A novel immobilization method for nuclease P1 on macroporous absorbent resin with glutaraldehyde cross-linking and determination of its properties
► Nuclease P1 immobilized on macroporous absorbent resin. ► The purification of enzyme uses heat-treatment to reduce the cost for research. ► Crude enzyme used for immobilization lowers the cost for industrial applications. ► The immobilization method is simultaneous immobilization and cross-linking...
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| Veröffentlicht in: | Process biochemistry (1991) 2012-04, Vol.47 (4), p.665-670 |
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| container_title | Process biochemistry (1991) |
| container_volume | 47 |
| creator | Li, Bingbing Chen, Yong Chen, Xiaochun Liu, Dong Niu, Huanqing Xiong, Jian Wu, Jinglan Xie, Jingjing Bai, Jianxin Ying, Hanjie |
| description | ► Nuclease P1 immobilized on macroporous absorbent resin. ► The purification of enzyme uses heat-treatment to reduce the cost for research. ► Crude enzyme used for immobilization lowers the cost for industrial applications. ► The immobilization method is simultaneous immobilization and cross-linking. ► Activation energy for immobilized enzyme was lower compared with that of free enzyme.
Microbial nuclease P1 from Penicllium citrinum was immobilized on macroporous absorbent resins: strong polar poly (styrene-co-DVB) resin (SPPSD), polymethacrylic ester resin and poly (styrene-co-DVB)-Br resin. The results showed that SPPSD was the best carrier. Three methods of glutaraldehyde cross-linking were used and simultaneous immobilization and cross-linking (CIS) was demonstrated to be the best method. The functional properties of immobilized nuclease P1 were studied and compared to those of the free enzyme. The highest enzyme activities of free and immobilized nuclease P1 were obtained in 0.2M acetate buffer at pH 4.5 and a temperature of 70°C. An increase in Km (from 3.165 to 18.125mgmL−1) and a decrease in Vmax (from 1667.18 to 443.95Umin−1mL−1) were recorded after immobilization. SPPSD-glutaraldehyde-nuclease P1 exhibited better thermal stability than the free enzyme. The apparent activation energy (Ea) of the free and immobilized nuclease P1 was 137.04kJmol−1 and 98.43kJmol−1, respectively, implying that the catalytic efficiency of the immobilized enzyme was restricted by mass-transfer rather than kinetic limit. |
| doi_str_mv | 10.1016/j.procbio.2012.01.008 |
| format | Article |
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Microbial nuclease P1 from Penicllium citrinum was immobilized on macroporous absorbent resins: strong polar poly (styrene-co-DVB) resin (SPPSD), polymethacrylic ester resin and poly (styrene-co-DVB)-Br resin. The results showed that SPPSD was the best carrier. Three methods of glutaraldehyde cross-linking were used and simultaneous immobilization and cross-linking (CIS) was demonstrated to be the best method. The functional properties of immobilized nuclease P1 were studied and compared to those of the free enzyme. The highest enzyme activities of free and immobilized nuclease P1 were obtained in 0.2M acetate buffer at pH 4.5 and a temperature of 70°C. An increase in Km (from 3.165 to 18.125mgmL−1) and a decrease in Vmax (from 1667.18 to 443.95Umin−1mL−1) were recorded after immobilization. SPPSD-glutaraldehyde-nuclease P1 exhibited better thermal stability than the free enzyme. The apparent activation energy (Ea) of the free and immobilized nuclease P1 was 137.04kJmol−1 and 98.43kJmol−1, respectively, implying that the catalytic efficiency of the immobilized enzyme was restricted by mass-transfer rather than kinetic limit.</description><identifier>ISSN: 1359-5113</identifier><identifier>EISSN: 1873-3298</identifier><identifier>DOI: 10.1016/j.procbio.2012.01.008</identifier><language>eng</language><publisher>Elsevier Ltd</publisher><subject>acetates ; activation energy ; catalytic activity ; crosslinking ; enzyme activity ; functional properties ; glutaraldehyde ; Glutaraldehyde cross-linking ; Immobilization ; immobilized enzymes ; Macroporous absorbent resin ; mass transfer ; Nuclease P1 ; resins ; temperature ; thermal stability</subject><ispartof>Process biochemistry (1991), 2012-04, Vol.47 (4), p.665-670</ispartof><rights>2012</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2106-90e556abd823c26001992f8b74c99bf88fe5d8fe87a04a7c4e9d16626ea5ba2f3</citedby><cites>FETCH-LOGICAL-c2106-90e556abd823c26001992f8b74c99bf88fe5d8fe87a04a7c4e9d16626ea5ba2f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1359511312000244$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids></links><search><creatorcontrib>Li, Bingbing</creatorcontrib><creatorcontrib>Chen, Yong</creatorcontrib><creatorcontrib>Chen, Xiaochun</creatorcontrib><creatorcontrib>Liu, Dong</creatorcontrib><creatorcontrib>Niu, Huanqing</creatorcontrib><creatorcontrib>Xiong, Jian</creatorcontrib><creatorcontrib>Wu, Jinglan</creatorcontrib><creatorcontrib>Xie, Jingjing</creatorcontrib><creatorcontrib>Bai, Jianxin</creatorcontrib><creatorcontrib>Ying, Hanjie</creatorcontrib><title>A novel immobilization method for nuclease P1 on macroporous absorbent resin with glutaraldehyde cross-linking and determination of its properties</title><title>Process biochemistry (1991)</title><description>► Nuclease P1 immobilized on macroporous absorbent resin. ► The purification of enzyme uses heat-treatment to reduce the cost for research. ► Crude enzyme used for immobilization lowers the cost for industrial applications. ► The immobilization method is simultaneous immobilization and cross-linking. ► Activation energy for immobilized enzyme was lower compared with that of free enzyme.
Microbial nuclease P1 from Penicllium citrinum was immobilized on macroporous absorbent resins: strong polar poly (styrene-co-DVB) resin (SPPSD), polymethacrylic ester resin and poly (styrene-co-DVB)-Br resin. The results showed that SPPSD was the best carrier. Three methods of glutaraldehyde cross-linking were used and simultaneous immobilization and cross-linking (CIS) was demonstrated to be the best method. The functional properties of immobilized nuclease P1 were studied and compared to those of the free enzyme. The highest enzyme activities of free and immobilized nuclease P1 were obtained in 0.2M acetate buffer at pH 4.5 and a temperature of 70°C. An increase in Km (from 3.165 to 18.125mgmL−1) and a decrease in Vmax (from 1667.18 to 443.95Umin−1mL−1) were recorded after immobilization. SPPSD-glutaraldehyde-nuclease P1 exhibited better thermal stability than the free enzyme. The apparent activation energy (Ea) of the free and immobilized nuclease P1 was 137.04kJmol−1 and 98.43kJmol−1, respectively, implying that the catalytic efficiency of the immobilized enzyme was restricted by mass-transfer rather than kinetic limit.</description><subject>acetates</subject><subject>activation energy</subject><subject>catalytic activity</subject><subject>crosslinking</subject><subject>enzyme activity</subject><subject>functional properties</subject><subject>glutaraldehyde</subject><subject>Glutaraldehyde cross-linking</subject><subject>Immobilization</subject><subject>immobilized enzymes</subject><subject>Macroporous absorbent resin</subject><subject>mass transfer</subject><subject>Nuclease P1</subject><subject>resins</subject><subject>temperature</subject><subject>thermal stability</subject><issn>1359-5113</issn><issn>1873-3298</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><recordid>eNqFkdFqFDEUhgexYG19BDF3Xs2YZHZmkispxapQUKi9DpnkZPesmWRNspX6GH1is07vhXASON85f37-pnnLaMcoGz_su0OKZsbYccp4R1lHqXjRnDMx9W3PpXhZ3_0g24Gx_lXzOuc9pT1jjJ43T1ckxAfwBJclzujxjy4YA1mg7KIlLiYSjsaDzkC-M3LqaJPiIaZ4zETPOaYZQiEJMgbyG8uObP2x6KS9hd2jBVLpnFuP4SeGLdHBEgsF0oJhVYqOYMmkWjhAKgj5sjlz2md483xfNPc3n35cf2lvv33-en112xrO6NhKCsMw6tkK3hs-Usqk5E7M08ZIOTshHAy2FjFputGT2YC0bBz5CHqYNXf9RfN-3Vulfx0hF7VgNuC9DlDNKTkKVg8dKzms5D8vCZw6JFx0elSMqlMEaq-eI1CnCBRlqkZQ596tc05HpbcJs7q_q0D9LJ026-aPKwHV6ANCUtkgBAMWE5iibMT_aPwF1EafiQ</recordid><startdate>20120401</startdate><enddate>20120401</enddate><creator>Li, Bingbing</creator><creator>Chen, Yong</creator><creator>Chen, Xiaochun</creator><creator>Liu, Dong</creator><creator>Niu, Huanqing</creator><creator>Xiong, Jian</creator><creator>Wu, Jinglan</creator><creator>Xie, Jingjing</creator><creator>Bai, Jianxin</creator><creator>Ying, Hanjie</creator><general>Elsevier Ltd</general><scope>FBQ</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>20120401</creationdate><title>A novel immobilization method for nuclease P1 on macroporous absorbent resin with glutaraldehyde cross-linking and determination of its properties</title><author>Li, Bingbing ; Chen, Yong ; Chen, Xiaochun ; Liu, Dong ; Niu, Huanqing ; Xiong, Jian ; Wu, Jinglan ; Xie, Jingjing ; Bai, Jianxin ; Ying, Hanjie</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2106-90e556abd823c26001992f8b74c99bf88fe5d8fe87a04a7c4e9d16626ea5ba2f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>acetates</topic><topic>activation energy</topic><topic>catalytic activity</topic><topic>crosslinking</topic><topic>enzyme activity</topic><topic>functional properties</topic><topic>glutaraldehyde</topic><topic>Glutaraldehyde cross-linking</topic><topic>Immobilization</topic><topic>immobilized enzymes</topic><topic>Macroporous absorbent resin</topic><topic>mass transfer</topic><topic>Nuclease P1</topic><topic>resins</topic><topic>temperature</topic><topic>thermal stability</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, Bingbing</creatorcontrib><creatorcontrib>Chen, Yong</creatorcontrib><creatorcontrib>Chen, Xiaochun</creatorcontrib><creatorcontrib>Liu, Dong</creatorcontrib><creatorcontrib>Niu, Huanqing</creatorcontrib><creatorcontrib>Xiong, Jian</creatorcontrib><creatorcontrib>Wu, Jinglan</creatorcontrib><creatorcontrib>Xie, Jingjing</creatorcontrib><creatorcontrib>Bai, Jianxin</creatorcontrib><creatorcontrib>Ying, Hanjie</creatorcontrib><collection>AGRIS</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Process biochemistry (1991)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, Bingbing</au><au>Chen, Yong</au><au>Chen, Xiaochun</au><au>Liu, Dong</au><au>Niu, Huanqing</au><au>Xiong, Jian</au><au>Wu, Jinglan</au><au>Xie, Jingjing</au><au>Bai, Jianxin</au><au>Ying, Hanjie</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel immobilization method for nuclease P1 on macroporous absorbent resin with glutaraldehyde cross-linking and determination of its properties</atitle><jtitle>Process biochemistry (1991)</jtitle><date>2012-04-01</date><risdate>2012</risdate><volume>47</volume><issue>4</issue><spage>665</spage><epage>670</epage><pages>665-670</pages><issn>1359-5113</issn><eissn>1873-3298</eissn><abstract>► Nuclease P1 immobilized on macroporous absorbent resin. ► The purification of enzyme uses heat-treatment to reduce the cost for research. ► Crude enzyme used for immobilization lowers the cost for industrial applications. ► The immobilization method is simultaneous immobilization and cross-linking. ► Activation energy for immobilized enzyme was lower compared with that of free enzyme.
Microbial nuclease P1 from Penicllium citrinum was immobilized on macroporous absorbent resins: strong polar poly (styrene-co-DVB) resin (SPPSD), polymethacrylic ester resin and poly (styrene-co-DVB)-Br resin. The results showed that SPPSD was the best carrier. Three methods of glutaraldehyde cross-linking were used and simultaneous immobilization and cross-linking (CIS) was demonstrated to be the best method. The functional properties of immobilized nuclease P1 were studied and compared to those of the free enzyme. The highest enzyme activities of free and immobilized nuclease P1 were obtained in 0.2M acetate buffer at pH 4.5 and a temperature of 70°C. An increase in Km (from 3.165 to 18.125mgmL−1) and a decrease in Vmax (from 1667.18 to 443.95Umin−1mL−1) were recorded after immobilization. SPPSD-glutaraldehyde-nuclease P1 exhibited better thermal stability than the free enzyme. The apparent activation energy (Ea) of the free and immobilized nuclease P1 was 137.04kJmol−1 and 98.43kJmol−1, respectively, implying that the catalytic efficiency of the immobilized enzyme was restricted by mass-transfer rather than kinetic limit.</abstract><pub>Elsevier Ltd</pub><doi>10.1016/j.procbio.2012.01.008</doi><tpages>6</tpages></addata></record> |
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| ispartof | Process biochemistry (1991), 2012-04, Vol.47 (4), p.665-670 |
| issn | 1359-5113 1873-3298 |
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| source | Elsevier ScienceDirect Journals Complete |
| subjects | acetates activation energy catalytic activity crosslinking enzyme activity functional properties glutaraldehyde Glutaraldehyde cross-linking Immobilization immobilized enzymes Macroporous absorbent resin mass transfer Nuclease P1 resins temperature thermal stability |
| title | A novel immobilization method for nuclease P1 on macroporous absorbent resin with glutaraldehyde cross-linking and determination of its properties |
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