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Substitution of His260 residue alters the thermostability of Pseudoalteromonas carrageenovora arylsulfatase
- Source :
- Acta Oceanologica Sinica. 38:75-82
- Publication Year :
- 2019
- Publisher :
- Springer Science and Business Media LLC, 2019.
-
Abstract
- This study aimed to improve the thermostability of arylsulfatase from Pseudoalteromonas carrageenovora. A library of P. carrageenovora arylsulfatase mutants was constructed by introducing random mutagenesis using error-prone PCR. After screening, two mutants of H260L and D84A/H260L showed enhanced thermal stability than the wild-type predecessor (WT). Site-directed mutagenesis demonstrated that only amino acid residue at Position 260 plays an important role in the thermostability of P. carrageenovora arylsulfatase. Thermal inactivation analysis showed that the half-life (t1/2) values at 55°C for H260L, H260I, H260Q, H260F and H260R were 40.6, 48.4, 30.9, 29.1 and 34.5 min, respectively, while that of WT was 9.1 min. Structure modeling demonstrated that the additional hydrogen bonds and/or optimization of surface charge-charge interactions could be responsible for the increased thermostability imparted by H260L, H260I, H260Q, H260F and H260R.
- Subjects :
- 010504 meteorology & atmospheric sciences
biology
Hydrogen bond
Chemistry
Mutagenesis
Mutant
Aquatic Science
010502 geochemistry & geophysics
Oceanography
biology.organism_classification
01 natural sciences
Residue (chemistry)
Biochemistry
biology.protein
Amino acid residue
Arylsulfatase
Pseudoalteromonas carrageenovora
0105 earth and related environmental sciences
Thermostability
Subjects
Details
- ISSN :
- 18691099 and 0253505X
- Volume :
- 38
- Database :
- OpenAIRE
- Journal :
- Acta Oceanologica Sinica
- Accession number :
- edsair.doi...........b51680df575c923c966f62e02af18c7d
- Full Text :
- https://doi.org/10.1007/s13131-019-1356-z