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Enzymatic activity and thermal stability of PEG-α-chymotrypsin conjugates
α-Chymotrypsin was chemically modified with methoxypoly(ethylene glycol) (PEG) of different molecular weights (700, 2,000, and 5,000 Da) and the amount of polymer attached to the enzyme was varied systematically from 1 to 9 PEG molecules per enzyme molecule. Upon PEG conjugation, enzyme catalytic tu...
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| Published in: | Biotechnology letters 2009-06, Vol.31 (6), p.883-887 |
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| Main Authors: | , , , |
| Format: | Article |
| Language: | English |
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| cites | cdi_FETCH-LOGICAL-c470t-e02fe987e83f278a34a80dd7f096d138a92914f51d24db41bda89163a435d2fa3 |
| container_end_page | 887 |
| container_issue | 6 |
| container_start_page | 883 |
| container_title | Biotechnology letters |
| container_volume | 31 |
| creator | Rodríguez-Martínez, José A. Rivera-Rivera, Izarys Solá, Ricardo J. Griebenow, Kai |
| description | α-Chymotrypsin was chemically modified with methoxypoly(ethylene glycol) (PEG) of different molecular weights (700, 2,000, and 5,000 Da) and the amount of polymer attached to the enzyme was varied systematically from 1 to 9 PEG molecules per enzyme molecule. Upon PEG conjugation, enzyme catalytic turnover (
k
cat
) decreased by 50% and substrate affinity was lowered as evidenced by an increase in the
K
M
from 0.05 to 0.19 mM. These effects were dependent on the amount of PEG bound to the enzyme but were independent of the PEG size. In contrast, stabilization toward thermal inactivation depended on the PEG molecular weight with conjugates with the larger PEGs being more stable. |
| doi_str_mv | 10.1007/s10529-009-9947-y |
| format | article |
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k
cat
) decreased by 50% and substrate affinity was lowered as evidenced by an increase in the
K
M
from 0.05 to 0.19 mM. These effects were dependent on the amount of PEG bound to the enzyme but were independent of the PEG size. In contrast, stabilization toward thermal inactivation depended on the PEG molecular weight with conjugates with the larger PEGs being more stable.</description><identifier>ISSN: 0141-5492</identifier><identifier>EISSN: 1573-6776</identifier><identifier>DOI: 10.1007/s10529-009-9947-y</identifier><identifier>PMID: 19224136</identifier><identifier>CODEN: BILED3</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Animals ; Applied Microbiology ; Biochemistry ; Biological and medical sciences ; Biomedical and Life Sciences ; Biotechnology ; Cattle ; Chymotrypsin - chemistry ; Chymotrypsin - metabolism ; Enzyme Stability ; Fundamental and applied biological sciences. Psychology ; Kinetics ; Life Sciences ; Microbiology ; Molecular Weight ; Original Research Paper ; Polyethylene Glycols - chemistry ; Temperature</subject><ispartof>Biotechnology letters, 2009-06, Vol.31 (6), p.883-887</ispartof><rights>Springer Science+Business Media B.V. 2009</rights><rights>2009 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c470t-e02fe987e83f278a34a80dd7f096d138a92914f51d24db41bda89163a435d2fa3</citedby><cites>FETCH-LOGICAL-c470t-e02fe987e83f278a34a80dd7f096d138a92914f51d24db41bda89163a435d2fa3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,315,786,790,891,27957,27958</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21534301$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19224136$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rodríguez-Martínez, José A.</creatorcontrib><creatorcontrib>Rivera-Rivera, Izarys</creatorcontrib><creatorcontrib>Solá, Ricardo J.</creatorcontrib><creatorcontrib>Griebenow, Kai</creatorcontrib><title>Enzymatic activity and thermal stability of PEG-α-chymotrypsin conjugates</title><title>Biotechnology letters</title><addtitle>Biotechnol Lett</addtitle><addtitle>Biotechnol Lett</addtitle><description>α-Chymotrypsin was chemically modified with methoxypoly(ethylene glycol) (PEG) of different molecular weights (700, 2,000, and 5,000 Da) and the amount of polymer attached to the enzyme was varied systematically from 1 to 9 PEG molecules per enzyme molecule. Upon PEG conjugation, enzyme catalytic turnover (
k
cat
) decreased by 50% and substrate affinity was lowered as evidenced by an increase in the
K
M
from 0.05 to 0.19 mM. These effects were dependent on the amount of PEG bound to the enzyme but were independent of the PEG size. In contrast, stabilization toward thermal inactivation depended on the PEG molecular weight with conjugates with the larger PEGs being more stable.</description><subject>Animals</subject><subject>Applied Microbiology</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Cattle</subject><subject>Chymotrypsin - chemistry</subject><subject>Chymotrypsin - metabolism</subject><subject>Enzyme Stability</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>Microbiology</subject><subject>Molecular Weight</subject><subject>Original Research Paper</subject><subject>Polyethylene Glycols - chemistry</subject><subject>Temperature</subject><issn>0141-5492</issn><issn>1573-6776</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><recordid>eNp9kc-KFDEQxoMo7rj6AF6kL3qL5l93kosgy-yqLOhBz6EmSc9k6E6PSXqhfStfxGfaDDOsevFUUPWrr4rvQ-glJW8pIfJdpqRlGhOisdZC4uURWtFWctxJ2T1GK0IFxa3Q7AI9y3lPKiiJfIouqGZMUN6t0Od1_LmMUIJtwJZwF8rSQHRN2fk0wtDkApswHLtT33xd3-Dfv7DdLeNU0nLIITZ2ivt5C8Xn5-hJD0P2L871En2_Xn-7-ohvv9x8uvpwi62QpGBPWO-1kl7xnkkFXIAizsme6M5RrkAzTUXfUseE2wi6caA07TgI3jrWA79E70-6h3kzemd9LAkGc0hhhLSYCYL5dxLDzmynO8Mk1UrpKvDmLJCmH7PPxYwhWz8MEP00Z9NJJhQTpIL0BNo05Zx8_3CEEnNMwJwSMNVYc0zALHXn1d_f_dk4W16B12cAsoWhTxBtyA8coy0XnNDKsROX6yhufTL7aU6xOvuf6_fffqE5</recordid><startdate>20090601</startdate><enddate>20090601</enddate><creator>Rodríguez-Martínez, José A.</creator><creator>Rivera-Rivera, Izarys</creator><creator>Solá, Ricardo J.</creator><creator>Griebenow, Kai</creator><general>Springer Netherlands</general><general>Springer</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20090601</creationdate><title>Enzymatic activity and thermal stability of PEG-α-chymotrypsin conjugates</title><author>Rodríguez-Martínez, José A. ; Rivera-Rivera, Izarys ; Solá, Ricardo J. ; Griebenow, Kai</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c470t-e02fe987e83f278a34a80dd7f096d138a92914f51d24db41bda89163a435d2fa3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Animals</topic><topic>Applied Microbiology</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>Cattle</topic><topic>Chymotrypsin - chemistry</topic><topic>Chymotrypsin - metabolism</topic><topic>Enzyme Stability</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Kinetics</topic><topic>Life Sciences</topic><topic>Microbiology</topic><topic>Molecular Weight</topic><topic>Original Research Paper</topic><topic>Polyethylene Glycols - chemistry</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rodríguez-Martínez, José A.</creatorcontrib><creatorcontrib>Rivera-Rivera, Izarys</creatorcontrib><creatorcontrib>Solá, Ricardo J.</creatorcontrib><creatorcontrib>Griebenow, Kai</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biotechnology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rodríguez-Martínez, José A.</au><au>Rivera-Rivera, Izarys</au><au>Solá, Ricardo J.</au><au>Griebenow, Kai</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enzymatic activity and thermal stability of PEG-α-chymotrypsin conjugates</atitle><jtitle>Biotechnology letters</jtitle><stitle>Biotechnol Lett</stitle><addtitle>Biotechnol Lett</addtitle><date>2009-06-01</date><risdate>2009</risdate><volume>31</volume><issue>6</issue><spage>883</spage><epage>887</epage><pages>883-887</pages><issn>0141-5492</issn><eissn>1573-6776</eissn><coden>BILED3</coden><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>α-Chymotrypsin was chemically modified with methoxypoly(ethylene glycol) (PEG) of different molecular weights (700, 2,000, and 5,000 Da) and the amount of polymer attached to the enzyme was varied systematically from 1 to 9 PEG molecules per enzyme molecule. Upon PEG conjugation, enzyme catalytic turnover (
k
cat
) decreased by 50% and substrate affinity was lowered as evidenced by an increase in the
K
M
from 0.05 to 0.19 mM. These effects were dependent on the amount of PEG bound to the enzyme but were independent of the PEG size. In contrast, stabilization toward thermal inactivation depended on the PEG molecular weight with conjugates with the larger PEGs being more stable.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>19224136</pmid><doi>10.1007/s10529-009-9947-y</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | Biotechnology letters, 2009-06, Vol.31 (6), p.883-887 |
| issn | 0141-5492 1573-6776 |
| language | eng |
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| subjects | Animals Applied Microbiology Biochemistry Biological and medical sciences Biomedical and Life Sciences Biotechnology Cattle Chymotrypsin - chemistry Chymotrypsin - metabolism Enzyme Stability Fundamental and applied biological sciences. Psychology Kinetics Life Sciences Microbiology Molecular Weight Original Research Paper Polyethylene Glycols - chemistry Temperature |
| title | Enzymatic activity and thermal stability of PEG-α-chymotrypsin conjugates |
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