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The effect of thermostabilising mutations on the pressure stability of Trichoderma reesei GH11 xylanase.
MedLine Citation:
PMID:  22942394     Owner:  NLM     Status:  Publisher    
We studied the pressure stability of disulphide bridge mutants of Trichoderma reesei XYNII at 500-5000 bar. The inactivation of XYNII and its mutants was strongest above 4000 bar. The pressure stability correlated with the thermostability order of the XYNII mutants, indicating that the stabilising mutations in protein regions important for thermostability also protect the enzyme at high pressure. In combination with high pressure, a mild heating had already inactivated the wild-type enzyme; the thermostabilising mutations largely counteracted this effect. At a low temperature, the mutations did not have any remarkable pressure stabilisation effect. Thus, thermal inactivation appeared to dominate over pressure inactivation at higher temperatures. Kinetic calculations indicated that pressure compressibility correlated with the thermostability of xylanase mutants.
H Li; L Murtomäki; M Leisola; O Turunen
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-8-31
Journal Detail:
Title:  Protein engineering, design & selection : PEDS     Volume:  -     ISSN:  1741-0134     ISO Abbreviation:  Protein Eng. Des. Sel.     Publication Date:  2012 Aug 
Date Detail:
Created Date:  2012-9-3     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101186484     Medline TA:  Protein Eng Des Sel     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Department of Biotechnology and Chemical Technology, School of Chemical Technology, Aalto University, PO Box 16100, FI-00076 Aalto, Finland.
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