Substitution of His260 residue alters the thermostability of Pseudoalteromonas carrageenovora arylsulfatase

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...

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Veröffentlicht in:	Acta oceanologica Sinica 2019-06, Vol.38 (6), p.75-82
Hauptverfasser:	Zhu, Yanbing, Yin, Xiaoqian, Liu, Han, Li, Hebin, Chen, Yanhong, Li, Lijun, Xiao, Anfeng, Ni, Hui
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino acids Arylsulfatase Climatology Cloning Construction contracts Deactivation DNA DNA polymerase E coli Earth and Environmental Science Earth Sciences Ecology Engineering Fluid Dynamics Environmental Chemistry Enzymes Evolution Food Hydrogen Hydrogen bonding Hydrogen bonds Inactivation Interactions Laboratories Marine & Freshwater Sciences Microorganisms Mutagenesis Mutants Nucleotide sequence Oceanography Optimization PCR Peptides Plasmids Pseudoalteromonas Random mutagenesis Residues Site-directed mutagenesis Surface charge Thermal cycling Thermal stability
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