Purification and properties of a thermostable phytase from Bacillus sp. DS11
Bacillus species producing a thermostable phytase was isolated from the soil of a Korean cattle shed. An extracellular phytase from Bacillus sp. DS11 was purified to homogeneity by acetone precipitation and Phenyl-Sepharose, Resource S, and Superose 12 column chromatographies. Its molecular weight w...
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| Veröffentlicht in: | Enzyme and microbial technology 1998, Vol.22 (1), p.2-7 |
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| creator | Kim, Young-Ok Kim, Hyung-Kwoun Bae, Kyung-Sook Yu, Ju-Hyun Oh, Tae-Kwang |
| description | Bacillus species producing a thermostable phytase was isolated from the soil of a Korean cattle shed. An extracellular phytase from
Bacillus sp. DS11 was purified to homogeneity by acetone precipitation and Phenyl-Sepharose, Resource S, and Superose 12 column chromatographies. Its molecular weight was estimated to be 44 kDa by SDS-polyacrylamide gel electrophoresis. Its optimum temperature for phytase activity was 70°C and about 50% of its original activity remained after incubation at 90°C for 10 min in the presence of 5 m
m CaCl
2. Calcium ions were required for thermal stability. The optimum pH for enzyme activity was 7.0 and fairly stable from pH 4.0–8.0. The enzyme had an isoelectric point of 5.3. The
K
m value for phytate was 0.55 m
m. Its activity was greatly inhibited by EDTA and metal ions such as Cd
2+ and Mn
2+. As for substrate specificity, it was very specific for phytate and had little or no activity on other phosphate esters. The enzyme efficiently hydrolyzed phytate in rice flour. |
| doi_str_mv | 10.1016/S0141-0229(97)00096-3 |
| format | Article |
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Bacillus sp. DS11 was purified to homogeneity by acetone precipitation and Phenyl-Sepharose, Resource S, and Superose 12 column chromatographies. Its molecular weight was estimated to be 44 kDa by SDS-polyacrylamide gel electrophoresis. Its optimum temperature for phytase activity was 70°C and about 50% of its original activity remained after incubation at 90°C for 10 min in the presence of 5 m
m CaCl
2. Calcium ions were required for thermal stability. The optimum pH for enzyme activity was 7.0 and fairly stable from pH 4.0–8.0. The enzyme had an isoelectric point of 5.3. The
K
m value for phytate was 0.55 m
m. Its activity was greatly inhibited by EDTA and metal ions such as Cd
2+ and Mn
2+. As for substrate specificity, it was very specific for phytate and had little or no activity on other phosphate esters. The enzyme efficiently hydrolyzed phytate in rice flour.</description><identifier>ISSN: 0141-0229</identifier><identifier>EISSN: 1879-0909</identifier><identifier>DOI: 10.1016/S0141-0229(97)00096-3</identifier><identifier>CODEN: EMTED2</identifier><language>eng</language><publisher>Amsterdam: Elsevier Inc</publisher><subject>Acetone ; Bacillus sp ; Bacteria ; Biological and medical sciences ; Biotechnology ; Column chromatography ; Enzyme engineering ; Fundamental and applied biological sciences. Psychology ; Improved methods for extraction and purification of enzymes ; Methods. Procedures. Technologies ; Phytase ; phytate ; Precipitation (chemical) ; Purification ; Thermodynamic stability ; thermostable enzyme</subject><ispartof>Enzyme and microbial technology, 1998, Vol.22 (1), p.2-7</ispartof><rights>1998</rights><rights>1998 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c433t-15be3ab57c7bd0804a6ddfe5149cc1315a258be3d2c7ce0c0c846f62a9bbf5b13</citedby><cites>FETCH-LOGICAL-c433t-15be3ab57c7bd0804a6ddfe5149cc1315a258be3d2c7ce0c0c846f62a9bbf5b13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0141022997000963$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,4010,27900,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2094531$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Kim, Young-Ok</creatorcontrib><creatorcontrib>Kim, Hyung-Kwoun</creatorcontrib><creatorcontrib>Bae, Kyung-Sook</creatorcontrib><creatorcontrib>Yu, Ju-Hyun</creatorcontrib><creatorcontrib>Oh, Tae-Kwang</creatorcontrib><title>Purification and properties of a thermostable phytase from Bacillus sp. DS11</title><title>Enzyme and microbial technology</title><description>Bacillus species producing a thermostable phytase was isolated from the soil of a Korean cattle shed. An extracellular phytase from
Bacillus sp. DS11 was purified to homogeneity by acetone precipitation and Phenyl-Sepharose, Resource S, and Superose 12 column chromatographies. Its molecular weight was estimated to be 44 kDa by SDS-polyacrylamide gel electrophoresis. Its optimum temperature for phytase activity was 70°C and about 50% of its original activity remained after incubation at 90°C for 10 min in the presence of 5 m
m CaCl
2. Calcium ions were required for thermal stability. The optimum pH for enzyme activity was 7.0 and fairly stable from pH 4.0–8.0. The enzyme had an isoelectric point of 5.3. The
K
m value for phytate was 0.55 m
m. Its activity was greatly inhibited by EDTA and metal ions such as Cd
2+ and Mn
2+. As for substrate specificity, it was very specific for phytate and had little or no activity on other phosphate esters. The enzyme efficiently hydrolyzed phytate in rice flour.</description><subject>Acetone</subject><subject>Bacillus sp</subject><subject>Bacteria</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Column chromatography</subject><subject>Enzyme engineering</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Improved methods for extraction and purification of enzymes</subject><subject>Methods. Procedures. Technologies</subject><subject>Phytase</subject><subject>phytate</subject><subject>Precipitation (chemical)</subject><subject>Purification</subject><subject>Thermodynamic stability</subject><subject>thermostable enzyme</subject><issn>0141-0229</issn><issn>1879-0909</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><recordid>eNqFkE1r3DAQhkVpoNs0P6GgQwjpwdsZS_7QqSSbjxYWEkh7FvJ4RFS8tit5C_n38e6GveY0l2fmfecR4ivCEgHL70-AGjPIc3Npqm8AYMpMfRALrCuTgQHzUSyOyCfxOaW_M4Raw0KsH7cx-EBuCkMvXd_KMQ4jxylwkoOXTk7PHDdDmlzTsRyfXyaXWPo4bOS1o9B12yTTuJQ3T4hfxIl3XeKzt3kq_tzd_l79zNYP979WV-uMtFJThkXDyjVFRVXTQg3alW3ruUBtiFBh4fKinpE2p4oYCKjWpS9zZ5rGFw2qU3FxuDt3_bflNNlNSMRd53oetsnmqABq1DNYHECKQ0qRvR1j2Lj4YhHszp3du7M7MdZUdu_Oqnnv_C3AJXKdj66nkI7LORhdqF2PHweM52f_B442UeCeuA2RabLtEN4JegVDxYLe</recordid><startdate>1998</startdate><enddate>1998</enddate><creator>Kim, Young-Ok</creator><creator>Kim, Hyung-Kwoun</creator><creator>Bae, Kyung-Sook</creator><creator>Yu, Ju-Hyun</creator><creator>Oh, Tae-Kwang</creator><general>Elsevier Inc</general><general>Elsevier Science</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>1998</creationdate><title>Purification and properties of a thermostable phytase from Bacillus sp. DS11</title><author>Kim, Young-Ok ; Kim, Hyung-Kwoun ; Bae, Kyung-Sook ; Yu, Ju-Hyun ; Oh, Tae-Kwang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c433t-15be3ab57c7bd0804a6ddfe5149cc1315a258be3d2c7ce0c0c846f62a9bbf5b13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Acetone</topic><topic>Bacillus sp</topic><topic>Bacteria</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Column chromatography</topic><topic>Enzyme engineering</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Improved methods for extraction and purification of enzymes</topic><topic>Methods. Procedures. Technologies</topic><topic>Phytase</topic><topic>phytate</topic><topic>Precipitation (chemical)</topic><topic>Purification</topic><topic>Thermodynamic stability</topic><topic>thermostable enzyme</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kim, Young-Ok</creatorcontrib><creatorcontrib>Kim, Hyung-Kwoun</creatorcontrib><creatorcontrib>Bae, Kyung-Sook</creatorcontrib><creatorcontrib>Yu, Ju-Hyun</creatorcontrib><creatorcontrib>Oh, Tae-Kwang</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><jtitle>Enzyme and microbial technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kim, Young-Ok</au><au>Kim, Hyung-Kwoun</au><au>Bae, Kyung-Sook</au><au>Yu, Ju-Hyun</au><au>Oh, Tae-Kwang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and properties of a thermostable phytase from Bacillus sp. DS11</atitle><jtitle>Enzyme and microbial technology</jtitle><date>1998</date><risdate>1998</risdate><volume>22</volume><issue>1</issue><spage>2</spage><epage>7</epage><pages>2-7</pages><issn>0141-0229</issn><eissn>1879-0909</eissn><coden>EMTED2</coden><abstract>Bacillus species producing a thermostable phytase was isolated from the soil of a Korean cattle shed. An extracellular phytase from
Bacillus sp. DS11 was purified to homogeneity by acetone precipitation and Phenyl-Sepharose, Resource S, and Superose 12 column chromatographies. Its molecular weight was estimated to be 44 kDa by SDS-polyacrylamide gel electrophoresis. Its optimum temperature for phytase activity was 70°C and about 50% of its original activity remained after incubation at 90°C for 10 min in the presence of 5 m
m CaCl
2. Calcium ions were required for thermal stability. The optimum pH for enzyme activity was 7.0 and fairly stable from pH 4.0–8.0. The enzyme had an isoelectric point of 5.3. The
K
m value for phytate was 0.55 m
m. Its activity was greatly inhibited by EDTA and metal ions such as Cd
2+ and Mn
2+. As for substrate specificity, it was very specific for phytate and had little or no activity on other phosphate esters. The enzyme efficiently hydrolyzed phytate in rice flour.</abstract><cop>Amsterdam</cop><pub>Elsevier Inc</pub><doi>10.1016/S0141-0229(97)00096-3</doi><tpages>6</tpages></addata></record> |
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| ispartof | Enzyme and microbial technology, 1998, Vol.22 (1), p.2-7 |
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| source | Elsevier ScienceDirect Journals |
| subjects | Acetone Bacillus sp Bacteria Biological and medical sciences Biotechnology Column chromatography Enzyme engineering Fundamental and applied biological sciences. Psychology Improved methods for extraction and purification of enzymes Methods. Procedures. Technologies Phytase phytate Precipitation (chemical) Purification Thermodynamic stability thermostable enzyme |
| title | Purification and properties of a thermostable phytase from Bacillus sp. DS11 |
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