Purification of xylanase from alkaliphilic Bacillus sp. K-8 by using corn husk column
The objective of this work was to apply low cost materials, agricultural residues, to the purification of xylanase. The results showed that crude extracellular, cellulase-free xylanase of an alkaliphilic Bacillus sp. strain K-8 could be purified in a single step by affinity adsorption–desorption on...
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| Veröffentlicht in: | Process biochemistry (1991) 2006-12, Vol.41 (12), p.2441-2445 |
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| container_title | Process biochemistry (1991) |
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| creator | Tachaapaikoon, Chakrit Kyu, Khin Lay Ratanakhanokchai, Khanok |
| description | The objective of this work was to apply low cost materials, agricultural residues, to the purification of xylanase. The results showed that crude extracellular, cellulase-free xylanase of an alkaliphilic
Bacillus sp. strain K-8 could be purified in a single step by affinity adsorption–desorption on a corn husk column using a high flow rate, under the conditions 25
mM acetate buffer, pH 4.0, 4
°C, which prevented the hydrolysis of xylan by xylanase. After adsorption, the xylanase was eluted from the enzyme–corn husk complex with 500
mM Urea. The enzyme was purified 5.3-fold to homogeneity from culture supernatant. The molecular weight of the purified enzyme was 24
kDa as determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The specific activity and recovery yield after purification were 25.4
U/mg protein and 42.3%, respectively. |
| doi_str_mv | 10.1016/j.procbio.2006.07.004 |
| format | Article |
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Bacillus sp. strain K-8 could be purified in a single step by affinity adsorption–desorption on a corn husk column using a high flow rate, under the conditions 25
mM acetate buffer, pH 4.0, 4
°C, which prevented the hydrolysis of xylan by xylanase. After adsorption, the xylanase was eluted from the enzyme–corn husk complex with 500
mM Urea. The enzyme was purified 5.3-fold to homogeneity from culture supernatant. The molecular weight of the purified enzyme was 24
kDa as determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The specific activity and recovery yield after purification were 25.4
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Bacillus sp. strain K-8 could be purified in a single step by affinity adsorption–desorption on a corn husk column using a high flow rate, under the conditions 25
mM acetate buffer, pH 4.0, 4
°C, which prevented the hydrolysis of xylan by xylanase. After adsorption, the xylanase was eluted from the enzyme–corn husk complex with 500
mM Urea. The enzyme was purified 5.3-fold to homogeneity from culture supernatant. The molecular weight of the purified enzyme was 24
kDa as determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The specific activity and recovery yield after purification were 25.4
U/mg protein and 42.3%, respectively.</description><subject>Affinity adsorption–desorption</subject><subject>Alkaliphilic Bacillus sp</subject><subject>Corn husk column</subject><subject>Enzyme purification</subject><subject>Enzyme–insoluble substrate complex</subject><subject>Xylanase</subject><issn>1359-5113</issn><issn>1873-3298</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><recordid>eNqFkDtPAzEQhE8IJELgJyC5ortjfb5nhSDiJSJBQWrLt1kTJ8452DlE_j2Okp5qp5gZ7XxJcs0h48Cr22W28Q4747IcoMqgzgCKk2TEm1qkIm-b06hF2aYl5-I8uQhhCSA45zBKZh-DN9qg2hrXM6fZ786qXgVi2rs1U3alrNksjDXIHhQaa4fAwiZjb2nDuh0bgum_GDrfs8UQVlHZYd1fJmda2UBXxztOZk-Pn5OXdPr-_Dq5n6ZYiHqbdk0reIm8FkSAQBi_aqt4uznoHKjUOVHTalRUNGXR0RyxqxQWWOm80J0YJzeH3gjge6CwlWsTkGycQG4IMt_3A2-isTwY0bsQPGm58Wat_E5ykHuIcimPEOUeooRaRogxd3fIUVzxY8jLgIZ6pLnxhFs5d-afhj-0FH8z</recordid><startdate>20061201</startdate><enddate>20061201</enddate><creator>Tachaapaikoon, Chakrit</creator><creator>Kyu, Khin Lay</creator><creator>Ratanakhanokchai, Khanok</creator><general>Elsevier Ltd</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7U5</scope><scope>8FD</scope><scope>F28</scope><scope>FR3</scope><scope>L7M</scope></search><sort><creationdate>20061201</creationdate><title>Purification of xylanase from alkaliphilic Bacillus sp. K-8 by using corn husk column</title><author>Tachaapaikoon, Chakrit ; Kyu, Khin Lay ; Ratanakhanokchai, Khanok</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c437t-b89315c173ee0c0ec031960ecbd0f20e5f2ee89fcae4854bedccb6ac4c6f24fb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Affinity adsorption–desorption</topic><topic>Alkaliphilic Bacillus sp</topic><topic>Corn husk column</topic><topic>Enzyme purification</topic><topic>Enzyme–insoluble substrate complex</topic><topic>Xylanase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tachaapaikoon, Chakrit</creatorcontrib><creatorcontrib>Kyu, Khin Lay</creatorcontrib><creatorcontrib>Ratanakhanokchai, Khanok</creatorcontrib><collection>CrossRef</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Process biochemistry (1991)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tachaapaikoon, Chakrit</au><au>Kyu, Khin Lay</au><au>Ratanakhanokchai, Khanok</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification of xylanase from alkaliphilic Bacillus sp. K-8 by using corn husk column</atitle><jtitle>Process biochemistry (1991)</jtitle><date>2006-12-01</date><risdate>2006</risdate><volume>41</volume><issue>12</issue><spage>2441</spage><epage>2445</epage><pages>2441-2445</pages><issn>1359-5113</issn><eissn>1873-3298</eissn><abstract>The objective of this work was to apply low cost materials, agricultural residues, to the purification of xylanase. The results showed that crude extracellular, cellulase-free xylanase of an alkaliphilic
Bacillus sp. strain K-8 could be purified in a single step by affinity adsorption–desorption on a corn husk column using a high flow rate, under the conditions 25
mM acetate buffer, pH 4.0, 4
°C, which prevented the hydrolysis of xylan by xylanase. After adsorption, the xylanase was eluted from the enzyme–corn husk complex with 500
mM Urea. The enzyme was purified 5.3-fold to homogeneity from culture supernatant. The molecular weight of the purified enzyme was 24
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| identifier | ISSN: 1359-5113 |
| ispartof | Process biochemistry (1991), 2006-12, Vol.41 (12), p.2441-2445 |
| issn | 1359-5113 1873-3298 |
| language | eng |
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| source | Elsevier ScienceDirect Journals |
| subjects | Affinity adsorption–desorption Alkaliphilic Bacillus sp Corn husk column Enzyme purification Enzyme–insoluble substrate complex Xylanase |
| title | Purification of xylanase from alkaliphilic Bacillus sp. K-8 by using corn husk column |
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