Loading…

Purification and Characterization of Extra-Cellular Cholesterol Oxidase From Rhodococcus sp. PTCC 1633

In this study to isolate cholesterol oxidase (Cho) producing microorganism, a bacterium with high ability to produce Cho was found. It was identified with morphological, biochemical and molecular methods as a new species of Rhodococcus. Rhodococcus sp. PTCC 1633 has both extra-cellular and intracell...

Full description

Saved in:
Bibliographic Details
Published in:Biotechnology (Faisalābād, Pakistan) Pakistan), 2008-12, Vol.7 (4), p.751-756
Main Authors: Yazdi, M.T., Yazdi, Z.T., Ghasemian, A., Zarrini, G., Olyaee, N.H., Sepehrizad, Z.
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c2436-7cc250dfea4c4162d2c4c6ad5e77799dc520419355b57d389de5076b60484fc63
cites cdi_FETCH-LOGICAL-c2436-7cc250dfea4c4162d2c4c6ad5e77799dc520419355b57d389de5076b60484fc63
container_end_page 756
container_issue 4
container_start_page 751
container_title Biotechnology (Faisalābād, Pakistan)
container_volume 7
creator Yazdi, M.T.
Yazdi, Z.T.
Ghasemian, A.
Zarrini, G.
Olyaee, N.H.
Sepehrizad, Z.
description In this study to isolate cholesterol oxidase (Cho) producing microorganism, a bacterium with high ability to produce Cho was found. It was identified with morphological, biochemical and molecular methods as a new species of Rhodococcus. Rhodococcus sp. PTCC 1633 has both extra-cellular and intracellular Cho. It was cultured in optimized condition and extra-cellular Cho concentrated by Three Phase Partitioning (TPP) with a recovery of 85%. The concentrated enzyme was purified by one step ion exchange chromatography. On SDS-PAGE the purified enzyme showed a molecular weight of about 55 kDa. The enzyme was active in a wide rang of pH and temperature with an optimum pH and temperature of 7.0-7.5 and 40 degree C, respectively, for activity. The K sub(m) value for this enzyme was 15 mu M. A thermal stability experiment showed high stability at 40 degree C in 24 h.
doi_str_mv 10.3923/biotech.2008.751.756
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_20287454</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>20287454</sourcerecordid><originalsourceid>FETCH-LOGICAL-c2436-7cc250dfea4c4162d2c4c6ad5e77799dc520419355b57d389de5076b60484fc63</originalsourceid><addsrcrecordid>eNotkE1LAzEQhnNQsFb_gYecvG3Nd3aPsrQqFFqkgreQTrI0sm1qsgvVX29KPbwMDA_DOw9CD5TMeMP40zbEwcNuxgipZ1rSEnWFJlTVrGKN-rxBtzl_ESJqTpsJ6tZjCl0AO4R4wPbgcLuzycLgU_i9LGOH56ch2ar1fT_2NhUk9j4XJPZ4dQrOZo8XKe7x-y66CBFgzDgfZ3i9aVtMFed36Lqzffb3_3OKPhbzTftaLVcvb-3zsgImuKo0AJPEdd4KEFQxx0CAsk56rXXTOJCMCNpwKbdSO143zkui1VaVd0QHik_R4-XuMcXvsXQ0-5Ch9LYHH8dsGGG1FlIUUFxASDHn5DtzTGFv04-hxJxFmn-R5izSFJEliv8B_-dqng</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>20287454</pqid></control><display><type>article</type><title>Purification and Characterization of Extra-Cellular Cholesterol Oxidase From Rhodococcus sp. PTCC 1633</title><source>Free E-Journal (出版社公開部分のみ)</source><creator>Yazdi, M.T. ; Yazdi, Z.T. ; Ghasemian, A. ; Zarrini, G. ; Olyaee, N.H. ; Sepehrizad, Z.</creator><creatorcontrib>Yazdi, M.T. ; Yazdi, Z.T. ; Ghasemian, A. ; Zarrini, G. ; Olyaee, N.H. ; Sepehrizad, Z.</creatorcontrib><description>In this study to isolate cholesterol oxidase (Cho) producing microorganism, a bacterium with high ability to produce Cho was found. It was identified with morphological, biochemical and molecular methods as a new species of Rhodococcus. Rhodococcus sp. PTCC 1633 has both extra-cellular and intracellular Cho. It was cultured in optimized condition and extra-cellular Cho concentrated by Three Phase Partitioning (TPP) with a recovery of 85%. The concentrated enzyme was purified by one step ion exchange chromatography. On SDS-PAGE the purified enzyme showed a molecular weight of about 55 kDa. The enzyme was active in a wide rang of pH and temperature with an optimum pH and temperature of 7.0-7.5 and 40 degree C, respectively, for activity. The K sub(m) value for this enzyme was 15 mu M. A thermal stability experiment showed high stability at 40 degree C in 24 h.</description><identifier>ISSN: 1682-296X</identifier><identifier>DOI: 10.3923/biotech.2008.751.756</identifier><language>eng</language><subject>Rhodococcus</subject><ispartof>Biotechnology (Faisalābād, Pakistan), 2008-12, Vol.7 (4), p.751-756</ispartof><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2436-7cc250dfea4c4162d2c4c6ad5e77799dc520419355b57d389de5076b60484fc63</citedby><cites>FETCH-LOGICAL-c2436-7cc250dfea4c4162d2c4c6ad5e77799dc520419355b57d389de5076b60484fc63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids></links><search><creatorcontrib>Yazdi, M.T.</creatorcontrib><creatorcontrib>Yazdi, Z.T.</creatorcontrib><creatorcontrib>Ghasemian, A.</creatorcontrib><creatorcontrib>Zarrini, G.</creatorcontrib><creatorcontrib>Olyaee, N.H.</creatorcontrib><creatorcontrib>Sepehrizad, Z.</creatorcontrib><title>Purification and Characterization of Extra-Cellular Cholesterol Oxidase From Rhodococcus sp. PTCC 1633</title><title>Biotechnology (Faisalābād, Pakistan)</title><description>In this study to isolate cholesterol oxidase (Cho) producing microorganism, a bacterium with high ability to produce Cho was found. It was identified with morphological, biochemical and molecular methods as a new species of Rhodococcus. Rhodococcus sp. PTCC 1633 has both extra-cellular and intracellular Cho. It was cultured in optimized condition and extra-cellular Cho concentrated by Three Phase Partitioning (TPP) with a recovery of 85%. The concentrated enzyme was purified by one step ion exchange chromatography. On SDS-PAGE the purified enzyme showed a molecular weight of about 55 kDa. The enzyme was active in a wide rang of pH and temperature with an optimum pH and temperature of 7.0-7.5 and 40 degree C, respectively, for activity. The K sub(m) value for this enzyme was 15 mu M. A thermal stability experiment showed high stability at 40 degree C in 24 h.</description><subject>Rhodococcus</subject><issn>1682-296X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><recordid>eNotkE1LAzEQhnNQsFb_gYecvG3Nd3aPsrQqFFqkgreQTrI0sm1qsgvVX29KPbwMDA_DOw9CD5TMeMP40zbEwcNuxgipZ1rSEnWFJlTVrGKN-rxBtzl_ESJqTpsJ6tZjCl0AO4R4wPbgcLuzycLgU_i9LGOH56ch2ar1fT_2NhUk9j4XJPZ4dQrOZo8XKe7x-y66CBFgzDgfZ3i9aVtMFed36Lqzffb3_3OKPhbzTftaLVcvb-3zsgImuKo0AJPEdd4KEFQxx0CAsk56rXXTOJCMCNpwKbdSO143zkui1VaVd0QHik_R4-XuMcXvsXQ0-5Ch9LYHH8dsGGG1FlIUUFxASDHn5DtzTGFv04-hxJxFmn-R5izSFJEliv8B_-dqng</recordid><startdate>20081201</startdate><enddate>20081201</enddate><creator>Yazdi, M.T.</creator><creator>Yazdi, Z.T.</creator><creator>Ghasemian, A.</creator><creator>Zarrini, G.</creator><creator>Olyaee, N.H.</creator><creator>Sepehrizad, Z.</creator><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>20081201</creationdate><title>Purification and Characterization of Extra-Cellular Cholesterol Oxidase From Rhodococcus sp. PTCC 1633</title><author>Yazdi, M.T. ; Yazdi, Z.T. ; Ghasemian, A. ; Zarrini, G. ; Olyaee, N.H. ; Sepehrizad, Z.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2436-7cc250dfea4c4162d2c4c6ad5e77799dc520419355b57d389de5076b60484fc63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Rhodococcus</topic><toplevel>online_resources</toplevel><creatorcontrib>Yazdi, M.T.</creatorcontrib><creatorcontrib>Yazdi, Z.T.</creatorcontrib><creatorcontrib>Ghasemian, A.</creatorcontrib><creatorcontrib>Zarrini, G.</creatorcontrib><creatorcontrib>Olyaee, N.H.</creatorcontrib><creatorcontrib>Sepehrizad, Z.</creatorcontrib><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</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><jtitle>Biotechnology (Faisalābād, Pakistan)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yazdi, M.T.</au><au>Yazdi, Z.T.</au><au>Ghasemian, A.</au><au>Zarrini, G.</au><au>Olyaee, N.H.</au><au>Sepehrizad, Z.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and Characterization of Extra-Cellular Cholesterol Oxidase From Rhodococcus sp. PTCC 1633</atitle><jtitle>Biotechnology (Faisalābād, Pakistan)</jtitle><date>2008-12-01</date><risdate>2008</risdate><volume>7</volume><issue>4</issue><spage>751</spage><epage>756</epage><pages>751-756</pages><issn>1682-296X</issn><abstract>In this study to isolate cholesterol oxidase (Cho) producing microorganism, a bacterium with high ability to produce Cho was found. It was identified with morphological, biochemical and molecular methods as a new species of Rhodococcus. Rhodococcus sp. PTCC 1633 has both extra-cellular and intracellular Cho. It was cultured in optimized condition and extra-cellular Cho concentrated by Three Phase Partitioning (TPP) with a recovery of 85%. The concentrated enzyme was purified by one step ion exchange chromatography. On SDS-PAGE the purified enzyme showed a molecular weight of about 55 kDa. The enzyme was active in a wide rang of pH and temperature with an optimum pH and temperature of 7.0-7.5 and 40 degree C, respectively, for activity. The K sub(m) value for this enzyme was 15 mu M. A thermal stability experiment showed high stability at 40 degree C in 24 h.</abstract><doi>10.3923/biotech.2008.751.756</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 1682-296X
ispartof Biotechnology (Faisalābād, Pakistan), 2008-12, Vol.7 (4), p.751-756
issn 1682-296X
language eng
recordid cdi_proquest_miscellaneous_20287454
source Free E-Journal (出版社公開部分のみ)
subjects Rhodococcus
title Purification and Characterization of Extra-Cellular Cholesterol Oxidase From Rhodococcus sp. PTCC 1633
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-08T14%3A29%3A39IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Purification%20and%20Characterization%20of%20Extra-Cellular%20Cholesterol%20Oxidase%20From%20Rhodococcus%20sp.%20PTCC%201633&rft.jtitle=Biotechnology%20(Faisala%CC%84ba%CC%84d,%20Pakistan)&rft.au=Yazdi,%20M.T.&rft.date=2008-12-01&rft.volume=7&rft.issue=4&rft.spage=751&rft.epage=756&rft.pages=751-756&rft.issn=1682-296X&rft_id=info:doi/10.3923/biotech.2008.751.756&rft_dat=%3Cproquest_cross%3E20287454%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c2436-7cc250dfea4c4162d2c4c6ad5e77799dc520419355b57d389de5076b60484fc63%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=20287454&rft_id=info:pmid/&rfr_iscdi=true