organic/inorganic hybrid gel |
| abstract |
Abstract Horseradish peroxidase (HRP) was immobilized in a mesoporous material (folded sheets mesoporous materials, FSM-16) and then entrapped in organic/inorganic hybrid gel comprising various molar ratios of dimethyldimethoxysilane (DMDMOS)/tetramethoxysilane (TMOS). When pore size of FSM-16 materials is much larger than the diameters of horseradish peroxidase (HRP), the residual enzymatic activity after thermal treatment (70 °C, 60 min) increased from 73 to 99%, and the oxidative conversion yield of 1,2-diaminobenzene in an organic solvent increased from 59 to 79% after 4 h and the level of leakage of immobilized HRP decreased from 6 to 1.5% on washing by secondary hybrid gel entrapment comprising a molar ratio of DMDMOS/TMOS=1:3. When pore size of FSM-16 materials just matches the diameter of the enzyme, the conversion yield in an organic solvent and the level of leakage of immobilized HRP did not change so much. |
| abstractGer |
Abstract Horseradish peroxidase (HRP) was immobilized in a mesoporous material (folded sheets mesoporous materials, FSM-16) and then entrapped in organic/inorganic hybrid gel comprising various molar ratios of dimethyldimethoxysilane (DMDMOS)/tetramethoxysilane (TMOS). When pore size of FSM-16 materials is much larger than the diameters of horseradish peroxidase (HRP), the residual enzymatic activity after thermal treatment (70 °C, 60 min) increased from 73 to 99%, and the oxidative conversion yield of 1,2-diaminobenzene in an organic solvent increased from 59 to 79% after 4 h and the level of leakage of immobilized HRP decreased from 6 to 1.5% on washing by secondary hybrid gel entrapment comprising a molar ratio of DMDMOS/TMOS=1:3. When pore size of FSM-16 materials just matches the diameter of the enzyme, the conversion yield in an organic solvent and the level of leakage of immobilized HRP did not change so much. |
| abstract_unstemmed |
Abstract Horseradish peroxidase (HRP) was immobilized in a mesoporous material (folded sheets mesoporous materials, FSM-16) and then entrapped in organic/inorganic hybrid gel comprising various molar ratios of dimethyldimethoxysilane (DMDMOS)/tetramethoxysilane (TMOS). When pore size of FSM-16 materials is much larger than the diameters of horseradish peroxidase (HRP), the residual enzymatic activity after thermal treatment (70 °C, 60 min) increased from 73 to 99%, and the oxidative conversion yield of 1,2-diaminobenzene in an organic solvent increased from 59 to 79% after 4 h and the level of leakage of immobilized HRP decreased from 6 to 1.5% on washing by secondary hybrid gel entrapment comprising a molar ratio of DMDMOS/TMOS=1:3. When pore size of FSM-16 materials just matches the diameter of the enzyme, the conversion yield in an organic solvent and the level of leakage of immobilized HRP did not change so much. |
| collection_details |
GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE |
| title_short |
New immobilization method for enzyme stabilization involving a mesoporous material and an organic/inorganic hybrid gel |
| url |
http://dx.doi.org/10.1023/A:1026702025928 |
| remote_bool |
true |
| author2 |
Li, Bo Takahashi, Haruo |
| author2Str |
Li, Bo Takahashi, Haruo |
| ppnlink |
NLEJ188984178 |
| mediatype_str_mv |
z |
| isOA_txt |
false |
| hochschulschrift_bool |
false |
| author2_role |
oth oth |
| up_date |
2024-07-06T10:10:01.673Z |
| _version_ |
1803823980660916224 |
| fullrecord_marcxml |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ193174928</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230506153058.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070526s2000 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ193174928</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">New immobilization method for enzyme stabilization involving a mesoporous material and an organic/inorganic hybrid gel</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2000</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">6</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Horseradish peroxidase (HRP) was immobilized in a mesoporous material (folded sheets mesoporous materials, FSM-16) and then entrapped in organic/inorganic hybrid gel comprising various molar ratios of dimethyldimethoxysilane (DMDMOS)/tetramethoxysilane (TMOS). When pore size of FSM-16 materials is much larger than the diameters of horseradish peroxidase (HRP), the residual enzymatic activity after thermal treatment (70 °C, 60 min) increased from 73 to 99%, and the oxidative conversion yield of 1,2-diaminobenzene in an organic solvent increased from 59 to 79% after 4 h and the level of leakage of immobilized HRP decreased from 6 to 1.5% on washing by secondary hybrid gel entrapment comprising a molar ratio of DMDMOS/TMOS=1:3. When pore size of FSM-16 materials just matches the diameter of the enzyme, the conversion yield in an organic solvent and the level of leakage of immobilized HRP did not change so much.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Springer Online Journal Archives 1860-2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Li, Bo</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Takahashi, Haruo</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Biotechnology letters</subfield><subfield code="d">1979</subfield><subfield code="g">22(2000) vom: Winter, Seite 1953-1958</subfield><subfield code="w">(DE-627)NLEJ188984178</subfield><subfield code="w">(DE-600)2012203-2</subfield><subfield code="x">1573-6776</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:22</subfield><subfield code="g">year:2000</subfield><subfield code="g">month:24</subfield><subfield code="g">pages:1953-1958</subfield><subfield code="g">extent:6</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1023/A:1026702025928</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SOJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">22</subfield><subfield code="j">2000</subfield><subfield code="c">24</subfield><subfield code="h">1953-1958</subfield><subfield code="g">6</subfield></datafield></record></collection>
|
| score |
7.4012136 |