Purification and properties of a phytase from Candida krusei WZ-001
A phytase from Candida krusei WZ-001 isolated from soil was purified to electrophoretic homogeneity by ion-exchange chromatography, hydrophobic interaction chromatography, and gel filtration. The phytase is composed of two different subunits with molecular masses of 116 kDa and 31 kDa on SDS-PAGE (o...
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| Veröffentlicht in: | Journal of bioscience and bioengineering 2002, Vol.94 (5), p.419-425 |
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| creator | Quan, Chun-Shan Fan, Sheng-Di Zhang, Ling-Hua Wang, Yun-Ji Ohta, Yoshiyuki |
| description | A phytase from
Candida krusei WZ-001 isolated from soil was purified to electrophoretic homogeneity by ion-exchange chromatography, hydrophobic interaction chromatography, and gel filtration. The phytase is composed of two different subunits with molecular masses of 116 kDa and 31 kDa on SDS-PAGE (or 120 kDa and 30 kDa on gel chromatography), with the larger subunit having a glycosylation rate of around 35%. The phytase has an optimum pH of 4.6, an optimum temperature of 40°C and a p
I value of 5.5. The phytase activity was stimulated by 2-mercapto-ethanol and dithiothreitol (DTT), and inhibited by Zn
2+, Mg
2+, iodoacetate, p
I value of 5.5. The phytase activity was stimulated by 2-mercapto-ethanol ethanol and dithiothreitol (DTT), and inhibited by Zn
2+, Mg
2+, iodoacetate,
p-chroloromercuribenzoate (
pCMB) and phenylmethylsulfonyl fluoride (PMSF). The phytase displayed a broad substrate specificity and the
K
m for phytate was 0.03 mM. Phytate was sequentially hydrolyzed by the phytase. Furthermore, 1D and 2D NMR analyses and bioassay of myoinositol indicated that the end hydrolysis product of phytate was myoinositol 2-monophosphate. |
| doi_str_mv | 10.1016/S1389-1723(02)80219-5 |
| format | Article |
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Candida krusei WZ-001 isolated from soil was purified to electrophoretic homogeneity by ion-exchange chromatography, hydrophobic interaction chromatography, and gel filtration. The phytase is composed of two different subunits with molecular masses of 116 kDa and 31 kDa on SDS-PAGE (or 120 kDa and 30 kDa on gel chromatography), with the larger subunit having a glycosylation rate of around 35%. The phytase has an optimum pH of 4.6, an optimum temperature of 40°C and a p
I value of 5.5. The phytase activity was stimulated by 2-mercapto-ethanol and dithiothreitol (DTT), and inhibited by Zn
2+, Mg
2+, iodoacetate, p
I value of 5.5. The phytase activity was stimulated by 2-mercapto-ethanol ethanol and dithiothreitol (DTT), and inhibited by Zn
2+, Mg
2+, iodoacetate,
p-chroloromercuribenzoate (
pCMB) and phenylmethylsulfonyl fluoride (PMSF). The phytase displayed a broad substrate specificity and the
K
m for phytate was 0.03 mM. Phytate was sequentially hydrolyzed by the phytase. Furthermore, 1D and 2D NMR analyses and bioassay of myoinositol indicated that the end hydrolysis product of phytate was myoinositol 2-monophosphate.</description><identifier>ISSN: 1389-1723</identifier><identifier>EISSN: 1347-4421</identifier><identifier>DOI: 10.1016/S1389-1723(02)80219-5</identifier><identifier>PMID: 16233328</identifier><identifier>CODEN: JFBIEX</identifier><language>eng</language><publisher>Amsterdarm: Elsevier B.V</publisher><subject>Biological and medical sciences ; Biotechnology ; CANDIDA ; Candida krusei ; Enzyme engineering ; Fundamental and applied biological sciences. Psychology ; Improved methods for extraction and purification of enzymes ; Methods. Procedures. Technologies ; microbial phytase ; phosphate ; PHYTASE ; phytate degradation ; PHYTATES ; PURIFICATION</subject><ispartof>Journal of bioscience and bioengineering, 2002, Vol.94 (5), p.419-425</ispartof><rights>2002</rights><rights>2003 INIST-CNRS</rights><rights>Copyright Japan Science and Technology Agency 2002</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c563t-2497327a755fae56a8a2c16009bffc01d5b649f1a721d5d6c30ad3506eb3eb953</citedby><cites>FETCH-LOGICAL-c563t-2497327a755fae56a8a2c16009bffc01d5b649f1a721d5d6c30ad3506eb3eb953</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S1389-1723(02)80219-5$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,4024,27923,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14544066$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16233328$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Quan, Chun-Shan</creatorcontrib><creatorcontrib>Fan, Sheng-Di</creatorcontrib><creatorcontrib>Zhang, Ling-Hua</creatorcontrib><creatorcontrib>Wang, Yun-Ji</creatorcontrib><creatorcontrib>Ohta, Yoshiyuki</creatorcontrib><title>Purification and properties of a phytase from Candida krusei WZ-001</title><title>Journal of bioscience and bioengineering</title><addtitle>J Biosci Bioeng</addtitle><description>A phytase from
Candida krusei WZ-001 isolated from soil was purified to electrophoretic homogeneity by ion-exchange chromatography, hydrophobic interaction chromatography, and gel filtration. The phytase is composed of two different subunits with molecular masses of 116 kDa and 31 kDa on SDS-PAGE (or 120 kDa and 30 kDa on gel chromatography), with the larger subunit having a glycosylation rate of around 35%. The phytase has an optimum pH of 4.6, an optimum temperature of 40°C and a p
I value of 5.5. The phytase activity was stimulated by 2-mercapto-ethanol and dithiothreitol (DTT), and inhibited by Zn
2+, Mg
2+, iodoacetate, p
I value of 5.5. The phytase activity was stimulated by 2-mercapto-ethanol ethanol and dithiothreitol (DTT), and inhibited by Zn
2+, Mg
2+, iodoacetate,
p-chroloromercuribenzoate (
pCMB) and phenylmethylsulfonyl fluoride (PMSF). The phytase displayed a broad substrate specificity and the
K
m for phytate was 0.03 mM. Phytate was sequentially hydrolyzed by the phytase. Furthermore, 1D and 2D NMR analyses and bioassay of myoinositol indicated that the end hydrolysis product of phytate was myoinositol 2-monophosphate.</description><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>CANDIDA</subject><subject>Candida krusei</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>microbial phytase</subject><subject>phosphate</subject><subject>PHYTASE</subject><subject>phytate degradation</subject><subject>PHYTATES</subject><subject>PURIFICATION</subject><issn>1389-1723</issn><issn>1347-4421</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><recordid>eNqFkVtrFTEUhYMotlZ_QiUgij6MZuc68yRyaL1QsKAi-BL2ZBJNPWdyTGaE_nszPQMFXwqBbNhfFitrEXIK7DUw0G--gGi7BgwXLxl_1TIOXaPukWMQ0jRScri_zCtyRB6VcsUYGGbgITkCzYUQvD0mm8s5xxAdTjGNFMeB7nPa-zxFX2gKFOn-1_WExdOQ045uKhEHpL_zXHyk3380VfQxeRBwW_yT9T4h387Pvm4-NBef33_cvLtonNJiarjsjOAGjVIBvdLYInegGev6EByDQfVadgHQ8DoP2gmGg1BM-174vlPihLw46FaLf2ZfJruLxfntFkef5mIN77hWLdwJQmuUBi4r-Ow_8CrNeayfsCAlCKE46EqpA-VyKiX7YPc57jBfW2B2KcPelGGXpC3j9qYMu_h9uqrP_c4Pt6_W9CvwfAWwONyGjKOL5ZaTSkqmFwOnBy5gsvgzV-bTJWdMLEeaun972Pua_t_osy0u-tH5IWbvJjukeIfVfzrKq5k</recordid><startdate>2002</startdate><enddate>2002</enddate><creator>Quan, Chun-Shan</creator><creator>Fan, Sheng-Di</creator><creator>Zhang, Ling-Hua</creator><creator>Wang, Yun-Ji</creator><creator>Ohta, Yoshiyuki</creator><general>Elsevier B.V</general><general>Elsevier Science</general><general>Elsevier Limited</general><scope>FBQ</scope><scope>IQODW</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>2002</creationdate><title>Purification and properties of a phytase from Candida krusei WZ-001</title><author>Quan, Chun-Shan ; Fan, Sheng-Di ; Zhang, Ling-Hua ; Wang, Yun-Ji ; Ohta, Yoshiyuki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c563t-2497327a755fae56a8a2c16009bffc01d5b649f1a721d5d6c30ad3506eb3eb953</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>CANDIDA</topic><topic>Candida krusei</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>microbial phytase</topic><topic>phosphate</topic><topic>PHYTASE</topic><topic>phytate degradation</topic><topic>PHYTATES</topic><topic>PURIFICATION</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Quan, Chun-Shan</creatorcontrib><creatorcontrib>Fan, Sheng-Di</creatorcontrib><creatorcontrib>Zhang, Ling-Hua</creatorcontrib><creatorcontrib>Wang, Yun-Ji</creatorcontrib><creatorcontrib>Ohta, Yoshiyuki</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of bioscience and bioengineering</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Quan, Chun-Shan</au><au>Fan, Sheng-Di</au><au>Zhang, Ling-Hua</au><au>Wang, Yun-Ji</au><au>Ohta, Yoshiyuki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and properties of a phytase from Candida krusei WZ-001</atitle><jtitle>Journal of bioscience and bioengineering</jtitle><addtitle>J Biosci Bioeng</addtitle><date>2002</date><risdate>2002</risdate><volume>94</volume><issue>5</issue><spage>419</spage><epage>425</epage><pages>419-425</pages><issn>1389-1723</issn><eissn>1347-4421</eissn><coden>JFBIEX</coden><abstract>A phytase from
Candida krusei WZ-001 isolated from soil was purified to electrophoretic homogeneity by ion-exchange chromatography, hydrophobic interaction chromatography, and gel filtration. The phytase is composed of two different subunits with molecular masses of 116 kDa and 31 kDa on SDS-PAGE (or 120 kDa and 30 kDa on gel chromatography), with the larger subunit having a glycosylation rate of around 35%. The phytase has an optimum pH of 4.6, an optimum temperature of 40°C and a p
I value of 5.5. The phytase activity was stimulated by 2-mercapto-ethanol and dithiothreitol (DTT), and inhibited by Zn
2+, Mg
2+, iodoacetate, p
I value of 5.5. The phytase activity was stimulated by 2-mercapto-ethanol ethanol and dithiothreitol (DTT), and inhibited by Zn
2+, Mg
2+, iodoacetate,
p-chroloromercuribenzoate (
pCMB) and phenylmethylsulfonyl fluoride (PMSF). The phytase displayed a broad substrate specificity and the
K
m for phytate was 0.03 mM. Phytate was sequentially hydrolyzed by the phytase. Furthermore, 1D and 2D NMR analyses and bioassay of myoinositol indicated that the end hydrolysis product of phytate was myoinositol 2-monophosphate.</abstract><cop>Amsterdarm</cop><pub>Elsevier B.V</pub><pmid>16233328</pmid><doi>10.1016/S1389-1723(02)80219-5</doi><tpages>7</tpages></addata></record> |
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| ispartof | Journal of bioscience and bioengineering, 2002, Vol.94 (5), p.419-425 |
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| subjects | Biological and medical sciences Biotechnology CANDIDA Candida krusei Enzyme engineering Fundamental and applied biological sciences. Psychology Improved methods for extraction and purification of enzymes Methods. Procedures. Technologies microbial phytase phosphate PHYTASE phytate degradation PHYTATES PURIFICATION |
| title | Purification and properties of a phytase from Candida krusei WZ-001 |
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