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Supramolecular-mediated thermostabilization of phenylalanine dehydrogenase modified with β-cyclodextrin derivatives
Two different monoactivated β-cyclodextrin derivatives, named mono-6-amino-6-deoxy-β-CD (CD1) and mono-6-(5-carboxypentane-1-carboxamidoyl)-6-deoxy-β-CD (CD2) were evaluated as modifying agents for Bacillus badius phenylalanine dehydrogenase. The enzyme glycosidated with CD1 and CD2 contained about...
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| Published in: | Biochemical engineering journal 2006-05, Vol.30 (1), p.26-32 |
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| Main Authors: | , , , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c273t-576bf9a3769e93d32f4e79fd2dcd98292bf1dd290ed75498e8709194ad6e98153 |
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| cites | cdi_FETCH-LOGICAL-c273t-576bf9a3769e93d32f4e79fd2dcd98292bf1dd290ed75498e8709194ad6e98153 |
| container_end_page | 32 |
| container_issue | 1 |
| container_start_page | 26 |
| container_title | Biochemical engineering journal |
| container_volume | 30 |
| creator | Villalonga, Reynaldo Tachibana, Shinjiro Cao, Roberto Ramirez, Hector L. Asano, Yasuhisa |
| description | Two different monoactivated β-cyclodextrin derivatives, named mono-6-amino-6-deoxy-β-CD (CD1) and mono-6-(5-carboxypentane-1-carboxamidoyl)-6-deoxy-β-CD (CD2) were evaluated as modifying agents for
Bacillus badius phenylalanine dehydrogenase. The enzyme glycosidated with CD1 and CD2 contained about 18
mol and 15
mol oligosaccharide per mol of protein and retained 60% and 81% of the initial activity, respectively. The optimum temperature for the catalytic activity of phenylalanine dehydrogenase was increased in 10
°C after attaching the CDs residues. The enzyme thermostability profile was improved, and its resistance to thermal inactivation at different temperatures ranging from 45
°C to 60
°C was noticeably increased after glycosidation. The activation free energy of thermal inactivation was increased by 16.8
kJ/mol and 12.6
kJ/mol for the enzyme modified with CD1 and CD2, respectively. The influence of supramolecular host–guest associations on the improved thermotolerance showed by the modified enzyme forms was demonstrated by fluorescence spectroscopy and enzymatic measurements. |
| doi_str_mv | 10.1016/j.bej.2006.01.013 |
| format | article |
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Bacillus badius phenylalanine dehydrogenase. The enzyme glycosidated with CD1 and CD2 contained about 18
mol and 15
mol oligosaccharide per mol of protein and retained 60% and 81% of the initial activity, respectively. The optimum temperature for the catalytic activity of phenylalanine dehydrogenase was increased in 10
°C after attaching the CDs residues. The enzyme thermostability profile was improved, and its resistance to thermal inactivation at different temperatures ranging from 45
°C to 60
°C was noticeably increased after glycosidation. The activation free energy of thermal inactivation was increased by 16.8
kJ/mol and 12.6
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Bacillus badius phenylalanine dehydrogenase. The enzyme glycosidated with CD1 and CD2 contained about 18
mol and 15
mol oligosaccharide per mol of protein and retained 60% and 81% of the initial activity, respectively. The optimum temperature for the catalytic activity of phenylalanine dehydrogenase was increased in 10
°C after attaching the CDs residues. The enzyme thermostability profile was improved, and its resistance to thermal inactivation at different temperatures ranging from 45
°C to 60
°C was noticeably increased after glycosidation. The activation free energy of thermal inactivation was increased by 16.8
kJ/mol and 12.6
kJ/mol for the enzyme modified with CD1 and CD2, respectively. The influence of supramolecular host–guest associations on the improved thermotolerance showed by the modified enzyme forms was demonstrated by fluorescence spectroscopy and enzymatic measurements.</description><subject>Amino acids</subject><subject>Bacillus badius</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Cyclodextrin</subject><subject>Enzyme activity</subject><subject>Enzyme technology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Phenylalanine dehydrogenase</subject><subject>Protein denaturation</subject><issn>1369-703X</issn><issn>1873-295X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><recordid>eNp9kM9KAzEQxhdRsFYfwNte9LY12Ww3GzxJ8R8UPKjQW0iTiU3JbmqSrdbH8kF8JlNa8CYMzBx-3zczX5adYzTCCNdXy9EclqMSoXqEcCpykA1wQ0lRsvHsMM2kZgVFZHacnYSwRAkklA6y-NyvvGidBdlb4YsWlBERVB4X4FsXopgba75ENK7Lnc5XC-g2VljRmQ5yBYuN8u4NOhEgb50y2iTth4mL_Oe7kBtpnYLP6E2XWG_WyWcN4TQ70sIGONv3YfZ6d_syeSimT_ePk5tpIUtKYjGm9VwzQWjNgBFFSl0BZVqVSirWlKyca6xUyRAoOq5YAw1FDLNKqBpYg8dkmF3ufFfevfcQIm9NkGDT9eD6wDFrqrrCdQLxDpTeheBB85U3rfAbjhHf5suXPOXLt_lyhFORpLnYm4sghdVedNKEPyGllFBUJe56x0H6dG3A8yANdDIF7UFGrpz5Z8svtTeUpQ</recordid><startdate>20060501</startdate><enddate>20060501</enddate><creator>Villalonga, Reynaldo</creator><creator>Tachibana, Shinjiro</creator><creator>Cao, Roberto</creator><creator>Ramirez, Hector L.</creator><creator>Asano, Yasuhisa</creator><general>Elsevier B.V</general><general>Elsevier Science</general><scope>IQODW</scope><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>20060501</creationdate><title>Supramolecular-mediated thermostabilization of phenylalanine dehydrogenase modified with β-cyclodextrin derivatives</title><author>Villalonga, Reynaldo ; Tachibana, Shinjiro ; Cao, Roberto ; Ramirez, Hector L. ; Asano, Yasuhisa</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c273t-576bf9a3769e93d32f4e79fd2dcd98292bf1dd290ed75498e8709194ad6e98153</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amino acids</topic><topic>Bacillus badius</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Cyclodextrin</topic><topic>Enzyme activity</topic><topic>Enzyme technology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Phenylalanine dehydrogenase</topic><topic>Protein denaturation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Villalonga, Reynaldo</creatorcontrib><creatorcontrib>Tachibana, Shinjiro</creatorcontrib><creatorcontrib>Cao, Roberto</creatorcontrib><creatorcontrib>Ramirez, Hector L.</creatorcontrib><creatorcontrib>Asano, Yasuhisa</creatorcontrib><collection>Pascal-Francis</collection><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>Biochemical engineering journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Villalonga, Reynaldo</au><au>Tachibana, Shinjiro</au><au>Cao, Roberto</au><au>Ramirez, Hector L.</au><au>Asano, Yasuhisa</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Supramolecular-mediated thermostabilization of phenylalanine dehydrogenase modified with β-cyclodextrin derivatives</atitle><jtitle>Biochemical engineering journal</jtitle><date>2006-05-01</date><risdate>2006</risdate><volume>30</volume><issue>1</issue><spage>26</spage><epage>32</epage><pages>26-32</pages><issn>1369-703X</issn><eissn>1873-295X</eissn><abstract>Two different monoactivated β-cyclodextrin derivatives, named mono-6-amino-6-deoxy-β-CD (CD1) and mono-6-(5-carboxypentane-1-carboxamidoyl)-6-deoxy-β-CD (CD2) were evaluated as modifying agents for
Bacillus badius phenylalanine dehydrogenase. The enzyme glycosidated with CD1 and CD2 contained about 18
mol and 15
mol oligosaccharide per mol of protein and retained 60% and 81% of the initial activity, respectively. The optimum temperature for the catalytic activity of phenylalanine dehydrogenase was increased in 10
°C after attaching the CDs residues. The enzyme thermostability profile was improved, and its resistance to thermal inactivation at different temperatures ranging from 45
°C to 60
°C was noticeably increased after glycosidation. The activation free energy of thermal inactivation was increased by 16.8
kJ/mol and 12.6
kJ/mol for the enzyme modified with CD1 and CD2, respectively. The influence of supramolecular host–guest associations on the improved thermotolerance showed by the modified enzyme forms was demonstrated by fluorescence spectroscopy and enzymatic measurements.</abstract><cop>Lausanne</cop><cop>Amsterdam</cop><cop>New York, NY</cop><pub>Elsevier B.V</pub><doi>10.1016/j.bej.2006.01.013</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1369-703X |
| ispartof | Biochemical engineering journal, 2006-05, Vol.30 (1), p.26-32 |
| issn | 1369-703X 1873-295X |
| language | eng |
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| source | ScienceDirect Journals |
| subjects | Amino acids Bacillus badius Biological and medical sciences Biotechnology Cyclodextrin Enzyme activity Enzyme technology Fundamental and applied biological sciences. Psychology Phenylalanine dehydrogenase Protein denaturation |
| title | Supramolecular-mediated thermostabilization of phenylalanine dehydrogenase modified with β-cyclodextrin derivatives |
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