title: The effect of thermostabilising mutations on the pressure stability of Trichoderma reesei GH11 xylanase.
abstract: 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.
authors.affiliation: Department of Biotechnology and Chemical Technology, School of Chemical Technology, Aalto University, Aalto, Finland.
authors.forename: H
authors.initials: H
authors.lastname: Li
authors.forename: L
authors.initials: L
authors.lastname: Murtomäki
authors.forename: M
authors.initials: M
authors.lastname: Leisola
authors.forename: O
authors.initials: O
authors.lastname: Turunen
mesh_terms: D043364:Endo-1,4-beta Xylanases / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D007700:Kinetics; D009154:Mutation; D011487:Protein Conformation; D015202:Protein Engineering; D055550:Protein Stability; D017434:Protein Structure, Tertiary; D013696:Temperature; D013816:Thermodynamics; D014242:Trichoderma / Q000201:enzymology* / Q000235:genetics*
chemical_list: D043364:Endo-1,4-beta Xylanases