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Preparation and Properties of a Cephalosporin Acetylesterase Adsorbed onto Bentonite
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| Zeitschriftentitel: | Antimicrobial Agents and Chemotherapy |
|---|---|
| Personen und Körperschaften: | , |
| In: | Antimicrobial Agents and Chemotherapy, 8, 1975, 3, S. 282-288 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Society for Microbiology
|
| Schlagwörter: |
| author_facet |
Abbott, Bernard J. Fukuda, D. S. Abbott, Bernard J. Fukuda, D. S. |
|---|---|
| author |
Abbott, Bernard J. Fukuda, D. S. |
| spellingShingle |
Abbott, Bernard J. Fukuda, D. S. Antimicrobial Agents and Chemotherapy Preparation and Properties of a Cephalosporin Acetylesterase Adsorbed onto Bentonite Infectious Diseases Pharmacology (medical) Pharmacology |
| author_sort |
abbott, bernard j. |
| spelling |
Abbott, Bernard J. Fukuda, D. S. 0066-4804 1098-6596 American Society for Microbiology Infectious Diseases Pharmacology (medical) Pharmacology http://dx.doi.org/10.1128/aac.8.3.282 <jats:p> A cephalosporin acetylesterase produced by <jats:italic>Bacillus subtilis</jats:italic> was immobilized by adsorption onto bentonite. The immobilized enzyme (E <jats:sub>I</jats:sub> ) and the soluble enzyme (E <jats:sub>S</jats:sub> ) exhibited Michaelis-Menton kinetics with 7-aminocephalosporanic acid (7-ACA): <jats:italic> K <jats:sub>m</jats:sub> </jats:italic> = 2.8 × 10 <jats:sup>−3</jats:sup> M and <jats:italic> K <jats:sub>m</jats:sub> </jats:italic> = 3.2 × 10 <jats:sup>−3</jats:sup> M, respectively. Similar kinetics were observed with 7-(thiophene-2-acetamido)cephalosporanic acid (cephalothin), but the <jats:italic> K <jats:sub>m</jats:sub> </jats:italic> value measured with E <jats:sub>I</jats:sub> (3.7 × 10 <jats:sup>−3</jats:sup> M) was less than one-half that measured with this substrate and E <jats:sub>S</jats:sub> . The reduction in <jats:italic> K <jats:sub>m</jats:sub> </jats:italic> value was correlated with the ability of bentonite to adsorb cephalothin. The reaction products, acetate and deacetyl-7-ACA, were weak competitive inhibitors of E <jats:sub>S</jats:sub> and E <jats:sub>I</jats:sub> . The <jats:italic> K <jats:sub>i</jats:sub> </jats:italic> values for E <jats:sub>I</jats:sub> were 5.0 × 10 <jats:sup>−2</jats:sup> M for acetate and 3.6 × 10 <jats:sup>−2</jats:sup> M for deacetyl-7-ACA. Similar values were measured with E <jats:sub>S</jats:sub> and these substrates. E <jats:sub>I</jats:sub> retained about 80% of its initial activity after 3 weeks of storage in solution at 25 C. However, the enzyme dissociated from the bentonite particles during the deacetylation reaction. This dissociation was minimized by cross-linking E <jats:sub>I</jats:sub> with glutaraldehyde or bis-dimethyladipimidate, or by adding Al(OH) <jats:sub>3</jats:sub> to the suspension. With the latter addition, E <jats:sub>I</jats:sub> was stabilized so that it could be reused nine times before one-half of the initial activity was lost. </jats:p> Preparation and Properties of a Cephalosporin Acetylesterase Adsorbed onto Bentonite Antimicrobial Agents and Chemotherapy |
| doi_str_mv |
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Medizin Chemie und Pharmazie |
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American Society for Microbiology, 1975 |
| imprint_str_mv |
American Society for Microbiology, 1975 |
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0066-4804 1098-6596 |
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0066-4804 1098-6596 |
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abbott1975preparationandpropertiesofacephalosporinacetylesteraseadsorbedontobentonite |
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1975 |
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American Society for Microbiology |
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ai |
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ai |
| series |
Antimicrobial Agents and Chemotherapy |
| source_id |
49 |
| title |
Preparation and Properties of a Cephalosporin Acetylesterase Adsorbed onto Bentonite |
| title_unstemmed |
Preparation and Properties of a Cephalosporin Acetylesterase Adsorbed onto Bentonite |
| title_full |
Preparation and Properties of a Cephalosporin Acetylesterase Adsorbed onto Bentonite |
| title_fullStr |
Preparation and Properties of a Cephalosporin Acetylesterase Adsorbed onto Bentonite |
| title_full_unstemmed |
Preparation and Properties of a Cephalosporin Acetylesterase Adsorbed onto Bentonite |
| title_short |
Preparation and Properties of a Cephalosporin Acetylesterase Adsorbed onto Bentonite |
| title_sort |
preparation and properties of a cephalosporin acetylesterase adsorbed onto bentonite |
| topic |
Infectious Diseases Pharmacology (medical) Pharmacology |
| url |
http://dx.doi.org/10.1128/aac.8.3.282 |
| publishDate |
1975 |
| physical |
282-288 |
| description |
<jats:p>
A cephalosporin acetylesterase produced by
<jats:italic>Bacillus subtilis</jats:italic>
was immobilized by adsorption onto bentonite. The immobilized enzyme (E
<jats:sub>I</jats:sub>
) and the soluble enzyme (E
<jats:sub>S</jats:sub>
) exhibited Michaelis-Menton kinetics with 7-aminocephalosporanic acid (7-ACA):
<jats:italic>
K
<jats:sub>m</jats:sub>
</jats:italic>
= 2.8 × 10
<jats:sup>−3</jats:sup>
M and
<jats:italic>
K
<jats:sub>m</jats:sub>
</jats:italic>
= 3.2 × 10
<jats:sup>−3</jats:sup>
M, respectively. Similar kinetics were observed with 7-(thiophene-2-acetamido)cephalosporanic acid (cephalothin), but the
<jats:italic>
K
<jats:sub>m</jats:sub>
</jats:italic>
value measured with E
<jats:sub>I</jats:sub>
(3.7 × 10
<jats:sup>−3</jats:sup>
M) was less than one-half that measured with this substrate and E
<jats:sub>S</jats:sub>
. The reduction in
<jats:italic>
K
<jats:sub>m</jats:sub>
</jats:italic>
value was correlated with the ability of bentonite to adsorb cephalothin. The reaction products, acetate and deacetyl-7-ACA, were weak competitive inhibitors of E
<jats:sub>S</jats:sub>
and E
<jats:sub>I</jats:sub>
. The
<jats:italic>
K
<jats:sub>i</jats:sub>
</jats:italic>
values for E
<jats:sub>I</jats:sub>
were 5.0 × 10
<jats:sup>−2</jats:sup>
M for acetate and 3.6 × 10
<jats:sup>−2</jats:sup>
M for deacetyl-7-ACA. Similar values were measured with E
<jats:sub>S</jats:sub>
and these substrates. E
<jats:sub>I</jats:sub>
retained about 80% of its initial activity after 3 weeks of storage in solution at 25 C. However, the enzyme dissociated from the bentonite particles during the deacetylation reaction. This dissociation was minimized by cross-linking E
<jats:sub>I</jats:sub>
with glutaraldehyde or bis-dimethyladipimidate, or by adding Al(OH)
<jats:sub>3</jats:sub>
to the suspension. With the latter addition, E
<jats:sub>I</jats:sub>
was stabilized so that it could be reused nine times before one-half of the initial activity was lost.
</jats:p> |
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| author | Abbott, Bernard J., Fukuda, D. S. |
| author_facet | Abbott, Bernard J., Fukuda, D. S., Abbott, Bernard J., Fukuda, D. S. |
| author_sort | abbott, bernard j. |
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| description | <jats:p> A cephalosporin acetylesterase produced by <jats:italic>Bacillus subtilis</jats:italic> was immobilized by adsorption onto bentonite. The immobilized enzyme (E <jats:sub>I</jats:sub> ) and the soluble enzyme (E <jats:sub>S</jats:sub> ) exhibited Michaelis-Menton kinetics with 7-aminocephalosporanic acid (7-ACA): <jats:italic> K <jats:sub>m</jats:sub> </jats:italic> = 2.8 × 10 <jats:sup>−3</jats:sup> M and <jats:italic> K <jats:sub>m</jats:sub> </jats:italic> = 3.2 × 10 <jats:sup>−3</jats:sup> M, respectively. Similar kinetics were observed with 7-(thiophene-2-acetamido)cephalosporanic acid (cephalothin), but the <jats:italic> K <jats:sub>m</jats:sub> </jats:italic> value measured with E <jats:sub>I</jats:sub> (3.7 × 10 <jats:sup>−3</jats:sup> M) was less than one-half that measured with this substrate and E <jats:sub>S</jats:sub> . The reduction in <jats:italic> K <jats:sub>m</jats:sub> </jats:italic> value was correlated with the ability of bentonite to adsorb cephalothin. The reaction products, acetate and deacetyl-7-ACA, were weak competitive inhibitors of E <jats:sub>S</jats:sub> and E <jats:sub>I</jats:sub> . The <jats:italic> K <jats:sub>i</jats:sub> </jats:italic> values for E <jats:sub>I</jats:sub> were 5.0 × 10 <jats:sup>−2</jats:sup> M for acetate and 3.6 × 10 <jats:sup>−2</jats:sup> M for deacetyl-7-ACA. Similar values were measured with E <jats:sub>S</jats:sub> and these substrates. E <jats:sub>I</jats:sub> retained about 80% of its initial activity after 3 weeks of storage in solution at 25 C. However, the enzyme dissociated from the bentonite particles during the deacetylation reaction. This dissociation was minimized by cross-linking E <jats:sub>I</jats:sub> with glutaraldehyde or bis-dimethyladipimidate, or by adding Al(OH) <jats:sub>3</jats:sub> to the suspension. With the latter addition, E <jats:sub>I</jats:sub> was stabilized so that it could be reused nine times before one-half of the initial activity was lost. </jats:p> |
| doi_str_mv | 10.1128/aac.8.3.282 |
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| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9hYWMuOC4zLjI4Mg |
| imprint | American Society for Microbiology, 1975 |
| imprint_str_mv | American Society for Microbiology, 1975 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229 |
| issn | 0066-4804, 1098-6596 |
| issn_str_mv | 0066-4804, 1098-6596 |
| language | English |
| last_indexed | 2024-03-01T15:05:07.191Z |
| match_str | abbott1975preparationandpropertiesofacephalosporinacetylesteraseadsorbedontobentonite |
| mega_collection | American Society for Microbiology (CrossRef) |
| physical | 282-288 |
| publishDate | 1975 |
| publishDateSort | 1975 |
| publisher | American Society for Microbiology |
| record_format | ai |
| recordtype | ai |
| series | Antimicrobial Agents and Chemotherapy |
| source_id | 49 |
| spelling | Abbott, Bernard J. Fukuda, D. S. 0066-4804 1098-6596 American Society for Microbiology Infectious Diseases Pharmacology (medical) Pharmacology http://dx.doi.org/10.1128/aac.8.3.282 <jats:p> A cephalosporin acetylesterase produced by <jats:italic>Bacillus subtilis</jats:italic> was immobilized by adsorption onto bentonite. The immobilized enzyme (E <jats:sub>I</jats:sub> ) and the soluble enzyme (E <jats:sub>S</jats:sub> ) exhibited Michaelis-Menton kinetics with 7-aminocephalosporanic acid (7-ACA): <jats:italic> K <jats:sub>m</jats:sub> </jats:italic> = 2.8 × 10 <jats:sup>−3</jats:sup> M and <jats:italic> K <jats:sub>m</jats:sub> </jats:italic> = 3.2 × 10 <jats:sup>−3</jats:sup> M, respectively. Similar kinetics were observed with 7-(thiophene-2-acetamido)cephalosporanic acid (cephalothin), but the <jats:italic> K <jats:sub>m</jats:sub> </jats:italic> value measured with E <jats:sub>I</jats:sub> (3.7 × 10 <jats:sup>−3</jats:sup> M) was less than one-half that measured with this substrate and E <jats:sub>S</jats:sub> . The reduction in <jats:italic> K <jats:sub>m</jats:sub> </jats:italic> value was correlated with the ability of bentonite to adsorb cephalothin. The reaction products, acetate and deacetyl-7-ACA, were weak competitive inhibitors of E <jats:sub>S</jats:sub> and E <jats:sub>I</jats:sub> . The <jats:italic> K <jats:sub>i</jats:sub> </jats:italic> values for E <jats:sub>I</jats:sub> were 5.0 × 10 <jats:sup>−2</jats:sup> M for acetate and 3.6 × 10 <jats:sup>−2</jats:sup> M for deacetyl-7-ACA. Similar values were measured with E <jats:sub>S</jats:sub> and these substrates. E <jats:sub>I</jats:sub> retained about 80% of its initial activity after 3 weeks of storage in solution at 25 C. However, the enzyme dissociated from the bentonite particles during the deacetylation reaction. This dissociation was minimized by cross-linking E <jats:sub>I</jats:sub> with glutaraldehyde or bis-dimethyladipimidate, or by adding Al(OH) <jats:sub>3</jats:sub> to the suspension. With the latter addition, E <jats:sub>I</jats:sub> was stabilized so that it could be reused nine times before one-half of the initial activity was lost. </jats:p> Preparation and Properties of a Cephalosporin Acetylesterase Adsorbed onto Bentonite Antimicrobial Agents and Chemotherapy |
| spellingShingle | Abbott, Bernard J., Fukuda, D. S., Antimicrobial Agents and Chemotherapy, Preparation and Properties of a Cephalosporin Acetylesterase Adsorbed onto Bentonite, Infectious Diseases, Pharmacology (medical), Pharmacology |
| title | Preparation and Properties of a Cephalosporin Acetylesterase Adsorbed onto Bentonite |
| title_full | Preparation and Properties of a Cephalosporin Acetylesterase Adsorbed onto Bentonite |
| title_fullStr | Preparation and Properties of a Cephalosporin Acetylesterase Adsorbed onto Bentonite |
| title_full_unstemmed | Preparation and Properties of a Cephalosporin Acetylesterase Adsorbed onto Bentonite |
| title_short | Preparation and Properties of a Cephalosporin Acetylesterase Adsorbed onto Bentonite |
| title_sort | preparation and properties of a cephalosporin acetylesterase adsorbed onto bentonite |
| title_unstemmed | Preparation and Properties of a Cephalosporin Acetylesterase Adsorbed onto Bentonite |
| topic | Infectious Diseases, Pharmacology (medical), Pharmacology |
| url | http://dx.doi.org/10.1128/aac.8.3.282 |