Thermostable alkaline cellulase from an alkaliphilic isolate, Bacillus sp. KSM-S237
Thermostable alkaline cellulase (endo-1,4-beta-glucanase, EC 3.2.1.4) activity was detected in the culture medium of a strictly alkaliphilic strain of Bacillus, designated KSM-S237. This novel enzyme was purified to homogeneity by a two-step column-chromatographic procedure with high yield. The N-te...
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| Veröffentlicht in: | Extremophiles : life under extreme conditions 1997-08, Vol.1 (3), p.151-156 |
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| creator | Hakamada, Y Koike, K Yoshimatsu, T Mori, H Kobayashi, T Ito, S |
| description | Thermostable alkaline cellulase (endo-1,4-beta-glucanase, EC 3.2.1.4) activity was detected in the culture medium of a strictly alkaliphilic strain of Bacillus, designated KSM-S237. This novel enzyme was purified to homogeneity by a two-step column-chromatographic procedure with high yield. The N-terminal amino acid sequence of the purified enzyme was Glu-Gly-Asn-Thr-Arg-Glu-Asp-Asn-Phe-Lys-His-Leu-Leu-Gly-Asn-Asp-Asn-Val- Lys-Arg. The enzyme had a molecular mass of approximately 86 kDa and an isoelectric point of pH 3.8. The enzyme had a pH optimum of 8.6-9.0 and displayed maximum activity at 45 degrees C. The alkaline enzyme was stable up to 50 degrees C and more than 30% of the original activity was detectable after heating at 100 degrees C and at pH 9.0 for 10 min. The enzyme hydrolyzed carboxymethylcellulose, lichenan (beta-1,3;1,4-linkage), and p-nitrophenyl derivatives of cellotriose and cellotetraose. Crystalline forms of cellulose (Avicel and filter paper), H3PO4-swollen cellulose, NaOH-swollen cellulose, curdlan (beta-1,3-linkage), laminarin (beta-1,3;1,6-linkage), and xylan were barely hydrolyzed at all. |
| doi_str_mv | 10.1007/s007920050028 |
| format | Article |
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The alkaline enzyme was stable up to 50 degrees C and more than 30% of the original activity was detectable after heating at 100 degrees C and at pH 9.0 for 10 min. The enzyme hydrolyzed carboxymethylcellulose, lichenan (beta-1,3;1,4-linkage), and p-nitrophenyl derivatives of cellotriose and cellotetraose. Crystalline forms of cellulose (Avicel and filter paper), H3PO4-swollen cellulose, NaOH-swollen cellulose, curdlan (beta-1,3-linkage), laminarin (beta-1,3;1,6-linkage), and xylan were barely hydrolyzed at all.</description><identifier>ISSN: 1431-0651</identifier><identifier>EISSN: 1433-4909</identifier><identifier>DOI: 10.1007/s007920050028</identifier><identifier>PMID: 9680321</identifier><language>eng</language><publisher>Germany</publisher><subject>Amino Acid Sequence ; Bacillus - classification ; Bacillus - enzymology ; Cellulase - chemistry ; Cellulase - isolation & purification ; Cellulase - metabolism ; Enzyme Stability ; Hydrogen-Ion Concentration ; Ions ; Isoelectric Point ; Metals ; Molecular Sequence Data ; Molecular Weight ; Space life sciences ; Substrate Specificity ; Temperature</subject><ispartof>Extremophiles : life under extreme conditions, 1997-08, Vol.1 (3), p.151-156</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c354t-3b4dc05ac8fb20e60e43a1b5810a06c4eee20ef305107c5af2a61b0d49abb2ea3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9680321$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hakamada, Y</creatorcontrib><creatorcontrib>Koike, K</creatorcontrib><creatorcontrib>Yoshimatsu, T</creatorcontrib><creatorcontrib>Mori, H</creatorcontrib><creatorcontrib>Kobayashi, T</creatorcontrib><creatorcontrib>Ito, S</creatorcontrib><title>Thermostable alkaline cellulase from an alkaliphilic isolate, Bacillus sp. KSM-S237</title><title>Extremophiles : life under extreme conditions</title><addtitle>Extremophiles</addtitle><description>Thermostable alkaline cellulase (endo-1,4-beta-glucanase, EC 3.2.1.4) activity was detected in the culture medium of a strictly alkaliphilic strain of Bacillus, designated KSM-S237. This novel enzyme was purified to homogeneity by a two-step column-chromatographic procedure with high yield. The N-terminal amino acid sequence of the purified enzyme was Glu-Gly-Asn-Thr-Arg-Glu-Asp-Asn-Phe-Lys-His-Leu-Leu-Gly-Asn-Asp-Asn-Val- Lys-Arg. The enzyme had a molecular mass of approximately 86 kDa and an isoelectric point of pH 3.8. The enzyme had a pH optimum of 8.6-9.0 and displayed maximum activity at 45 degrees C. The alkaline enzyme was stable up to 50 degrees C and more than 30% of the original activity was detectable after heating at 100 degrees C and at pH 9.0 for 10 min. The enzyme hydrolyzed carboxymethylcellulose, lichenan (beta-1,3;1,4-linkage), and p-nitrophenyl derivatives of cellotriose and cellotetraose. Crystalline forms of cellulose (Avicel and filter paper), H3PO4-swollen cellulose, NaOH-swollen cellulose, curdlan (beta-1,3-linkage), laminarin (beta-1,3;1,6-linkage), and xylan were barely hydrolyzed at all.</description><subject>Amino Acid Sequence</subject><subject>Bacillus - classification</subject><subject>Bacillus - enzymology</subject><subject>Cellulase - chemistry</subject><subject>Cellulase - isolation & purification</subject><subject>Cellulase - metabolism</subject><subject>Enzyme Stability</subject><subject>Hydrogen-Ion Concentration</subject><subject>Ions</subject><subject>Isoelectric Point</subject><subject>Metals</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Space life sciences</subject><subject>Substrate Specificity</subject><subject>Temperature</subject><issn>1431-0651</issn><issn>1433-4909</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkL1PwzAQxS0EKlAYGZE8MZFyjuN8jFDxJYoYWubo7F5Ug9OEOBn473FphMRyd7r309PTY-xCwEwAZDc-jCIGUABxfsBORCJllBRQHP7eIoJUiWN26v0HgFBBmLBJkeYgY3HClqsNdXXje9SOOLpPdHZL3JBzg0NPvOqamuN2lNqNddZw6xuHPV3zOzQ2kJ77dsZflq_RMpbZGTuq0Hk6H_eUvT_cr-ZP0eLt8Xl-u4iMVEkfSZ2sDSg0eaVjoBQokSi0ygUgpCYhovCuJCgBmVFYxZgKDeukQK1jQjllV3vftmu-BvJ9WVu_S45bagZfZkUqQhwVwGgPmq7xvqOqbDtbY_ddCih3JZb_Sgz85Wg86JrWf_TYmvwBmAJryg</recordid><startdate>19970801</startdate><enddate>19970801</enddate><creator>Hakamada, Y</creator><creator>Koike, K</creator><creator>Yoshimatsu, T</creator><creator>Mori, H</creator><creator>Kobayashi, T</creator><creator>Ito, S</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19970801</creationdate><title>Thermostable alkaline cellulase from an alkaliphilic isolate, Bacillus sp. 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KSM-S237</atitle><jtitle>Extremophiles : life under extreme conditions</jtitle><addtitle>Extremophiles</addtitle><date>1997-08-01</date><risdate>1997</risdate><volume>1</volume><issue>3</issue><spage>151</spage><epage>156</epage><pages>151-156</pages><issn>1431-0651</issn><eissn>1433-4909</eissn><abstract>Thermostable alkaline cellulase (endo-1,4-beta-glucanase, EC 3.2.1.4) activity was detected in the culture medium of a strictly alkaliphilic strain of Bacillus, designated KSM-S237. This novel enzyme was purified to homogeneity by a two-step column-chromatographic procedure with high yield. The N-terminal amino acid sequence of the purified enzyme was Glu-Gly-Asn-Thr-Arg-Glu-Asp-Asn-Phe-Lys-His-Leu-Leu-Gly-Asn-Asp-Asn-Val- Lys-Arg. The enzyme had a molecular mass of approximately 86 kDa and an isoelectric point of pH 3.8. The enzyme had a pH optimum of 8.6-9.0 and displayed maximum activity at 45 degrees C. 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| ispartof | Extremophiles : life under extreme conditions, 1997-08, Vol.1 (3), p.151-156 |
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| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Amino Acid Sequence Bacillus - classification Bacillus - enzymology Cellulase - chemistry Cellulase - isolation & purification Cellulase - metabolism Enzyme Stability Hydrogen-Ion Concentration Ions Isoelectric Point Metals Molecular Sequence Data Molecular Weight Space life sciences Substrate Specificity Temperature |
| title | Thermostable alkaline cellulase from an alkaliphilic isolate, Bacillus sp. KSM-S237 |
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